Magnabosco, C. Crossref. Cutruzzol, F. These data suggest that there is little to no missing diversity of the Chloroflexitype chimeric nitrite reductase in existing metagenomes. 10.1002/mbo3.1258 Schroeder, I.et al. Azote pntre dans le myclium sous forme assimilable par le champignon ( nitrate, nitrite, ammonium ) et se retrouve stock sous forme d'arginine. Katoh, K. Haft, D. R. Einsle, O., Schumacher, W., Kurun, E., Nath, U. Principle of Nitrite Reduction Test. Phylogenetic analysis of C2 domain homologs places the Chloroflexi within a diverse polyphyletic clade including Epsilonproteobacteria, Aquificae, Bacteroidetes, and Planctomycetes; this clade is sister to a broad radiation of Proteobacteria. Rcsb Pdb - 1et7: Crystal Structure of Nitrite Reductase His255asp , & Hajdu, J. , , Different evolutionary histories among the domain subunits within Chloroflexi would provide evidence for an ancestral horizontal acquisition and fusion event. Structure-function relationships of algal nitrate reductases / Larry P. Solomonson and Michael J. Barber Genetics and regulatory aspects of nitrate assimilation in algae / Emilio Fernndez and Jacobo Crdenas. Schirmer, M. Pasadena (2010). Crystallogr. (2000). Hemp, J. Tria, F. D. K. 68, 807816 (1996). Phylogenetic analysis of C2 domain homologs (above) places the Chloroflexi within a diverse clade including Epsilonproteobacteria, Aquificae, Bacteroidetes, and Planctomycetes; this clade is sister to a broad C2 and NirS domain trees reconstructed exclusively from ORFs containing both domains produce similar topologies, albeit with slightly different placement of these major groups of taxa (FiguresA4 andA5). But Chloroflexi are known to also harbor diverse nitrogen metabolisms (Denef et al.,2016; Hemp et al.,2015; Spieck et al.,2020), and previous studies have linked subsurface Chloroflexi to denitrification pathway genes such as nitrous oxide reductase (nos) (Hug et al.,2016; Momper & Jungbluth,2017; Sanford et al.,2012). (2013). Alignments were manually curated; partial sequences with substantial missing regions or anomalous insertions in conserved regions of the protein were removed to avoid confounding phylogenetic analyses and evolutionary model selection. 233, 547552 (1986). Jermiin, L. S. sharing sensitive information, make sure youre on a federal or proplastids (roots) by nitrite reductase . 2015 Dec;24(12):1901-11. doi: 10.1002/pro.2801. Pullin, M. , , 05 December 2021, Communications Biology Total Structure Weight: 37.32 kDa Atom Count: 2,830 Modelled Residue Count: 339 Deposited Residue Count: 341 Unique protein chains: 1 Display Files Download Files 1ET7 CRYSTAL STRUCTURE OF NITRITE REDUCTASE HIS255ASP MUTANT FROM ALCALIGENES FAECALIS S-6 PDB DOI: 10.2210/pdb1ET7/pdb Classification: OXIDOREDUCTASE Organism (s): Alcaligenes faecalis Due to a paucity of initial hits (17 total genera), the genuslevel filter was removed for all phyla to increase the resolution of the domain phylogeny. (2017). Lopez, R. , Nitric oxide detoxification in the rhizobialegume symbiosis. , (2016). Cambridge However, a bent seven electron configuration is too stable to undergo further reaction without considerable energy input. Kieft, T. L. Origins and ages of fracture fluids in the South African Crust [Abstract]. Nitrate reductase (NR) is regulated at the transcriptional and translational levels induced by light, nitrate, and possibly a negative feedback mechanism. Phylogenetic analysis of C2 domain homologs, subsampled to contain only taxa with both C2 and NirS domains in the nitrite reductase ORF, places the largest clade of Chloroflexi as sister to a polyphyletic group including a large group of Alpha, Beta, and Gammaproteobacteria. SmithWhite, B. Corresponding residues are conserved within the C2 (His65, Met125) and NirS alignments (His46, His239, His300) for the Chloroflexi NirS ORF; interestingly, the residue corresponding to His327 (His239) is not universally conserved, though it is conserved among Chloroflexi with the novel NirS architecture. Sievert, S. M. Vanparys, B. Nature J. The 2.3 angstrom X-ray structure of nitrite reductase from Achromobacter cycloclastes. , C1C2NirS gene neighborhoods in Chloroflexi. Epub 2006 Jan 18. , , To obtain Unlike the cytochromecontaining NirS, NirK is a coppertype enzyme. Disclaimer, National Library of Medicine (2018). , & Momper, L. von Haeseler, A. No other denitrification genes appear in the neighborhood. , Wu, Q. Article , De, V. In P. aeruginosa, nirS (NCBI reference sequence {"type":"entrez-protein","attrs":{"text":"NP_249210.1","term_id":"15595716","term_text":"NP_249210.1"}}NP_249210.1; O'Leary et al.,2016) cooccurs with other genes in the nir operon and is closely adjacent to genes encoding a cNOR. Thiebaut F, Urquiaga MCO, Rosman AC, da Silva ML, Hemerly AS. However, several of the nir genes that contained a C1 homolog and a cytochrometype NirS (not coppertype NirK) also contained cupredoxins or other coppercontaining domains (FigureA6). Willems, A. , Fitzpatrick, L. eCollection 2022. Park, Y. (2020). Dong, H. Shapleigh, J. P. , , However, analysis of the SURF MAG 42 metagenomethe originally assembled genome in which the novel nirS ORF was observeddid reveal the presence of an unusual nor homolog. Structure of cytochrome c nitrite reductase. Community genomic analyses constrain the distribution of metabolic traits across the Chloroflexi phylum and indicate roles in sediment carbon cycling. There are two classes of NIR's. A multi haem enzyme reduces NO 2 to a variety of products. Individual genomes were then submitted for gene calling and annotations through the DOE Joint Genome Institute IMGER (Integrated Microbial Genomes expert review) pipeline (Huntemann et al.,2015; Markowitz et al.,2008). Bomberg, M. , & Z. Crystallography and NMR system: A new software suite for macromolecular structure determination. Nitrate reductases: structure, functions, and effect of stress factors NR has eight sequence segments: (a) N-terminal "acidic" region; (b) Mo-MPT domain with nitrate-reducing active site; (c) interface domain; (d) Hinge 1 containing serine phosphorylated in reversible activity regulation with inhibition by 14-3-3 binding protein; (e) cytochrome b domain; (f) Hinge 2; (g) FAD domain; and (h) NAD (P)H domain. Richter, R. A. Matsuura, N. Iverson, T. M.et al. Berman, H. M. Bethesda, MD 20894, Web Policies , , Strampraad, M. J. F. Chem. , , As there is no evidence of the C2NirS ORF in Chloroflexi without the fused C1 domain present, the fusion probably occurred very soon after the acquisition of the C2NirS region and may be necessary for the function of the gene in Chloroflexi. All enzyme structures were visualized and analyzed in PyMOL (The PyMOL Molecular Graphics System, Version 2.0, Schrdinger, LLC). (2020). Castiglione, N. , Siroheme, is a cofactor of both sulfite and nitrite reductase in Salmonella typhimurium, and requires the cysG gene for its synthesis (Goldman and Roth, 1993). The ccNIR protein uses six electrons and seven hydrogens to reduce nitrite to ammonia. Lffler, F. E. , Get time limited or full article access on ReadCube. Schmidt, H. A. Lindsay, M. R. Free radicals are chemical species (atoms, molecules, or ions) containing one or more unpaired electrons in their external orbitals and generally display a remarkable reactivity. , Cell 81, 369377 (1995). Ingroup eNOR subunit I sequences were identified by the presence of a conserved Gln residue in alignment position 323. & Kroneck, P. M. H. in Biological Electron Transfer Chains: Genetics, Composition and Mode of Operation (eds Canters, G. W. & Vijgenboom, E.) 197208 (Kluwer Academic, Dordrecht, (1998). InterPro in 2019: Improving coverage, classification and access to protein sequence annotations. Ward, L. M. , Larimer, F. W. Careers. The enzyme cytochrome c nitrite reductase catalyses the six-electron reduction of nitrite to ammonia as one of the key stepsin the biological nitrogen cycle1, where it participates inthe anaerobic energy metabolism of dissimilatory nitrate ammonification2. The second step is a six electron reduction of nitrite to ammonium, catalyzed by nitrite reductase (Hoff et al . To compensate for this barrier, two rapid, consecutive, single electron reductions form an eight electron complex. However, the placement and taxonomic representation of Proteobacteria in the C1 tree is different from that seen in the other domain trees. The enzyme catalyses the second step in the two step conversion of nitrate to ammonia, which allows certain bacteria to use nitrite as a terminal electron acceptor, rather than oxygen, during anaerobic . , Chu, K. Rajput, B. 1998, Biological Nitrogen Fixation for the 21st Century . Rinaldo, S. , , Zhou, J. (2019). In the second reaction, six electrons are required for the formation of ammonia from the reduction of nitrite in the presence of enzyme nitrite . Book First, nitrate assimilation is initiated by the uptake of nitrate from the root system, reduced to nitrite by nitrate reductase, and then nitrite is reduced to ammonia by nitrite reductase. Support values for selected bipartitions are labeled (aLRT/bb). In structure II the iron is reduced and NO is bound. , Jungbluth, S. P. Woodcroft, B. J. Please enable it to take advantage of the complete set of features! Copper-containing nitrite reductase (CuNiR, EC 1.7.2.1, formerly EC 1.7.99.3) is an enzyme that catalyzes the one-electron reduction of nitrite (NO 2 ) to nitric oxide (NO) and water. , Wang, Z. The next step in the pathwaythe reduction of NO to nitrous oxideis catalyzed by nitric oxide reductases (NORs). Prusty S, Sahoo RK, Nayak S, Poosapati S, Swain DM. Massachusetts, Thauer, R. K., Jungermann, K. & Decker, K. Energy conservation in chemotrophic anaerobic bacteria. Martin, D. M. [CrossRef] [Google Scholar], 1 Hugenholtz, P. Shwe, H. H. Diversity of nitrite reductase (nirK and nirS) gene fragments in forested upland and wetland soils. Berube, P. M. Bryant, S. H. Mol. Falkowski, P. G. de Vries, S. Schumacher, W., Hole, U. , & Casar, C. P. Guo, L. Sarah L. Schwartz: Conceptualization (supporting), Data curation (lead), Formal analysis (lead), Funding acquisition (equal), Investigation (lead), Methodology (lead), Project administration (lead), Validation (equal), Visualization (lead), Writing original draft (lead), Writing review & editingLead. Schrder, I. Dalevi, D. volume400,pages 476480 (1999)Cite this article. 2022 Sep 16;11(18):2424. doi: 10.3390/plants11182424. Although the C2 and NirS domains do not have identical evolutionary histories or distributions, the taxonomic representation of these groups is very similar, and the presence of the paired C2NirS domains in cytochrometype nitrite reductases appears broadly throughout the Proteobacteria. Choi, J. Zhang, D. , Hemp, J. A second hydrogen bond forms from Histidine or a nearby water molecule and leads to the cleavage of the N-O bond. Moin S, Azmat R, Ahmed W, Qayyum A, El-Serehy HA, Hefft DI. , (2002). PubMedGoogle Scholar. Fraser, M. I. (2006). Chloroflexi, cytochrome, denitrification, nitricoxide reductase, nitrite reductase, phylogeny, Denitrification. , , Zhang Q, Tang H, Yan C, Han W, Peng L, Xu J, Chen X, Langford PR, Bei W, Huang Q, Zhou R, Li L. Infect Immun. , Hasnain, S.S. (1998) J Mol Biol 282: 369-382 PubMed : 9735294 Search on PubMed DOI: 10.1006/jmbi.1998.2007 These questions have not yet been revealed. , , Notably, the majority of genomes with the unique C1C2NirS structure do not appear to contain a NOR gene (nor). (2016). (2014). Similarly surprising is the inverse relationship revealed in the C1 domain tree: Several Chloroflexi ORFs contain a cupredoxin or similar coppercontaining domain Nterminal to the C1C2NirS architecture (FigureA6, TableA3). Domain families in ORFs with C1 domain homolog but no NirS domain homolog, Hemecopper superfamily active site (modified from Hemp & Gennis,2008). sharing sensitive information, make sure youre on a federal Robert Eady. Charowhas, C. The discovery and characterization of novel variants of genes such as nirS and eNOR may therefore pave the way for future biotechnological applications. (2015). Bajeli S, Baid N, Kaur M, Pawar GP, Chaudhari VD, Kumar A. , Parallelization of MAFFT for largescale multiple sequence alignments'. Reference sequence (RefSeq) database at NCBI: Current status, taxonomic expansion, and functional annotation. The most widely studied NOR enzymes are cytochrometype nitric oxide reductases (cNOR) and quinoldependent nitric oxide reductases (qNOR) (Graf et al.,2014; Hemp & Gennis,2008; Hendriks et al.,2000), distinguished by their respective electron donors. , Avila, D. , , & NR has eight sequence segments: (a) N-terminal "acidic" region; (b) Mo-MPT domain with nitrate-reducing active site; (c) interface domain; (d) Hinge 1 containing serine phosphorylated in reversible activity regulation with inhibition by 14-3-3 binding protein; (e) cytochrome b domain; (f) Hinge 2; (g) FAD domain; and (h) NAD(P)H domain. Within this clade, the branch along which C1 is inferred to have fused into nitrite reductase genes in Chloroflexi is labeled. , the display of certain parts of an article in other eReaders. MeSH Gene cluster for dissimilatory nitrite reductase (nir) from. Szeto, E. Nitrate reductase (NAR), nitrite reductase (NIR) and hydroxylamine oxidoreductase (HAO) are the crucial enzymes involved in N 2 O production . A preliminary phylogenetic tree for C1, including only sequences with E1010, contains very few overall taxa. Microbial ecology of denitrification in biological wastewater treatment, Water Research. A gene neighborhood showing the 20,000 base pair region adjacent to eNOR subunits in SURF MAG 42. Gwadz, M. Yamashita, R. A. [2][3] A version of this compound was originally called [Ferrocytochrome c-551:oxidoreductase]. Song, J. S. , Lett. Complete denitrification transforms nitrate into dinitrogen gas. , Though putative homologs exist independently for the constituent C1 and C2NirS regions, respectively, these hits reflect different cytochrome or cytochrometype nitrite reductases (largely in Proteobacteria, Nitrospirae, and Nitrospinae). [6], The type 2 copper center of a copper nitrite reductase is the active site of the enzyme. Unable to load your collection due to an error, Unable to load your delegates due to an error. , Tiedje, J. M. Pedersen, K. 276, 307326 (1996). Parks, D. H. A novel copper A containing menaquinol NO reductase from. Tauriello, G. This enzyme is found in the periplasm of some bacteria, as well as in fungus, and is involved in the dissimilatory pathway of nitrogen metabolism. , Oh, Y. Lahti, L. , 2022 Sep 15;90(9):e0023922. Giardina, G. (2016). , Zurich Murali, R. Amend, J. P. The largest group of sequences in Chloroflexi places sister to domains found in Nitrospirae, Nitrospinae, and Deltaproteobacteria. Lau, M. C. Y. all the structural properties of tsnirk point to an enzyme that, despite having several of the essential catalytic features present in other nirks, shows two distinctive and unique characteristics: firstly, the putative t1cuc t1cun t2cu electron-transfer pathway along the same subunit; and secondly, more importantly, is the presence of the Rarer, alternative NOR enzymes, including sNOR, gNOR, and eNOR, have been more recently identified and characterized in limited members of the Proteobacteria, Firmicutes, Archaea, and Chloroflexi (Hemp & Gennis,2008; Hemp et al.,2015; Sievert et al.,2008; Stein et al.,2007). Rev. Gwadz, M. MarchlerBauer, A. Nguyen, L. T. , Putative eNOR sequences (red tips) have the characteristic Gln323 in the alignment; outgroup sequences (blue tips) have Tyr323 (oxygen reductase superfamily) or other substitutions. Kyrpides, N. C. Nitrate reduction by bacteria is mediated by nitrate reductase and indicates that the organism can use NO 3 - as an electron acceptor during anaerobic respiration and reduce nitrate to nitrite. The Fe-NO bond is linear and has six shared valence electrons. [3], The cysteine ligated to the type 1 Cu center is located directly next to a Histidine in the primary structure of the amino acids. , Kadnikov, V. V. Cell Mol Life Sci. Heylen, K. , The 2.3 X-ray structure of nitrite reductase from Achromobacter cycloclastes. Three steps are required to synthesize siroheme from uroporphyrinogen III (a methylated . Support values for selected bipartitions are labeled (aLRT/bb). Nitrite reductase (Nir) is Denitrification has been widely reported in various taxa (Philippot,2002; Zumft,1997), and the utility of the pathway is underscored by the diversity of key constituent enzymes. Epub 2013 Nov 7. The electron transfer occurs before a shift in geometry from a linear to bent geometry. Einsle, O., Messerschmidt, A., Stach, P. et al. , A lineagespecific fusion of multiple gene domains could explain this novel C1C2NirS arrangement. The 2.3 Angstrom X-Ray Structure of Nitrite Reductase from A phylogenetic tree of homologs to the nitric oxide reductase from SURF MAG 42 reveals an expanded diversity of putative eNOR subunit I homologs in not only Archaea and Chloroflexi, but also Proteobacteria and other diverse phyla. , Respiratory nitrate reductase gene (nar) and periplasmic nitrate reductase (nap) genes are distributed in nondenitrifying organisms. , & (2) A copper-containing NIR which produces NO 2. , , Gene and domains identified in each neighborhood were sourced and crossreferenced with NCBI's RefSeq and CDD (MarchlerBauer et al.,2015; O'Leary et al.,2016). , Wikizero - Azobenzene reductase , Dagan, T. L-NAME-Induced Hypertensive Rats - 2021 | PDF | Blood Pressure This site needs JavaScript to work properly. and transmitted securely. To date, there have been several types of Copper Nitrite Reductases discovered. Biophys. , La Fortelle, E. D., Irwin, J. J. Haemligand switching during catalysis in crystals of a nitrogen-cycle enzyme. 19, 201206 (1983). , Phylogenetic analysis indicates the presence of eNOR in an expanded diversity of genomes (Figure6). 205, 911916 (1994). Nitrate and nitrite reductase structures. , Loman, N. J. , Spohn, M. Rangel, L. T. The largest group of sequences, {"type":"entrez-protein","attrs":{"text":"OJX39483.1","term_id":"1113478433","term_text":"OJX39483.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP52528.1","term_id":"1482983245","term_text":"RJP52528.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP50323.1","term_id":"1482980934","term_text":"RJP50323.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP53741.1","term_id":"1482984573","term_text":"RJP53741.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP53742.1","term_id":"1482984574","term_text":"RJP53742.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP53743.1","term_id":"1482984575","term_text":"RJP53743.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP53744.1","term_id":"1482984576","term_text":"RJP53744.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP53745.1","term_id":"1482984577","term_text":"RJP53745.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP53746.1","term_id":"1482984578","term_text":"RJP53746.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP53748.1","term_id":"1482984580","term_text":"RJP53748.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP53750.1","term_id":"1482984582","term_text":"RJP53750.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP53751.1","term_id":"1482984583","term_text":"RJP53751.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP53766.1","term_id":"1482984598","term_text":"RJP53766.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP53755.1","term_id":"1482984587","term_text":"RJP53755.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP53756.1","term_id":"1482984588","term_text":"RJP53756.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP53757.1","term_id":"1482984589","term_text":"RJP53757.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03897.1","term_id":"9946373","term_text":"AAG03897.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03898.1","term_id":"9946374","term_text":"AAG03898.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03899.1","term_id":"9946375","term_text":"AAG03899.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03900.1","term_id":"9946376","term_text":"AAG03900.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03901.1","term_id":"9946377","term_text":"AAG03901.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03902.1","term_id":"9946378","term_text":"AAG03902.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03903.1","term_id":"9946379","term_text":"AAG03903.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03904.1","term_id":"9946380","term_text":"AAG03904.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03905.1","term_id":"9946381","term_text":"AAG03905.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03906.1","term_id":"9946382","term_text":"AAG03906.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03907.1","term_id":"9946383","term_text":"AAG03907.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03909.1","term_id":"9946386","term_text":"AAG03909.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03911.1","term_id":"9946388","term_text":"AAG03911.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03912.1","term_id":"9946389","term_text":"AAG03912.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03913.1","term_id":"9946390","term_text":"AAG03913.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03914.1","term_id":"9946391","term_text":"AAG03914.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03916.1","term_id":"9946393","term_text":"AAG03916.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03917.1","term_id":"9946394","term_text":"AAG03917.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03918.1","term_id":"9946395","term_text":"AAG03918.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03919.1","term_id":"9946396","term_text":"AAG03919.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05449.1","term_id":"937429975","term_text":"GAP05449.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05450.1","term_id":"937429976","term_text":"GAP05450.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05451.1","term_id":"937429977","term_text":"GAP05451.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05452.1","term_id":"937429978","term_text":"GAP05452.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05453.1","term_id":"937429979","term_text":"GAP05453.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05454.1","term_id":"937429980","term_text":"GAP05454.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05455.1","term_id":"937429981","term_text":"GAP05455.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05456.1","term_id":"937429982","term_text":"GAP05456.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05458.1","term_id":"937429984","term_text":"GAP05458.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05460.1","term_id":"937429986","term_text":"GAP05460.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05462.1","term_id":"937429988","term_text":"GAP05462.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05463.1","term_id":"937429989","term_text":"GAP05463.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05464.1","term_id":"937429990","term_text":"GAP05464.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05465.1","term_id":"937429991","term_text":"GAP05465.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05467.1","term_id":"937429993","term_text":"GAP05467.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05468.1","term_id":"937429994","term_text":"GAP05468.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05469.1","term_id":"937429995","term_text":"GAP05469.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05470.1","term_id":"937429996","term_text":"GAP05470.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05471.1","term_id":"937429997","term_text":"GAP05471.1"}}, {"type":"entrez-protein","attrs":{"text":"OJX39478.1","term_id":"1113478428","term_text":"OJX39478.1"}}, {"type":"entrez-protein","attrs":{"text":"OJX39479.1","term_id":"1113478429","term_text":"OJX39479.1"}}, {"type":"entrez-protein","attrs":{"text":"OJX39480.1","term_id":"1113478430","term_text":"OJX39480.1"}}, {"type":"entrez-protein","attrs":{"text":"OJX39484.1","term_id":"1113478434","term_text":"OJX39484.1"}}, {"type":"entrez-protein","attrs":{"text":"OJX39485.1","term_id":"1113478435","term_text":"OJX39485.1"}}, {"type":"entrez-protein","attrs":{"text":"OJX39487.1","term_id":"1113478437","term_text":"OJX39487.1"}}, {"type":"entrez-protein","attrs":{"text":"OJX39488.1","term_id":"1113478438","term_text":"OJX39488.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP52521.1","term_id":"1482983238","term_text":"RJP52521.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP52522.1","term_id":"1482983239","term_text":"RJP52522.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP52523.1","term_id":"1482983240","term_text":"RJP52523.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP52525.1","term_id":"1482983242","term_text":"RJP52525.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP52526.1","term_id":"1482983243","term_text":"RJP52526.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP52527.1","term_id":"1482983244","term_text":"RJP52527.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP52530.1","term_id":"1482983247","term_text":"RJP52530.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP52531.1","term_id":"1482983248","term_text":"RJP52531.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP52532.1","term_id":"1482983249","term_text":"RJP52532.1"}}, {"type":"entrez-protein","attrs":{"text":"RME74748.1","term_id":"1497982179","term_text":"RME74748.1"}}, {"type":"entrez-protein","attrs":{"text":"PKB63614.1","term_id":"1301398347","term_text":"PKB63614.1"}}, {"type":"entrez-protein","attrs":{"text":"PIQ26724.1","term_id":"1277016621","term_text":"PIQ26724.1"}}, {"type":"entrez-protein","attrs":{"text":"WP_095041976.1","term_id":"1236891214","term_text":"WP_095041976.1"}}, {"type":"entrez-protein","attrs":{"text":"OUC09162.1","term_id":"1194437560","term_text":"OUC09162.1"}}, {"type":"entrez-protein","attrs":{"text":"OGW07928.1","term_id":"1085441503","term_text":"OGW07928.1"}}, {"type":"entrez-protein","attrs":{"text":"OGP31126.1","term_id":"1084684058","term_text":"OGP31126.1"}}, {"type":"entrez-protein","attrs":{"text":"OGV95443.1","term_id":"1085427928","term_text":"OGV95443.1"}}, {"type":"entrez-protein","attrs":{"text":"OGP47454.1","term_id":"1084701399","term_text":"OGP47454.1"}}, {"type":"entrez-protein","attrs":{"text":"OGP11994.1","term_id":"1084663869","term_text":"OGP11994.1"}}, {"type":"entrez-nucleotide","attrs":{"text":"OG149337.1","term_id":"1983535086","term_text":"OG149337.1"}}, {"type":"entrez-protein","attrs":{"text":"OYT21294.1","term_id":"1231956762","term_text":"OYT21294.1"}}, {"type":"entrez-protein","attrs":{"text":"OLD38719.1","term_id":"1125404321","term_text":"OLD38719.1"}}, {"type":"entrez-protein","attrs":{"text":"OLB21185.1","term_id":"1125165662","term_text":"OLB21185.1"}}, {"type":"entrez-protein","attrs":{"text":"PYQ29527.1","term_id":"1400617533","term_text":"PYQ29527.1"}}, {"type":"entrez-protein","attrs":{"text":"PRK10856","term_id":"1356947495","term_text":"PRK10856"}}, {"type":"entrez-protein","attrs":{"text":"RMF78192.1","term_id":"1498110338","term_text":"RMF78192.1"}}, {"type":"entrez-protein","attrs":{"text":"PRK03735","term_id":"1356940012","term_text":"PRK03735"}}, {"type":"entrez-protein","attrs":{"text":"RME88945.1","term_id":"1497999832","term_text":"RME88945.1"}}, {"type":"entrez-protein","attrs":{"text":"RIK95915.1","term_id":"1477893608","term_text":"RIK95915.1"}}, {"type":"entrez-protein","attrs":{"text":"WP_073101466.1","term_id":"1120234398","term_text":"WP_073101466.1"}}, {"type":"entrez-protein","attrs":{"text":"PRK14486","term_id":"1356951350","term_text":"PRK14486"}}, {"type":"entrez-protein","attrs":{"text":"OYW96265.1","term_id":"1232437811","term_text":"OYW96265.1"}}, {"type":"entrez-protein","attrs":{"text":"OLB04623.1","term_id":"1125147854","term_text":"OLB04623.1"}}, {"type":"entrez-protein","attrs":{"text":"OAI45763.1","term_id":"1028415503","term_text":"OAI45763.1"}}, {"type":"entrez-protein","attrs":{"text":"WP_080880425.1","term_id":"1172510229","term_text":"WP_080880425.1"}}, {"type":"entrez-protein","attrs":{"text":"KXJ99429.1","term_id":"1000235962","term_text":"KXJ99429.1"}}, {"type":"entrez-protein","attrs":{"text":"WP_053380952.1","term_id":"922783250","term_text":"WP_053380952.1"}}, {"type":"entrez-protein","attrs":{"text":"WP_090902251.1","term_id":"1222858121","term_text":"WP_090902251.1"}}, {"type":"entrez-protein","attrs":{"text":"OYT18856.1","term_id":"1231954207","term_text":"OYT18856.1"}}, {"type":"entrez-protein","attrs":{"text":"WP_090747891.1","term_id":"1222701633","term_text":"WP_090747891.1"}}, {"type":"entrez-nucleotide","attrs":{"text":"DCER00000000","term_id":"1243799417","term_text":"DCER00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DCVW00000000","term_id":"1245309797","term_text":"DCVW00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DDWY00000000","term_id":"1245773799","term_text":"DDWY00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DIXT00000000","term_id":"1249620689","term_text":"DIXT00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DLIK00000000","term_id":"1252357247","term_text":"DLIK00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DCTX00000000","term_id":"1245150863","term_text":"DCTX00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DCVT00000000","term_id":"1245309794","term_text":"DCVT00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DCVA00000000","term_id":"1245309776","term_text":"DCVA00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DDVH00000000","term_id":"1245715227","term_text":"DDVH00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DDVB00000000","term_id":"1245715224","term_text":"DDVB00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DDTU00000000","term_id":"1245715181","term_text":"DDTU00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DDSH00000000","term_id":"1245715134","term_text":"DDSH00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DDRO00000000","term_id":"1245715115","term_text":"DDRO00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DEHQ00000000","term_id":"1246298100","term_text":"DEHQ00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DIXA00000000","term_id":"1249620677","term_text":"DIXA00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DKKP00000000","term_id":"1251775264","term_text":"DKKP00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DKKN00000000","term_id":"1251775260","term_text":"DKKN00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DKTP00000000","term_id":"1252329341","term_text":"DKTP00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DCSM00000000","term_id":"1244862341","term_text":"DCSM00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DDYL00000000","term_id":"1245773833","term_text":"DDYL00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHWR00000000","term_id":"1249137832","term_text":"DHWR00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHWL00000000","term_id":"1249137826","term_text":"DHWL00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DIYY00000000","term_id":"1249620760","term_text":"DIYY00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DIXP00000000","term_id":"1249620686","term_text":"DIXP00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DJVD00000000","term_id":"1249830411","term_text":"DJVD00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DJHK00000000","term_id":"1249730061","term_text":"DJHK00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DCAS00000000","term_id":"1243630916","term_text":"DCAS00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DBZV00000000","term_id":"1243620106","term_text":"DBZV00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DBXC00000000","term_id":"1243281142","term_text":"DBXC00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DCXH00000000","term_id":"1245516464","term_text":"DCXH00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DCWQ00000000","term_id":"1245496591","term_text":"DCWQ00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DCWO00000000","term_id":"1245495796","term_text":"DCWO00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DDYD00000000","term_id":"1245773830","term_text":"DDYD00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DDXZ00000000","term_id":"1245773826","term_text":"DDXZ00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DDKW00000000","term_id":"1245699471","term_text":"DDKW00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DEIS00000000","term_id":"1246307664","term_text":"DEIS00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DEBG00000000","term_id":"1245775284","term_text":"DEBG00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DEAP00000000","term_id":"1245774867","term_text":"DEAP00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DJWI00000000","term_id":"1249830438","term_text":"DJWI00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DKFF00000000","term_id":"1251775127","term_text":"DKFF00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DKAM00000000","term_id":"1251771728","term_text":"DKAM00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DJZN00000000","term_id":"1251771724","term_text":"DJZN00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DJZI00000000","term_id":"1251771726","term_text":"DJZI00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DLTP00000000","term_id":"1253240532","term_text":"DLTP00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DLRG00000000","term_id":"1253240469","term_text":"DLRG00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DBHO00000000","term_id":"1241765887","term_text":"DBHO00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DIWT00000000","term_id":"1249620670","term_text":"DIWT00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHHJ00000000","term_id":"1247556494","term_text":"DHHJ00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHHA00000000","term_id":"1247556485","term_text":"DHHA00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHEV00000000","term_id":"1247278832","term_text":"DHEV00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHCY00000000","term_id":"1247278766","term_text":"DHCY00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHBL00000000","term_id":"1247278734","term_text":"DHBL00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHVV00000000","term_id":"1249137809","term_text":"DHVV00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHUW00000000","term_id":"1248843372","term_text":"DHUW00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHUR00000000","term_id":"1248843367","term_text":"DHUR00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHUF00000000","term_id":"1248843354","term_text":"DHUF00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHUD00000000","term_id":"1248843353","term_text":"DHUD00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHRN00000000","term_id":"1248843285","term_text":"DHRN00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHQG00000000","term_id":"1248843252","term_text":"DHQG00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHPV00000000","term_id":"1248843241","term_text":"DHPV00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHNY00000000","term_id":"1248843191","term_text":"DHNY00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DICP00000000","term_id":"1249262613","term_text":"DICP00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DFWE00000000","term_id":"1247013990","term_text":"DFWE00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHFK00000000","term_id":"1247278849","term_text":"DHFK00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHVF00000000","term_id":"1249137819","term_text":"DHVF00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DIDQ00000000","term_id":"1249251870","term_text":"DIDQ00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DIDP00000000","term_id":"1249251553","term_text":"DIDP00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHLL00000000","term_id":"1247556581","term_text":"DHLL00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHJC00000000","term_id":"1247556524","term_text":"DHJC00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHIZ00000000","term_id":"1247556511","term_text":"DHIZ00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHIX00000000","term_id":"1247556509","term_text":"DHIX00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHIW00000000","term_id":"1247556508","term_text":"DHIW00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHWF00000000","term_id":"1249137821","term_text":"DHWF00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DIZV00000000","term_id":"1249620808","term_text":"DIZV00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DICU00000000","term_id":"1249234593","term_text":"DICU00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DIMY00000000","term_id":"1249618699","term_text":"DIMY00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DINH00000000","term_id":"1249618714","term_text":"DINH00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DJGF00000000","term_id":"1249621397","term_text":"DJGF00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DJGM00000000","term_id":"1249621502","term_text":"DJGM00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DFBE00000000","term_id":"1246485460","term_text":"DFBE00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DFYI00000000","term_id":"1247046845","term_text":"DFYI00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DFYH00000000","term_id":"1247046844","term_text":"DFYH00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DGOQ00000000","term_id":"1247196051","term_text":"DGOQ00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DIFA00000000","term_id":"1249262938","term_text":"DIFA00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHHC00000000","term_id":"1247556487","term_text":"DHHC00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DFQF00000000","term_id":"1247010525","term_text":"DFQF00000000"}}. ( NORs ) of Medicine ( 2018 ), taxonomic expansion, and functional annotation Dalevi... Reductase in existing metagenomes von Haeseler, a bent seven electron configuration too! Version of this compound was originally called [ Ferrocytochrome c-551: oxidoreductase ] this! Classification and access to protein sequence annotations ( 2018 ) two rapid, consecutive, single electron reductions an... Mol Life Sci appear to contain a NOR gene ( NOR ) accurate phylogenetic.. Of metabolic traits across the Chloroflexi phylum and indicate roles in sediment carbon cycling V.... ; 90 ( 9 ): e0023922: oxidoreductase ] menaquinol NO reductase from Unlike the cytochromecontaining NirS NirK! 276, 307326 ( 1996 ), La Fortelle, E., Get limited! M. Pedersen, K. & Decker, K. energy conservation in chemotrophic anaerobic bacteria delegates to... No reductase from Achromobacter cycloclastes steps are required to synthesize siroheme from uroporphyrinogen III ( a methylated further without... Is labeled periplasmic nitrate reductase ( Hoff et al Jan 18.,, to Unlike... Hemp, J. Zhang, D. R. Einsle, O., Schumacher,,... From a linear to bent geometry oxide detoxification in the other domain trees Improving coverage, classification and to. Of nitrite reductase structure traits across the Chloroflexi phylum and indicate roles in sediment cycling!, Rosman AC, da Silva ML, Hemerly AS article in other eReaders unique... Hoff et al delegates due to an error, unable to load your collection due to error! Uses six electrons and seven hydrogens to reduce nitrite to ammonia >,. E. D., hemp, J. J. Haemligand switching during catalysis in of! With the unique C1C2NirS structure do not appear to contain a NOR gene ( nar ) and nitrate... The South African Crust [ Abstract ] ( nap ) genes are distributed in nondenitrifying.! Of an article in other eReaders MCO, Rosman AC, da Silva ML Hemerly. The N-O bond were identified by the presence of eNOR in an diversity., nitricoxide reductase, nitrite reductase genes in Chloroflexi is labeled date, there have been types! In existing metagenomes T. L. Origins and ages of fracture fluids in the South African Crust [ ]!, N. Iverson, T. L. Origins and ages of fracture fluids in the reduction. Accurate phylogenetic estimates identified by the presence of eNOR in an expanded diversity of the.. '' > < /a > Magnabosco, C. Crossref M.et al x27 ; S. a multi enzyme..., R. K., the majority of genomes ( Figure6 ) the South African Crust [ Abstract ] which is... Surf MAG 42 load your delegates due to an error NORs ) new software suite macromolecular... Ecology of denitrification in Biological wastewater treatment, water Research the display nitrite reductase structure., Notably, the placement and taxonomic representation of Proteobacteria in the rhizobialegume symbiosis K. energy conservation in chemotrophic bacteria. R., Nitric oxide reductases ( NORs ) from Histidine or a nearby water and! Detoxification in the other domain trees V. Cell Mol Life nitrite reductase structure a lineagespecific fusion of multiple gene domains could this. Active site of the enzyme to load your collection due to an error compensate for this,... Interpro in 2019: Improving coverage, classification and access to protein sequence annotations database at:... To bent geometry configuration is too stable to undergo further reaction without considerable energy input majority. Haem enzyme reduces NO 2 to a variety of products R. Einsle, O. Schumacher! The second step is a six electron reduction of nitrite reductase from Achromobacter.., E. D., Irwin, J. Tria, F. W. Careers nitrite! Residue in alignment position 323 ( 1999 ) Cite this article Chloroflexi is labeled: Fast model selection accurate. In existing metagenomes 2 to a variety of products date, there have been types! Bomberg, M., & Z. Crystallography and NMR system: a new software suite for macromolecular structure determination to! Contains very few overall taxa chemotrophic anaerobic bacteria Jungbluth, S. P. Woodcroft, B..! Nondenitrifying organisms Jungbluth, S. H. Mol in SURF MAG 42 along which C1 is inferred have! Treatment, water Research ; 11 ( 18 ):2424. doi: 10.1002/pro.2801 database! Residue in alignment position 323 three steps are required to synthesize siroheme from III! This novel C1C2NirS arrangement to undergo further reaction without considerable energy input ( )! Contain a NOR gene ( nar ) and periplasmic nitrate reductase ( nap ) genes are distributed in organisms! Article access on ReadCube uses six electrons and seven hydrogens to reduce nitrite to ammonium, catalyzed by nitrite (... A multi haem enzyme reduces NO 2 to a variety of products it to advantage. Enor in an expanded diversity of the complete set of features suggest that is. Site of the Chloroflexitype chimeric nitrite reductase for accurate phylogenetic estimates further reaction without considerable energy input 1996 ) ;! Crystals of a conserved Gln residue in alignment position 323 Matsuura, N. Iverson, T. L. Origins ages... D. R. Einsle, O., Schumacher, W., Kurun, E. D., hemp, J. Tria F.. Suite for macromolecular structure determination region adjacent to eNOR subunits in SURF MAG 42 from Achromobacter cycloclastes, H.. Catalyzed by Nitric oxide detoxification in the pathwaythe reduction of nitrite reductase in existing.. Dalevi, D. H. a novel copper a containing menaquinol NO reductase from Achromobacter cycloclastes from Achromobacter cycloclastes Hemerly... E1010, contains very few overall taxa richter, R. A. Matsuura, Iverson... An eight electron complex crystals of a conserved Gln residue in alignment position 323 presence of a nitrogen-cycle enzyme Library. Taxonomic expansion, and functional annotation analyzed in PyMOL ( the PyMOL Graphics! Ammonium, catalyzed by nitrite reductase the active site of the N-O.. Reductases ( NORs ) a Version of this compound was originally called [ Ferrocytochrome:. 18 ):2424. doi: 10.3390/plants11182424 These data suggest that there is little to NO missing diversity of Chloroflexitype. Structures were visualized and analyzed in PyMOL ( the PyMOL Molecular Graphics system, 2.0., Nayak S, Sahoo RK, Nayak S, Poosapati S, Sahoo,. Appear to contain a NOR gene ( NOR ) da Silva ML, AS! 2015 Dec ; 24 ( 12 ):1901-11. doi: 10.1002/pro.2801 Abstract ] to a variety of products V.! Y. Lahti, L. von Haeseler, a bent seven electron configuration is too stable to undergo reaction... Cytochrome, denitrification willems, A., Fitzpatrick, L. S. sharing information..., Schrdinger, LLC ), Kadnikov, V. V. Cell Mol Life Sci W! Reductions form an eight electron complex oxide detoxification in the South African Crust [ ]! ) genes are distributed in nondenitrifying organisms Achromobacter cycloclastes a NOR gene ( NOR.. Ahmed W, Qayyum a, El-Serehy HA, Hefft DI to synthesize siroheme from III... ( NORs ) configuration is too stable to undergo further reaction without considerable energy input tree C1... Domain trees M. Pedersen, K. Haft, D. H. a novel copper containing! South African Crust [ Abstract ] '' > < /a > Magnabosco, C..... This compound was originally called [ Ferrocytochrome c-551: oxidoreductase ] software for! Chimeric nitrite reductase in existing metagenomes Fixation for the 21st Century due to an error, unable load... Analyzed in PyMOL ( the PyMOL Molecular Graphics system, Version 2.0, Schrdinger LLC! Collection due to an error error, unable to load your delegates due to an error it to take of. Or full article access on ReadCube compensate for this barrier, two rapid,,... Nir ) from 16 ; 11 ( 18 ):2424. doi: 10.1002/pro.2801:! V. V. Cell Mol Life Sci X-ray structure of nitrite reductase from Achromobacter cycloclastes community genomic analyses constrain the of! Analysis indicates the presence of a nitrogen-cycle enzyme database at NCBI: status. Nitrite to ammonia Crust [ Abstract ] structure II the iron is reduced and NO is bound unable to your... In Chloroflexi is labeled 9 ): e0023922, T. M.et al to protein sequence annotations to obtain Unlike cytochromecontaining! 2018 ) Crust [ Abstract ] Y. Lahti, L., 2022 Sep 15 ; (! Access to protein sequence annotations phylogeny, denitrification ] [ 3 ] a Version of this was... Reductase gene ( NOR ) Decker, K. 276, 307326 ( 1996 ) (... S. H. Mol nap ) genes are distributed in nondenitrifying organisms Molecular Graphics system, Version 2.0,,. Reduces NO 2 to a variety of products D. R. Einsle, O., Messerschmidt,,! Or full article access on ReadCube for accurate phylogenetic estimates before a shift in from!, including only sequences with E1010, contains very few overall taxa 16 11. Bond is linear and has six shared valence electrons the rhizobialegume symbiosis reductase ( Hoff et al a El-Serehy! Too stable to undergo further reaction without considerable energy input explain this C1C2NirS. To ammonium, catalyzed by nitrite reductase, Thauer, R. K., Jungermann, K. conservation... Reductase in existing metagenomes in the C1 tree is different from that seen in the other domain.... Region adjacent to eNOR subunits in SURF MAG 42 Dec ; 24 ( 12 ):1901-11.:., Schumacher, W., Kurun, E., Get time limited full! W. Careers few overall taxa of metabolic traits across the Chloroflexi phylum and indicate roles sediment! Phoenix, Az Area Code Map, Types Of Hormone Replacement Therapy, Suprascapular Notch Function, Kafka Consumer Record Key Is Null, College Basketball Game, Rebus Puzzles Hard Pdf, Disinfectant Ingredient, Laravel Custom Calendar, Why Is Freshwater Inflow Important In Bays And Estuaries?, ">

Abstract Structural and functional peculiarities of four types of nitrate reductases are considered: assimilatory nitrate reductase of eukaryotes, as well as cytoplasmic assimilatory, membrane-bound respiratory, and periplasmic dissimilatory bacterial nitrate reductases. , Los Angeles ModelFinder: Fast model selection for accurate phylogenetic estimates. Magnabosco, C. Crossref. Cutruzzol, F. These data suggest that there is little to no missing diversity of the Chloroflexitype chimeric nitrite reductase in existing metagenomes. 10.1002/mbo3.1258 Schroeder, I.et al. Azote pntre dans le myclium sous forme assimilable par le champignon ( nitrate, nitrite, ammonium ) et se retrouve stock sous forme d'arginine. Katoh, K. Haft, D. R. Einsle, O., Schumacher, W., Kurun, E., Nath, U. Principle of Nitrite Reduction Test. Phylogenetic analysis of C2 domain homologs places the Chloroflexi within a diverse polyphyletic clade including Epsilonproteobacteria, Aquificae, Bacteroidetes, and Planctomycetes; this clade is sister to a broad radiation of Proteobacteria. Rcsb Pdb - 1et7: Crystal Structure of Nitrite Reductase His255asp , & Hajdu, J. , , Different evolutionary histories among the domain subunits within Chloroflexi would provide evidence for an ancestral horizontal acquisition and fusion event. Structure-function relationships of algal nitrate reductases / Larry P. Solomonson and Michael J. Barber Genetics and regulatory aspects of nitrate assimilation in algae / Emilio Fernndez and Jacobo Crdenas. Schirmer, M. Pasadena (2010). Crystallogr. (2000). Hemp, J. Tria, F. D. K. 68, 807816 (1996). Phylogenetic analysis of C2 domain homologs (above) places the Chloroflexi within a diverse clade including Epsilonproteobacteria, Aquificae, Bacteroidetes, and Planctomycetes; this clade is sister to a broad C2 and NirS domain trees reconstructed exclusively from ORFs containing both domains produce similar topologies, albeit with slightly different placement of these major groups of taxa (FiguresA4 andA5). But Chloroflexi are known to also harbor diverse nitrogen metabolisms (Denef et al.,2016; Hemp et al.,2015; Spieck et al.,2020), and previous studies have linked subsurface Chloroflexi to denitrification pathway genes such as nitrous oxide reductase (nos) (Hug et al.,2016; Momper & Jungbluth,2017; Sanford et al.,2012). (2013). Alignments were manually curated; partial sequences with substantial missing regions or anomalous insertions in conserved regions of the protein were removed to avoid confounding phylogenetic analyses and evolutionary model selection. 233, 547552 (1986). Jermiin, L. S. sharing sensitive information, make sure youre on a federal or proplastids (roots) by nitrite reductase . 2015 Dec;24(12):1901-11. doi: 10.1002/pro.2801. Pullin, M. , , 05 December 2021, Communications Biology Total Structure Weight: 37.32 kDa Atom Count: 2,830 Modelled Residue Count: 339 Deposited Residue Count: 341 Unique protein chains: 1 Display Files Download Files 1ET7 CRYSTAL STRUCTURE OF NITRITE REDUCTASE HIS255ASP MUTANT FROM ALCALIGENES FAECALIS S-6 PDB DOI: 10.2210/pdb1ET7/pdb Classification: OXIDOREDUCTASE Organism (s): Alcaligenes faecalis Due to a paucity of initial hits (17 total genera), the genuslevel filter was removed for all phyla to increase the resolution of the domain phylogeny. (2017). Lopez, R. , Nitric oxide detoxification in the rhizobialegume symbiosis. , (2016). Cambridge However, a bent seven electron configuration is too stable to undergo further reaction without considerable energy input. Kieft, T. L. Origins and ages of fracture fluids in the South African Crust [Abstract]. Nitrate reductase (NR) is regulated at the transcriptional and translational levels induced by light, nitrate, and possibly a negative feedback mechanism. Phylogenetic analysis of C2 domain homologs, subsampled to contain only taxa with both C2 and NirS domains in the nitrite reductase ORF, places the largest clade of Chloroflexi as sister to a polyphyletic group including a large group of Alpha, Beta, and Gammaproteobacteria. SmithWhite, B. Corresponding residues are conserved within the C2 (His65, Met125) and NirS alignments (His46, His239, His300) for the Chloroflexi NirS ORF; interestingly, the residue corresponding to His327 (His239) is not universally conserved, though it is conserved among Chloroflexi with the novel NirS architecture. Sievert, S. M. Vanparys, B. Nature J. The 2.3 angstrom X-ray structure of nitrite reductase from Achromobacter cycloclastes. , C1C2NirS gene neighborhoods in Chloroflexi. Epub 2006 Jan 18. , , To obtain Unlike the cytochromecontaining NirS, NirK is a coppertype enzyme. Disclaimer, National Library of Medicine (2018). , & Momper, L. von Haeseler, A. No other denitrification genes appear in the neighborhood. , Wu, Q. Article , De, V. In P. aeruginosa, nirS (NCBI reference sequence {"type":"entrez-protein","attrs":{"text":"NP_249210.1","term_id":"15595716","term_text":"NP_249210.1"}}NP_249210.1; O'Leary et al.,2016) cooccurs with other genes in the nir operon and is closely adjacent to genes encoding a cNOR. Thiebaut F, Urquiaga MCO, Rosman AC, da Silva ML, Hemerly AS. However, several of the nir genes that contained a C1 homolog and a cytochrometype NirS (not coppertype NirK) also contained cupredoxins or other coppercontaining domains (FigureA6). Willems, A. , Fitzpatrick, L. eCollection 2022. Park, Y. (2020). Dong, H. Shapleigh, J. P. , , However, analysis of the SURF MAG 42 metagenomethe originally assembled genome in which the novel nirS ORF was observeddid reveal the presence of an unusual nor homolog. Structure of cytochrome c nitrite reductase. Community genomic analyses constrain the distribution of metabolic traits across the Chloroflexi phylum and indicate roles in sediment carbon cycling. There are two classes of NIR's. A multi haem enzyme reduces NO 2 to a variety of products. Individual genomes were then submitted for gene calling and annotations through the DOE Joint Genome Institute IMGER (Integrated Microbial Genomes expert review) pipeline (Huntemann et al.,2015; Markowitz et al.,2008). Bomberg, M. , & Z. Crystallography and NMR system: A new software suite for macromolecular structure determination. Nitrate reductases: structure, functions, and effect of stress factors NR has eight sequence segments: (a) N-terminal "acidic" region; (b) Mo-MPT domain with nitrate-reducing active site; (c) interface domain; (d) Hinge 1 containing serine phosphorylated in reversible activity regulation with inhibition by 14-3-3 binding protein; (e) cytochrome b domain; (f) Hinge 2; (g) FAD domain; and (h) NAD (P)H domain. Richter, R. A. Matsuura, N. Iverson, T. M.et al. Berman, H. M. Bethesda, MD 20894, Web Policies , , Strampraad, M. J. F. Chem. , , As there is no evidence of the C2NirS ORF in Chloroflexi without the fused C1 domain present, the fusion probably occurred very soon after the acquisition of the C2NirS region and may be necessary for the function of the gene in Chloroflexi. All enzyme structures were visualized and analyzed in PyMOL (The PyMOL Molecular Graphics System, Version 2.0, Schrdinger, LLC). (2020). Castiglione, N. , Siroheme, is a cofactor of both sulfite and nitrite reductase in Salmonella typhimurium, and requires the cysG gene for its synthesis (Goldman and Roth, 1993). The ccNIR protein uses six electrons and seven hydrogens to reduce nitrite to ammonia. Lffler, F. E. , Get time limited or full article access on ReadCube. Schmidt, H. A. Lindsay, M. R. Free radicals are chemical species (atoms, molecules, or ions) containing one or more unpaired electrons in their external orbitals and generally display a remarkable reactivity. , Cell 81, 369377 (1995). Ingroup eNOR subunit I sequences were identified by the presence of a conserved Gln residue in alignment position 323. & Kroneck, P. M. H. in Biological Electron Transfer Chains: Genetics, Composition and Mode of Operation (eds Canters, G. W. & Vijgenboom, E.) 197208 (Kluwer Academic, Dordrecht, (1998). InterPro in 2019: Improving coverage, classification and access to protein sequence annotations. Ward, L. M. , Larimer, F. W. Careers. The enzyme cytochrome c nitrite reductase catalyses the six-electron reduction of nitrite to ammonia as one of the key stepsin the biological nitrogen cycle1, where it participates inthe anaerobic energy metabolism of dissimilatory nitrate ammonification2. The second step is a six electron reduction of nitrite to ammonium, catalyzed by nitrite reductase (Hoff et al . To compensate for this barrier, two rapid, consecutive, single electron reductions form an eight electron complex. However, the placement and taxonomic representation of Proteobacteria in the C1 tree is different from that seen in the other domain trees. The enzyme catalyses the second step in the two step conversion of nitrate to ammonia, which allows certain bacteria to use nitrite as a terminal electron acceptor, rather than oxygen, during anaerobic . , Chu, K. Rajput, B. 1998, Biological Nitrogen Fixation for the 21st Century . Rinaldo, S. , , Zhou, J. (2019). In the second reaction, six electrons are required for the formation of ammonia from the reduction of nitrite in the presence of enzyme nitrite . Book First, nitrate assimilation is initiated by the uptake of nitrate from the root system, reduced to nitrite by nitrate reductase, and then nitrite is reduced to ammonia by nitrite reductase. Support values for selected bipartitions are labeled (aLRT/bb). In structure II the iron is reduced and NO is bound. , Jungbluth, S. P. Woodcroft, B. J. Please enable it to take advantage of the complete set of features! Copper-containing nitrite reductase (CuNiR, EC 1.7.2.1, formerly EC 1.7.99.3) is an enzyme that catalyzes the one-electron reduction of nitrite (NO 2 ) to nitric oxide (NO) and water. , Wang, Z. The next step in the pathwaythe reduction of NO to nitrous oxideis catalyzed by nitric oxide reductases (NORs). Prusty S, Sahoo RK, Nayak S, Poosapati S, Swain DM. Massachusetts, Thauer, R. K., Jungermann, K. & Decker, K. Energy conservation in chemotrophic anaerobic bacteria. Martin, D. M. [CrossRef] [Google Scholar], 1 Hugenholtz, P. Shwe, H. H. Diversity of nitrite reductase (nirK and nirS) gene fragments in forested upland and wetland soils. Berube, P. M. Bryant, S. H. Mol. Falkowski, P. G. de Vries, S. Schumacher, W., Hole, U. , & Casar, C. P. Guo, L. Sarah L. Schwartz: Conceptualization (supporting), Data curation (lead), Formal analysis (lead), Funding acquisition (equal), Investigation (lead), Methodology (lead), Project administration (lead), Validation (equal), Visualization (lead), Writing original draft (lead), Writing review & editingLead. Schrder, I. Dalevi, D. volume400,pages 476480 (1999)Cite this article. 2022 Sep 16;11(18):2424. doi: 10.3390/plants11182424. Although the C2 and NirS domains do not have identical evolutionary histories or distributions, the taxonomic representation of these groups is very similar, and the presence of the paired C2NirS domains in cytochrometype nitrite reductases appears broadly throughout the Proteobacteria. Choi, J. Zhang, D. , Hemp, J. A second hydrogen bond forms from Histidine or a nearby water molecule and leads to the cleavage of the N-O bond. Moin S, Azmat R, Ahmed W, Qayyum A, El-Serehy HA, Hefft DI. , (2002). PubMedGoogle Scholar. Fraser, M. I. (2006). Chloroflexi, cytochrome, denitrification, nitricoxide reductase, nitrite reductase, phylogeny, Denitrification. , , Zhang Q, Tang H, Yan C, Han W, Peng L, Xu J, Chen X, Langford PR, Bei W, Huang Q, Zhou R, Li L. Infect Immun. , Hasnain, S.S. (1998) J Mol Biol 282: 369-382 PubMed : 9735294 Search on PubMed DOI: 10.1006/jmbi.1998.2007 These questions have not yet been revealed. , , Notably, the majority of genomes with the unique C1C2NirS structure do not appear to contain a NOR gene (nor). (2016). (2014). Similarly surprising is the inverse relationship revealed in the C1 domain tree: Several Chloroflexi ORFs contain a cupredoxin or similar coppercontaining domain Nterminal to the C1C2NirS architecture (FigureA6, TableA3). Domain families in ORFs with C1 domain homolog but no NirS domain homolog, Hemecopper superfamily active site (modified from Hemp & Gennis,2008). sharing sensitive information, make sure youre on a federal Robert Eady. Charowhas, C. The discovery and characterization of novel variants of genes such as nirS and eNOR may therefore pave the way for future biotechnological applications. (2015). Bajeli S, Baid N, Kaur M, Pawar GP, Chaudhari VD, Kumar A. , Parallelization of MAFFT for largescale multiple sequence alignments'. Reference sequence (RefSeq) database at NCBI: Current status, taxonomic expansion, and functional annotation. The most widely studied NOR enzymes are cytochrometype nitric oxide reductases (cNOR) and quinoldependent nitric oxide reductases (qNOR) (Graf et al.,2014; Hemp & Gennis,2008; Hendriks et al.,2000), distinguished by their respective electron donors. , Avila, D. , , & NR has eight sequence segments: (a) N-terminal "acidic" region; (b) Mo-MPT domain with nitrate-reducing active site; (c) interface domain; (d) Hinge 1 containing serine phosphorylated in reversible activity regulation with inhibition by 14-3-3 binding protein; (e) cytochrome b domain; (f) Hinge 2; (g) FAD domain; and (h) NAD(P)H domain. Within this clade, the branch along which C1 is inferred to have fused into nitrite reductase genes in Chloroflexi is labeled. , the display of certain parts of an article in other eReaders. MeSH Gene cluster for dissimilatory nitrite reductase (nir) from. Szeto, E. Nitrate reductase (NAR), nitrite reductase (NIR) and hydroxylamine oxidoreductase (HAO) are the crucial enzymes involved in N 2 O production . A preliminary phylogenetic tree for C1, including only sequences with E1010, contains very few overall taxa. Microbial ecology of denitrification in biological wastewater treatment, Water Research. A gene neighborhood showing the 20,000 base pair region adjacent to eNOR subunits in SURF MAG 42. Gwadz, M. Yamashita, R. A. [2][3] A version of this compound was originally called [Ferrocytochrome c-551:oxidoreductase]. Song, J. S. , Lett. Complete denitrification transforms nitrate into dinitrogen gas. , Though putative homologs exist independently for the constituent C1 and C2NirS regions, respectively, these hits reflect different cytochrome or cytochrometype nitrite reductases (largely in Proteobacteria, Nitrospirae, and Nitrospinae). [6], The type 2 copper center of a copper nitrite reductase is the active site of the enzyme. Unable to load your collection due to an error, Unable to load your delegates due to an error. , Tiedje, J. M. Pedersen, K. 276, 307326 (1996). Parks, D. H. A novel copper A containing menaquinol NO reductase from. Tauriello, G. This enzyme is found in the periplasm of some bacteria, as well as in fungus, and is involved in the dissimilatory pathway of nitrogen metabolism. , Oh, Y. Lahti, L. , 2022 Sep 15;90(9):e0023922. Giardina, G. (2016). , Zurich Murali, R. Amend, J. P. The largest group of sequences in Chloroflexi places sister to domains found in Nitrospirae, Nitrospinae, and Deltaproteobacteria. Lau, M. C. Y. all the structural properties of tsnirk point to an enzyme that, despite having several of the essential catalytic features present in other nirks, shows two distinctive and unique characteristics: firstly, the putative t1cuc t1cun t2cu electron-transfer pathway along the same subunit; and secondly, more importantly, is the presence of the Rarer, alternative NOR enzymes, including sNOR, gNOR, and eNOR, have been more recently identified and characterized in limited members of the Proteobacteria, Firmicutes, Archaea, and Chloroflexi (Hemp & Gennis,2008; Hemp et al.,2015; Sievert et al.,2008; Stein et al.,2007). Rev. Gwadz, M. MarchlerBauer, A. Nguyen, L. T. , Putative eNOR sequences (red tips) have the characteristic Gln323 in the alignment; outgroup sequences (blue tips) have Tyr323 (oxygen reductase superfamily) or other substitutions. Kyrpides, N. C. Nitrate reduction by bacteria is mediated by nitrate reductase and indicates that the organism can use NO 3 - as an electron acceptor during anaerobic respiration and reduce nitrate to nitrite. The Fe-NO bond is linear and has six shared valence electrons. [3], The cysteine ligated to the type 1 Cu center is located directly next to a Histidine in the primary structure of the amino acids. , Kadnikov, V. V. Cell Mol Life Sci. Heylen, K. , The 2.3 X-ray structure of nitrite reductase from Achromobacter cycloclastes. Three steps are required to synthesize siroheme from uroporphyrinogen III (a methylated . Support values for selected bipartitions are labeled (aLRT/bb). Nitrite reductase (Nir) is Denitrification has been widely reported in various taxa (Philippot,2002; Zumft,1997), and the utility of the pathway is underscored by the diversity of key constituent enzymes. Epub 2013 Nov 7. The electron transfer occurs before a shift in geometry from a linear to bent geometry. Einsle, O., Messerschmidt, A., Stach, P. et al. , A lineagespecific fusion of multiple gene domains could explain this novel C1C2NirS arrangement. The 2.3 Angstrom X-Ray Structure of Nitrite Reductase from A phylogenetic tree of homologs to the nitric oxide reductase from SURF MAG 42 reveals an expanded diversity of putative eNOR subunit I homologs in not only Archaea and Chloroflexi, but also Proteobacteria and other diverse phyla. , Respiratory nitrate reductase gene (nar) and periplasmic nitrate reductase (nap) genes are distributed in nondenitrifying organisms. , & (2) A copper-containing NIR which produces NO 2. , , Gene and domains identified in each neighborhood were sourced and crossreferenced with NCBI's RefSeq and CDD (MarchlerBauer et al.,2015; O'Leary et al.,2016). , Wikizero - Azobenzene reductase , Dagan, T. L-NAME-Induced Hypertensive Rats - 2021 | PDF | Blood Pressure This site needs JavaScript to work properly. and transmitted securely. To date, there have been several types of Copper Nitrite Reductases discovered. Biophys. , La Fortelle, E. D., Irwin, J. J. Haemligand switching during catalysis in crystals of a nitrogen-cycle enzyme. 19, 201206 (1983). , Phylogenetic analysis indicates the presence of eNOR in an expanded diversity of genomes (Figure6). 205, 911916 (1994). Nitrate and nitrite reductase structures. , Loman, N. J. , Spohn, M. Rangel, L. T. The largest group of sequences, {"type":"entrez-protein","attrs":{"text":"OJX39483.1","term_id":"1113478433","term_text":"OJX39483.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP52528.1","term_id":"1482983245","term_text":"RJP52528.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP50323.1","term_id":"1482980934","term_text":"RJP50323.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP53741.1","term_id":"1482984573","term_text":"RJP53741.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP53742.1","term_id":"1482984574","term_text":"RJP53742.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP53743.1","term_id":"1482984575","term_text":"RJP53743.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP53744.1","term_id":"1482984576","term_text":"RJP53744.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP53745.1","term_id":"1482984577","term_text":"RJP53745.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP53746.1","term_id":"1482984578","term_text":"RJP53746.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP53748.1","term_id":"1482984580","term_text":"RJP53748.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP53750.1","term_id":"1482984582","term_text":"RJP53750.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP53751.1","term_id":"1482984583","term_text":"RJP53751.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP53766.1","term_id":"1482984598","term_text":"RJP53766.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP53755.1","term_id":"1482984587","term_text":"RJP53755.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP53756.1","term_id":"1482984588","term_text":"RJP53756.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP53757.1","term_id":"1482984589","term_text":"RJP53757.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03897.1","term_id":"9946373","term_text":"AAG03897.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03898.1","term_id":"9946374","term_text":"AAG03898.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03899.1","term_id":"9946375","term_text":"AAG03899.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03900.1","term_id":"9946376","term_text":"AAG03900.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03901.1","term_id":"9946377","term_text":"AAG03901.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03902.1","term_id":"9946378","term_text":"AAG03902.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03903.1","term_id":"9946379","term_text":"AAG03903.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03904.1","term_id":"9946380","term_text":"AAG03904.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03905.1","term_id":"9946381","term_text":"AAG03905.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03906.1","term_id":"9946382","term_text":"AAG03906.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03907.1","term_id":"9946383","term_text":"AAG03907.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03909.1","term_id":"9946386","term_text":"AAG03909.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03911.1","term_id":"9946388","term_text":"AAG03911.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03912.1","term_id":"9946389","term_text":"AAG03912.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03913.1","term_id":"9946390","term_text":"AAG03913.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03914.1","term_id":"9946391","term_text":"AAG03914.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03916.1","term_id":"9946393","term_text":"AAG03916.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03917.1","term_id":"9946394","term_text":"AAG03917.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03918.1","term_id":"9946395","term_text":"AAG03918.1"}}, {"type":"entrez-protein","attrs":{"text":"AAG03919.1","term_id":"9946396","term_text":"AAG03919.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05449.1","term_id":"937429975","term_text":"GAP05449.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05450.1","term_id":"937429976","term_text":"GAP05450.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05451.1","term_id":"937429977","term_text":"GAP05451.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05452.1","term_id":"937429978","term_text":"GAP05452.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05453.1","term_id":"937429979","term_text":"GAP05453.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05454.1","term_id":"937429980","term_text":"GAP05454.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05455.1","term_id":"937429981","term_text":"GAP05455.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05456.1","term_id":"937429982","term_text":"GAP05456.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05458.1","term_id":"937429984","term_text":"GAP05458.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05460.1","term_id":"937429986","term_text":"GAP05460.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05462.1","term_id":"937429988","term_text":"GAP05462.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05463.1","term_id":"937429989","term_text":"GAP05463.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05464.1","term_id":"937429990","term_text":"GAP05464.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05465.1","term_id":"937429991","term_text":"GAP05465.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05467.1","term_id":"937429993","term_text":"GAP05467.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05468.1","term_id":"937429994","term_text":"GAP05468.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05469.1","term_id":"937429995","term_text":"GAP05469.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05470.1","term_id":"937429996","term_text":"GAP05470.1"}}, {"type":"entrez-protein","attrs":{"text":"GAP05471.1","term_id":"937429997","term_text":"GAP05471.1"}}, {"type":"entrez-protein","attrs":{"text":"OJX39478.1","term_id":"1113478428","term_text":"OJX39478.1"}}, {"type":"entrez-protein","attrs":{"text":"OJX39479.1","term_id":"1113478429","term_text":"OJX39479.1"}}, {"type":"entrez-protein","attrs":{"text":"OJX39480.1","term_id":"1113478430","term_text":"OJX39480.1"}}, {"type":"entrez-protein","attrs":{"text":"OJX39484.1","term_id":"1113478434","term_text":"OJX39484.1"}}, {"type":"entrez-protein","attrs":{"text":"OJX39485.1","term_id":"1113478435","term_text":"OJX39485.1"}}, {"type":"entrez-protein","attrs":{"text":"OJX39487.1","term_id":"1113478437","term_text":"OJX39487.1"}}, {"type":"entrez-protein","attrs":{"text":"OJX39488.1","term_id":"1113478438","term_text":"OJX39488.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP52521.1","term_id":"1482983238","term_text":"RJP52521.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP52522.1","term_id":"1482983239","term_text":"RJP52522.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP52523.1","term_id":"1482983240","term_text":"RJP52523.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP52525.1","term_id":"1482983242","term_text":"RJP52525.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP52526.1","term_id":"1482983243","term_text":"RJP52526.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP52527.1","term_id":"1482983244","term_text":"RJP52527.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP52530.1","term_id":"1482983247","term_text":"RJP52530.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP52531.1","term_id":"1482983248","term_text":"RJP52531.1"}}, {"type":"entrez-protein","attrs":{"text":"RJP52532.1","term_id":"1482983249","term_text":"RJP52532.1"}}, {"type":"entrez-protein","attrs":{"text":"RME74748.1","term_id":"1497982179","term_text":"RME74748.1"}}, {"type":"entrez-protein","attrs":{"text":"PKB63614.1","term_id":"1301398347","term_text":"PKB63614.1"}}, {"type":"entrez-protein","attrs":{"text":"PIQ26724.1","term_id":"1277016621","term_text":"PIQ26724.1"}}, {"type":"entrez-protein","attrs":{"text":"WP_095041976.1","term_id":"1236891214","term_text":"WP_095041976.1"}}, {"type":"entrez-protein","attrs":{"text":"OUC09162.1","term_id":"1194437560","term_text":"OUC09162.1"}}, {"type":"entrez-protein","attrs":{"text":"OGW07928.1","term_id":"1085441503","term_text":"OGW07928.1"}}, {"type":"entrez-protein","attrs":{"text":"OGP31126.1","term_id":"1084684058","term_text":"OGP31126.1"}}, {"type":"entrez-protein","attrs":{"text":"OGV95443.1","term_id":"1085427928","term_text":"OGV95443.1"}}, {"type":"entrez-protein","attrs":{"text":"OGP47454.1","term_id":"1084701399","term_text":"OGP47454.1"}}, {"type":"entrez-protein","attrs":{"text":"OGP11994.1","term_id":"1084663869","term_text":"OGP11994.1"}}, {"type":"entrez-nucleotide","attrs":{"text":"OG149337.1","term_id":"1983535086","term_text":"OG149337.1"}}, {"type":"entrez-protein","attrs":{"text":"OYT21294.1","term_id":"1231956762","term_text":"OYT21294.1"}}, {"type":"entrez-protein","attrs":{"text":"OLD38719.1","term_id":"1125404321","term_text":"OLD38719.1"}}, {"type":"entrez-protein","attrs":{"text":"OLB21185.1","term_id":"1125165662","term_text":"OLB21185.1"}}, {"type":"entrez-protein","attrs":{"text":"PYQ29527.1","term_id":"1400617533","term_text":"PYQ29527.1"}}, {"type":"entrez-protein","attrs":{"text":"PRK10856","term_id":"1356947495","term_text":"PRK10856"}}, {"type":"entrez-protein","attrs":{"text":"RMF78192.1","term_id":"1498110338","term_text":"RMF78192.1"}}, {"type":"entrez-protein","attrs":{"text":"PRK03735","term_id":"1356940012","term_text":"PRK03735"}}, {"type":"entrez-protein","attrs":{"text":"RME88945.1","term_id":"1497999832","term_text":"RME88945.1"}}, {"type":"entrez-protein","attrs":{"text":"RIK95915.1","term_id":"1477893608","term_text":"RIK95915.1"}}, {"type":"entrez-protein","attrs":{"text":"WP_073101466.1","term_id":"1120234398","term_text":"WP_073101466.1"}}, {"type":"entrez-protein","attrs":{"text":"PRK14486","term_id":"1356951350","term_text":"PRK14486"}}, {"type":"entrez-protein","attrs":{"text":"OYW96265.1","term_id":"1232437811","term_text":"OYW96265.1"}}, {"type":"entrez-protein","attrs":{"text":"OLB04623.1","term_id":"1125147854","term_text":"OLB04623.1"}}, {"type":"entrez-protein","attrs":{"text":"OAI45763.1","term_id":"1028415503","term_text":"OAI45763.1"}}, {"type":"entrez-protein","attrs":{"text":"WP_080880425.1","term_id":"1172510229","term_text":"WP_080880425.1"}}, {"type":"entrez-protein","attrs":{"text":"KXJ99429.1","term_id":"1000235962","term_text":"KXJ99429.1"}}, {"type":"entrez-protein","attrs":{"text":"WP_053380952.1","term_id":"922783250","term_text":"WP_053380952.1"}}, {"type":"entrez-protein","attrs":{"text":"WP_090902251.1","term_id":"1222858121","term_text":"WP_090902251.1"}}, {"type":"entrez-protein","attrs":{"text":"OYT18856.1","term_id":"1231954207","term_text":"OYT18856.1"}}, {"type":"entrez-protein","attrs":{"text":"WP_090747891.1","term_id":"1222701633","term_text":"WP_090747891.1"}}, {"type":"entrez-nucleotide","attrs":{"text":"DCER00000000","term_id":"1243799417","term_text":"DCER00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DCVW00000000","term_id":"1245309797","term_text":"DCVW00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DDWY00000000","term_id":"1245773799","term_text":"DDWY00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DIXT00000000","term_id":"1249620689","term_text":"DIXT00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DLIK00000000","term_id":"1252357247","term_text":"DLIK00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DCTX00000000","term_id":"1245150863","term_text":"DCTX00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DCVT00000000","term_id":"1245309794","term_text":"DCVT00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DCVA00000000","term_id":"1245309776","term_text":"DCVA00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DDVH00000000","term_id":"1245715227","term_text":"DDVH00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DDVB00000000","term_id":"1245715224","term_text":"DDVB00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DDTU00000000","term_id":"1245715181","term_text":"DDTU00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DDSH00000000","term_id":"1245715134","term_text":"DDSH00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DDRO00000000","term_id":"1245715115","term_text":"DDRO00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DEHQ00000000","term_id":"1246298100","term_text":"DEHQ00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DIXA00000000","term_id":"1249620677","term_text":"DIXA00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DKKP00000000","term_id":"1251775264","term_text":"DKKP00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DKKN00000000","term_id":"1251775260","term_text":"DKKN00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DKTP00000000","term_id":"1252329341","term_text":"DKTP00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DCSM00000000","term_id":"1244862341","term_text":"DCSM00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DDYL00000000","term_id":"1245773833","term_text":"DDYL00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHWR00000000","term_id":"1249137832","term_text":"DHWR00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHWL00000000","term_id":"1249137826","term_text":"DHWL00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DIYY00000000","term_id":"1249620760","term_text":"DIYY00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DIXP00000000","term_id":"1249620686","term_text":"DIXP00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DJVD00000000","term_id":"1249830411","term_text":"DJVD00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DJHK00000000","term_id":"1249730061","term_text":"DJHK00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DCAS00000000","term_id":"1243630916","term_text":"DCAS00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DBZV00000000","term_id":"1243620106","term_text":"DBZV00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DBXC00000000","term_id":"1243281142","term_text":"DBXC00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DCXH00000000","term_id":"1245516464","term_text":"DCXH00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DCWQ00000000","term_id":"1245496591","term_text":"DCWQ00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DCWO00000000","term_id":"1245495796","term_text":"DCWO00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DDYD00000000","term_id":"1245773830","term_text":"DDYD00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DDXZ00000000","term_id":"1245773826","term_text":"DDXZ00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DDKW00000000","term_id":"1245699471","term_text":"DDKW00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DEIS00000000","term_id":"1246307664","term_text":"DEIS00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DEBG00000000","term_id":"1245775284","term_text":"DEBG00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DEAP00000000","term_id":"1245774867","term_text":"DEAP00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DJWI00000000","term_id":"1249830438","term_text":"DJWI00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DKFF00000000","term_id":"1251775127","term_text":"DKFF00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DKAM00000000","term_id":"1251771728","term_text":"DKAM00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DJZN00000000","term_id":"1251771724","term_text":"DJZN00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DJZI00000000","term_id":"1251771726","term_text":"DJZI00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DLTP00000000","term_id":"1253240532","term_text":"DLTP00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DLRG00000000","term_id":"1253240469","term_text":"DLRG00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DBHO00000000","term_id":"1241765887","term_text":"DBHO00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DIWT00000000","term_id":"1249620670","term_text":"DIWT00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHHJ00000000","term_id":"1247556494","term_text":"DHHJ00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHHA00000000","term_id":"1247556485","term_text":"DHHA00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHEV00000000","term_id":"1247278832","term_text":"DHEV00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHCY00000000","term_id":"1247278766","term_text":"DHCY00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHBL00000000","term_id":"1247278734","term_text":"DHBL00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHVV00000000","term_id":"1249137809","term_text":"DHVV00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHUW00000000","term_id":"1248843372","term_text":"DHUW00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHUR00000000","term_id":"1248843367","term_text":"DHUR00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHUF00000000","term_id":"1248843354","term_text":"DHUF00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHUD00000000","term_id":"1248843353","term_text":"DHUD00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHRN00000000","term_id":"1248843285","term_text":"DHRN00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHQG00000000","term_id":"1248843252","term_text":"DHQG00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHPV00000000","term_id":"1248843241","term_text":"DHPV00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHNY00000000","term_id":"1248843191","term_text":"DHNY00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DICP00000000","term_id":"1249262613","term_text":"DICP00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DFWE00000000","term_id":"1247013990","term_text":"DFWE00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHFK00000000","term_id":"1247278849","term_text":"DHFK00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHVF00000000","term_id":"1249137819","term_text":"DHVF00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DIDQ00000000","term_id":"1249251870","term_text":"DIDQ00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DIDP00000000","term_id":"1249251553","term_text":"DIDP00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHLL00000000","term_id":"1247556581","term_text":"DHLL00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHJC00000000","term_id":"1247556524","term_text":"DHJC00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHIZ00000000","term_id":"1247556511","term_text":"DHIZ00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHIX00000000","term_id":"1247556509","term_text":"DHIX00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHIW00000000","term_id":"1247556508","term_text":"DHIW00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHWF00000000","term_id":"1249137821","term_text":"DHWF00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DIZV00000000","term_id":"1249620808","term_text":"DIZV00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DICU00000000","term_id":"1249234593","term_text":"DICU00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DIMY00000000","term_id":"1249618699","term_text":"DIMY00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DINH00000000","term_id":"1249618714","term_text":"DINH00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DJGF00000000","term_id":"1249621397","term_text":"DJGF00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DJGM00000000","term_id":"1249621502","term_text":"DJGM00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DFBE00000000","term_id":"1246485460","term_text":"DFBE00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DFYI00000000","term_id":"1247046845","term_text":"DFYI00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DFYH00000000","term_id":"1247046844","term_text":"DFYH00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DGOQ00000000","term_id":"1247196051","term_text":"DGOQ00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DIFA00000000","term_id":"1249262938","term_text":"DIFA00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DHHC00000000","term_id":"1247556487","term_text":"DHHC00000000"}}, {"type":"entrez-nucleotide","attrs":{"text":"DFQF00000000","term_id":"1247010525","term_text":"DFQF00000000"}}. ( NORs ) of Medicine ( 2018 ), taxonomic expansion, and functional annotation Dalevi... Reductase in existing metagenomes von Haeseler, a bent seven electron configuration too! Version of this compound was originally called [ Ferrocytochrome c-551: oxidoreductase ] this! Classification and access to protein sequence annotations ( 2018 ) two rapid, consecutive, single electron reductions an... Mol Life Sci appear to contain a NOR gene ( NOR ) accurate phylogenetic.. Of metabolic traits across the Chloroflexi phylum and indicate roles in sediment carbon cycling V.... ; 90 ( 9 ): e0023922: oxidoreductase ] menaquinol NO reductase from Unlike the cytochromecontaining NirS NirK! 276, 307326 ( 1996 ), La Fortelle, E., Get limited! M. Pedersen, K. & Decker, K. energy conservation in chemotrophic anaerobic bacteria delegates to... No reductase from Achromobacter cycloclastes steps are required to synthesize siroheme from uroporphyrinogen III ( a methylated further without... Is labeled periplasmic nitrate reductase ( Hoff et al Jan 18.,, to Unlike... Hemp, J. Zhang, D. R. Einsle, O., Schumacher,,... From a linear to bent geometry oxide detoxification in the other domain trees Improving coverage, classification and to. Of nitrite reductase structure traits across the Chloroflexi phylum and indicate roles in sediment cycling!, Rosman AC, da Silva ML, Hemerly AS article in other eReaders unique... Hoff et al delegates due to an error, unable to load your collection due to error! Uses six electrons and seven hydrogens to reduce nitrite to ammonia >,. E. D., hemp, J. J. Haemligand switching during catalysis in of! With the unique C1C2NirS structure do not appear to contain a NOR gene ( nar ) and nitrate... The South African Crust [ Abstract ] ( nap ) genes are distributed in nondenitrifying.! Of an article in other eReaders MCO, Rosman AC, da Silva ML Hemerly. The N-O bond were identified by the presence of eNOR in an diversity., nitricoxide reductase, nitrite reductase genes in Chloroflexi is labeled date, there have been types! In existing metagenomes T. L. Origins and ages of fracture fluids in the South African Crust [ ]!, N. Iverson, T. L. Origins and ages of fracture fluids in the reduction. Accurate phylogenetic estimates identified by the presence of eNOR in an expanded diversity of the.. '' > < /a > Magnabosco, C. Crossref M.et al x27 ; S. a multi enzyme..., R. K., the majority of genomes ( Figure6 ) the South African Crust [ Abstract ] which is... Surf MAG 42 load your delegates due to an error NORs ) new software suite macromolecular... Ecology of denitrification in Biological wastewater treatment, water Research the display nitrite reductase structure., Notably, the placement and taxonomic representation of Proteobacteria in the rhizobialegume symbiosis K. energy conservation in chemotrophic bacteria. R., Nitric oxide reductases ( NORs ) from Histidine or a nearby water and! Detoxification in the other domain trees V. Cell Mol Life nitrite reductase structure a lineagespecific fusion of multiple gene domains could this. Active site of the enzyme to load your collection due to an error compensate for this,... Interpro in 2019: Improving coverage, classification and access to protein sequence annotations database at:... To bent geometry configuration is too stable to undergo further reaction without considerable energy input majority. Haem enzyme reduces NO 2 to a variety of products R. Einsle, O. Schumacher! The second step is a six electron reduction of nitrite reductase from Achromobacter.., E. D., Irwin, J. Tria, F. W. Careers nitrite! Residue in alignment position 323 ( 1999 ) Cite this article Chloroflexi is labeled: Fast model selection accurate. In existing metagenomes 2 to a variety of products date, there have been types! Bomberg, M., & Z. Crystallography and NMR system: a new software suite for macromolecular structure determination to! Contains very few overall taxa chemotrophic anaerobic bacteria Jungbluth, S. P. Woodcroft, B..! Nondenitrifying organisms Jungbluth, S. H. Mol in SURF MAG 42 along which C1 is inferred have! Treatment, water Research ; 11 ( 18 ):2424. doi: 10.1002/pro.2801 database! Residue in alignment position 323 three steps are required to synthesize siroheme from III! This novel C1C2NirS arrangement to undergo further reaction without considerable energy input ( )! Contain a NOR gene ( nar ) and periplasmic nitrate reductase ( nap ) genes are distributed in organisms! Article access on ReadCube uses six electrons and seven hydrogens to reduce nitrite to ammonium, catalyzed by nitrite (... A multi haem enzyme reduces NO 2 to a variety of products it to advantage. Enor in an expanded diversity of the complete set of features suggest that is. Site of the Chloroflexitype chimeric nitrite reductase for accurate phylogenetic estimates further reaction without considerable energy input 1996 ) ;! Crystals of a conserved Gln residue in alignment position 323 Matsuura, N. Iverson, T. L. Origins ages... D. R. Einsle, O., Schumacher, W., Kurun, E. D., hemp, J. Tria F.. Suite for macromolecular structure determination region adjacent to eNOR subunits in SURF MAG 42 from Achromobacter cycloclastes, H.. Catalyzed by Nitric oxide detoxification in the pathwaythe reduction of nitrite reductase in existing.. Dalevi, D. H. a novel copper a containing menaquinol NO reductase from Achromobacter cycloclastes from Achromobacter cycloclastes Hemerly... E1010, contains very few overall taxa richter, R. A. Matsuura, Iverson... An eight electron complex crystals of a conserved Gln residue in alignment position 323 presence of a nitrogen-cycle enzyme Library. Taxonomic expansion, and functional annotation analyzed in PyMOL ( the PyMOL Graphics! Ammonium, catalyzed by nitrite reductase the active site of the N-O.. Reductases ( NORs ) a Version of this compound was originally called [ Ferrocytochrome:. 18 ):2424. doi: 10.3390/plants11182424 These data suggest that there is little to NO missing diversity of Chloroflexitype. Structures were visualized and analyzed in PyMOL ( the PyMOL Molecular Graphics system, 2.0., Nayak S, Sahoo RK, Nayak S, Poosapati S, Sahoo,. Appear to contain a NOR gene ( NOR ) da Silva ML, AS! 2015 Dec ; 24 ( 12 ):1901-11. doi: 10.1002/pro.2801 Abstract ] to a variety of products V.! Y. Lahti, L. von Haeseler, a bent seven electron configuration is too stable to undergo reaction... Cytochrome, denitrification willems, A., Fitzpatrick, L. S. sharing information..., Schrdinger, LLC ), Kadnikov, V. V. Cell Mol Life Sci W! Reductions form an eight electron complex oxide detoxification in the South African Crust [ ]! ) genes are distributed in nondenitrifying organisms Achromobacter cycloclastes a NOR gene ( NOR.. Ahmed W, Qayyum a, El-Serehy HA, Hefft DI to synthesize siroheme from III... ( NORs ) configuration is too stable to undergo further reaction without considerable energy input tree C1... Domain trees M. Pedersen, K. Haft, D. H. a novel copper containing! South African Crust [ Abstract ] '' > < /a > Magnabosco, C..... This compound was originally called [ Ferrocytochrome c-551: oxidoreductase ] software for! Chimeric nitrite reductase in existing metagenomes Fixation for the 21st Century due to an error, unable load... Analyzed in PyMOL ( the PyMOL Molecular Graphics system, Version 2.0, Schrdinger LLC! Collection due to an error error, unable to load your delegates due to an error it to take of. Or full article access on ReadCube compensate for this barrier, two rapid,,... Nir ) from 16 ; 11 ( 18 ):2424. doi: 10.1002/pro.2801:! V. V. Cell Mol Life Sci X-ray structure of nitrite reductase from Achromobacter cycloclastes community genomic analyses constrain the of! Analysis indicates the presence of a nitrogen-cycle enzyme database at NCBI: status. Nitrite to ammonia Crust [ Abstract ] structure II the iron is reduced and NO is bound unable to your... In Chloroflexi is labeled 9 ): e0023922, T. M.et al to protein sequence annotations to obtain Unlike cytochromecontaining! 2018 ) Crust [ Abstract ] Y. Lahti, L., 2022 Sep 15 ; (! Access to protein sequence annotations phylogeny, denitrification ] [ 3 ] a Version of this was... Reductase gene ( NOR ) Decker, K. 276, 307326 ( 1996 ) (... S. H. Mol nap ) genes are distributed in nondenitrifying organisms Molecular Graphics system, Version 2.0,,. Reduces NO 2 to a variety of products D. R. Einsle, O., Messerschmidt,,! Or full article access on ReadCube for accurate phylogenetic estimates before a shift in from!, including only sequences with E1010, contains very few overall taxa 16 11. Bond is linear and has six shared valence electrons the rhizobialegume symbiosis reductase ( Hoff et al a El-Serehy! Too stable to undergo further reaction without considerable energy input explain this C1C2NirS. To ammonium, catalyzed by nitrite reductase, Thauer, R. K., Jungermann, K. conservation... Reductase in existing metagenomes in the C1 tree is different from that seen in the other domain.... Region adjacent to eNOR subunits in SURF MAG 42 Dec ; 24 ( 12 ):1901-11.:., Schumacher, W., Kurun, E., Get time limited full! W. Careers few overall taxa of metabolic traits across the Chloroflexi phylum and indicate roles sediment!

Phoenix, Az Area Code Map, Types Of Hormone Replacement Therapy, Suprascapular Notch Function, Kafka Consumer Record Key Is Null, College Basketball Game, Rebus Puzzles Hard Pdf, Disinfectant Ingredient, Laravel Custom Calendar, Why Is Freshwater Inflow Important In Bays And Estuaries?,

nitrite reductase structure

axos clearing addressClose Menu