Identification
Name:Respiratory nitrate reductase 1 beta chain
Synonyms:
  • Nitrate reductase A subunit beta
  • Quinol-nitrate oxidoreductase subunit beta
Gene Name:narH
Enzyme Class:
Biological Properties
General Function:Involved in iron-sulfur cluster binding
Specific Function:The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The beta chain is an electron transfer unit containing four cysteine clusters involved in the formation of iron-sulfur centers. Electrons are transferred from the gamma chain to the molybdenum cofactor of the alpha subunit
Cellular Location:Cell membrane; Peripheral membrane protein
SMPDB Pathways:
KEGG Pathways:
  • Microbial metabolism in diverse environments ec01120
  • Nitrogen metabolism ec00910
KEGG Reactions:
1.0Thumb+1.0Acceptor+1.0Thumb+1.0Acceptor1.0Thumb+1.0Reduced acceptor+1.0Reduced acceptor
1.0Nitrite + 1.0Acceptor + 1.0Water + 1.0Acceptor ↔ 1.0Nitrate + 1.0Reduced acceptor + 1.0Reduced acceptor
ReactionCard
2.0Ferricytochrome c+1.0Thumb+1.0Thumb1.0Thumb+2.0Ferrocytochrome c+2.0Thumb
2.0Ferricytochrome c + 1.0Nitrite + 1.0Water ↔ 1.0Nitrate + 2.0Ferrocytochrome c + 2.0Hydrogen ion
ReactionCard
SMPDB Reactions:
1.0Nitrate+1.0cytochrome c nitrite reductase+1.0Thumb1.0Nitrite+1.0cytochrome c nitrite reductase+1.0Thumb+1.0Thumb
1.0Nitrate + 1.0cytochrome c nitrite reductase + 1.0Nitrate ↔ 1.0Nitrite + 1.0cytochrome c nitrite reductase + 1.0Water + 1.0Nitrite
ReactionCard
1.0Thumb+2.0Thumb+2.0Electron1.0Thumb+1.0Thumb
1.0Selenate + 2.0Hydrogen ion + 2.0Electron → 1.0Selenite + 1.0Water
ReactionCard
1.0Thumb+2.0Thumb+1.0a menaquinol1.0Thumb+1.0Thumb+1.0a menaquinone
1.0Nitrate + 2.0Hydrogen ion + 1.0a menaquinol → 1.0Nitrite + 1.0Water + 1.0a menaquinone
ReactionCard
Complex Reactions:
2.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb+2.0Thumb
2.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Menaquinone 8+1.0Thumb+2.0Thumb
2.0Hydrogen ion + 1.0Menaquinol 8 + 1.0Nitrate → 1.0Water + 1.0Menaquinone 8 + 1.0Nitrite + 2.0Hydrogen ion
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB21652Ferricytochrome cMetaboCard
ECMDB23135Ferrocytochrome cMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21245Menaquinol 8MetaboCard
ECMDB02878NitrateMetaboCard
ECMDB02786NitriteMetaboCard
ECMDB23788SelenateMetaboCard
ECMDB21355SeleniteMetaboCard
ECMDB01060Ubiquinol-8MetaboCard
ECMDB21296Ubiquinone-8MetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Component
macromolecular complex
nitrate reductase complex
protein complex
Function
catalytic activity
nitrate reductase activity
oxidoreductase activity
oxidoreductase activity, acting on other nitrogenous compounds as donors
Process
metabolic process
nitrate metabolic process
nitrogen compound metabolic process
oxidation reduction
Gene Properties
Blattner:b1225
Gene OrientationClockwise
Centisome Percentage:27.65
Left Sequence End1282827
Right Sequence End1284365
Gene Sequence:
>1539 bp
ATGGCAAGAGCTGTACACCGTAGTGGGTTAGTGGCGCTGGGCATTGCGACAGCGTTGATG
GCATCTTGTGCATTCGCTGCCAAAGATGTGGTGGTGGCGGTAGGATCGAATTTCACCACG
CTCGATCCGTATGACGCAAATGACACGTTATCTCAGGCCGTAGCGAAATCGTTTTACCAG
GGGCTGTTCGGTCTGGATAAAGAGATGAAACTGAAAAACGTGCTGGCGGAGAGTTATACC
GTTTCCGATGACGGCATTACTTACACCGTGAAATTGCGGGAAGGCATTAAATTCCAGGAT
GGCACCGATTTCAACGCCGCGGCGGTGAAAGCGAATCTGGACCGGGCCAGCGATCCGGCG
AATCATCTTAAACGCTATAACCTGTATAAGAATATTGCTAAAACGGAAGCGATCGATCCG
ACAACGGTAAAGATTACCCTCAAACAGCCGTTCTCAGCGTTTATTAATATTCTTGCCCAT
CCGGCGACCGCGATGATTTCACCGGCAGCGCTGGAAAAATATGGCAAGGAGATTGGTTTT
TATCCGGTGGGAACCGGACCGTATGAACTGGATACCTGGAATCAGACCGATTTTGTGAAG
GTGAAAAAATTCGCGGGTTACTGGCAGCCAGGATTGCCCAAACTGGACAGCATAACCTGG
CGTCCGGTGGCGGATAACAACACCCGCGCGGCAATGCTGCAAACCGGTGAAGCGCAGTTT
GCTTTCCCCATTCCTTACGAGCAGGCCACACTGCTGGAGAAAAACAAAAATATCGAGTTG
ATGGCCAGTCCGTCAATTATGCAGCGTTATATCAGTATGAACGTGACGCAAAAGCCGTTC
GATAACCCGAAGGTCCGTGAGGCGCTGAATTACGCCATTAACCGTCCGGCGCTGGTGAAA
GTTGCCTTTGCGGGCTATGCAACGCCAGCTACTGGTGTGGTACCGCCAAGTATCGCCTAC
GCGCAAAGTTATAAACCGTGGCCTTACGATCCAGTGAAAGCGCGCGAATTACTGAAAGAG
GCGGGATATCCCAACGGTTTCAGTACCACGCTGTGGTCGTCACATAACCACAGCACCGCG
CAGAAAGTGCTGCAATTTACCCAGCAGCAGTTAGCGCAGGTCGGGATTAAAGCCCAGGTG
ACTGCGATGGATGCCGGACAGCGGGCGGCAGAAGTTGAAGGTAAAGGGCAAAAAGAGAGC
GGCGTGCGGATGTTCTACACTGGCTGGTCGGCTTCAACCGGCGAAGCGGACTGGGCACTA
TCGCCGCTGTTTGCCTCGCAGAACTGGCCACCGACGCTGTTTAATACCGCGTTTTACAGC
AATAAACAGGTGGATGACTTCCTGGCTCAGGCACTGAAAACTAATGATCCGGCGGAAAAG
ACCCGCTTATATAAGGCGGCGCAGGATATCATCTGGCAAGAATCGCCGTGGATCCCGCTG
GTGGTAGAAAAACTGGTGTCGGCACACAGTAAAAACCTGACCGGTTTTTGGATCATGCCA
GACACCGGCTTCAGCTTTGAAGACGCGGATTTGCAATAA
Protein Properties
Pfam Domain Function:Not Available
Protein Residues:512
Protein Molecular Weight:58066
Protein Theoretical pI:7
PDB File:1Y5N
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Respiratory nitrate reductase 1 beta chain
MKIRSQVGMVLNLDKCIGCHTCSVTCKNVWTSREGVEYAWFNNVETKPGQGFPTDWENQE
KYKGGWIRKINGKLQPRMGNRAMLLGKIFANPHLPGIDDYYEPFDFDYQNLHTAPEGSKS
QPIARPRSLITGERMAKIEKGPNWEDDLGGEFDKLAKDKNFDNIQKAMYSQFENTFMMYL
PRLCEHCLNPACVATCPSGAIYKREEDGIVLIDQDKCRGWRMCITGCPYKKIYFNWKSGK
SEKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADAIERAASTENEKDLYQRQLDVF
LDPNDPKVIEQAIKDGIPLSVIEAAQQSPVYKMAMEWKLALPLHPEYRTLPMVWYVPPLS
PIQSAADAGELGSNGILPDVESLRIPVQYLANLLTAGDTKPVLRALKRMLAMRHYKRAET
VDGKVDTRALEEVGLTEAQAQEMYRYLAIANYEDRFVVPSSHRELAREAFPEKNGCGFTF
GDGCHGSDTKFNLFNSRRIDAIDVTSKTEPHP
References
External Links:
ResourceLink
Uniprot ID:P11349
Uniprot Name:NARH_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674773
PDB ID:1Y5N
Ecogene ID:EG10639
Ecocyc:EG10639
ColiBase:b1225
Kegg Gene:b1225
EchoBASE ID:EB0633
CCDB:NARH_ECOLI
BacMap:16129188
General Reference:
  • Augier, V., Asso, M., Guigliarelli, B., More, C., Bertrand, P., Santini, C. L., Blasco, F., Chippaux, M., Giordano, G. (1993). "Removal of the high-potential [4Fe-4S] center of the beta-subunit from Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of site-directed mutated enzymes." Biochemistry 32:5099-5108. Pubmed: 8388253
  • Augier, V., Guigliarelli, B., Asso, M., Bertrand, P., Frixon, C., Giordano, G., Chippaux, M., Blasco, F. (1993). "Site-directed mutagenesis of conserved cysteine residues within the beta subunit of Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of the mutated enzymes." Biochemistry 32:2013-2023. Pubmed: 8383531
  • Bertero, M. G., Rothery, R. A., Palak, M., Hou, C., Lim, D., Blasco, F., Weiner, J. H., Strynadka, N. C. (2003). "Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A." Nat Struct Biol 10:681-687. Pubmed: 12910261
  • Blasco, F., Iobbi, C., Giordano, G., Chippaux, M., Bonnefoy, V. (1989). "Nitrate reductase of Escherichia coli: completion of the nucleotide sequence of the nar operon and reassessment of the role of the alpha and beta subunits in iron binding and electron transfer." Mol Gen Genet 218:249-256. Pubmed: 2674654
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Guigliarelli, B., Asso, M., More, C., Augier, V., Blasco, F., Pommier, J., Giordano, G., Bertrand, P. (1992). "EPR and redox characterization of iron-sulfur centers in nitrate reductases A and Z from Escherichia coli. Evidence for a high-potential and a low-potential class and their relevance in the electron-transfer mechanism." Eur J Biochem 207:61-68. Pubmed: 1321049
  • Guigliarelli, B., Magalon, A., Asso, M., Bertrand, P., Frixon, C., Giordano, G., Blasco, F. (1996). "Complete coordination of the four Fe-S centers of the beta subunit from Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of site-directed mutants lacking the highest or lowest potential [4Fe-4S] clusters." Biochemistry 35:4828-4836. Pubmed: 8664273
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Jormakka, M., Richardson, D., Byrne, B., Iwata, S. (2004). "Architecture of NarGH reveals a structural classification of Mo-bisMGD enzymes." Structure 12:95-104. Pubmed: 14725769
  • Oshima, T., Aiba, H., Baba, T., Fujita, K., Hayashi, K., Honjo, A., Ikemoto, K., Inada, T., Itoh, T., Kajihara, M., Kanai, K., Kashimoto, K., Kimura, S., Kitagawa, M., Makino, K., Masuda, S., Miki, T., Mizobuchi, K., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." DNA Res 3:137-155. Pubmed: 8905232
  • Rothery, R. A., Magalon, A., Giordano, G., Guigliarelli, B., Blasco, F., Weiner, J. H. (1998). "The molybdenum cofactor of Escherichia coli nitrate reductase A (NarGHI). Effect of a mobAB mutation and interactions with [Fe-S] clusters." J Biol Chem 273:7462-7469. Pubmed: 9516445
  • Sodergren, E. J., DeMoss, J. A. (1988). "narI region of the Escherichia coli nitrate reductase (nar) operon contains two genes." J Bacteriol 170:1721-1729. Pubmed: 2832376
  • Sodergren, E. J., Hsu, P. Y., DeMoss, J. A. (1988). "Roles of the narJ and narI gene products in the expression of nitrate reductase in Escherichia coli." J Biol Chem 263:16156-16162. Pubmed: 3053688