Respiratory nitrate reductase 1 beta chain

Details

Name
Respiratory nitrate reductase 1 beta chain
Synonyms
  • 1.7.99.4
  • Nitrate reductase A subunit beta
  • Quinol-nitrate oxidoreductase subunit beta
Gene Name
narH
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0012660|Respiratory nitrate reductase 1 beta chain
MKIRSQVGMVLNLDKCIGCHTCSVTCKNVWTSREGVEYAWFNNVETKPGQGFPTDWENQE
KYKGGWIRKINGKLQPRMGNRAMLLGKIFANPHLPGIDDYYEPFDFDYQNLHTAPEGSKS
QPIARPRSLITGERMAKIEKGPNWEDDLGGEFDKLAKDKNFDNIQKAMYSQFENTFMMYL
PRLCEHCLNPACVATCPSGAIYKREEDGIVLIDQDKCRGWRMCITGCPYKKIYFNWKSGK
SEKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADAIERAASTENEKDLYQRQLDVF
LDPNDPKVIEQAIKDGIPLSVIEAAQQSPVYKMAMEWKLALPLHPEYRTLPMVWYVPPLS
PIQSAADAGELGSNGILPDVESLRIPVQYLANLLTAGDTKPVLRALKRMLAMRHYKRAET
VDGKVDTRALEEVGLTEAQAQEMYRYLAIANYEDRFVVPSSHRELAREAFPEKNGCGFTF
GDGCHGSDTKFNLFNSRRIDAIDVTSKTEPHP
Number of residues
512
Molecular Weight
58065.915
Theoretical pI
6.76
GO Classification
Functions
3 iron, 4 sulfur cluster binding / 4 iron, 4 sulfur cluster binding / electron carrier activity / metal ion binding / nitrate reductase activity / oxidoreductase activity
Processes
anaerobic respiration / nitrate assimilation / nitrate metabolic process
Components
cytoplasm / intrinsic component of membrane / intrinsic component of the cytoplasmic side of the plasma membrane / membrane / NarGHI complex
General Function
Oxidoreductase activity
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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cell membrane
Gene sequence
>lcl|BSEQ0012661|Respiratory nitrate reductase 1 beta chain (narH)
ATGAAAATTCGTTCACAAGTCGGCATGGTGCTGAATCTCGATAAGTGCATCGGCTGCCAC
ACCTGTTCAGTTACCTGTAAAAACGTCTGGACCAGCCGTGAAGGCGTGGAATATGCGTGG
TTCAACAACGTGGAAACCAAGCCGGGCCAGGGCTTCCCGACTGACTGGGAAAACCAGGAA
AAATACAAAGGCGGCTGGATCCGTAAAATCAACGGCAAACTGCAGCCGCGCATGGGTAAC
CGTGCCATGCTGCTGGGTAAAATCTTCGCTAACCCGCATCTGCCGGGGATCGACGATTAT
TACGAGCCGTTCGATTTTGACTATCAGAACCTGCATACCGCGCCGGAAGGCAGCAAATCG
CAGCCGATTGCCCGTCCGCGTTCGCTGATTACCGGGGAACGGATGGCGAAAATCGAAAAA
GGGCCGAACTGGGAAGATGACCTGGGCGGTGAGTTTGACAAACTGGCGAAAGACAAGAAC
TTCGACAACATCCAGAAGGCGATGTATAGCCAGTTCGAAAACACCTTCATGATGTATTTG
CCGCGCCTGTGCGAACACTGCCTGAACCCGGCATGTGTGGCGACCTGCCCGAGCGGTGCG
ATTTACAAGCGTGAAGAAGATGGCATCGTCCTGATCGACCAGGATAAATGCCGTGGCTGG
CGTATGTGCATCACTGGATGCCCGTACAAAAAAATCTACTTCAACTGGAAGAGCGGTAAG
TCTGAGAAGTGCATCTTCTGCTATCCGCGTATTGAAGCGGGTCAGCCGACCGTGTGCTCA
GAAACCTGTGTCGGTCGTATCCGTTATCTTGGCGTGCTGTTGTACGATGCCGACGCTATT
GAACGTGCAGCCAGCACCGAGAACGAGAAAGATCTTTACCAGCGTCAGCTGGACGTGTTC
CTCGATCCGAACGATCCGAAAGTCATCGAGCAGGCGATTAAAGACGGTATTCCGCTGAGC
GTTATTGAAGCCGCACAGCAGTCGCCGGTTTATAAAATGGCAATGGAATGGAAACTGGCG
CTGCCGCTGCATCCGGAATATCGCACACTGCCGATGGTCTGGTACGTGCCGCCTCTGTCT
CCGATTCAGTCTGCAGCAGACGCGGGTGAGCTGGGTAGCAACGGCATTCTGCCAGACGTC
GAAAGCCTGCGTATTCCGGTACAGTATCTGGCGAATCTGCTGACCGCCGGTGATACCAAA
CCGGTACTGCGCGCACTGAAACGTATGCTGGCGATGCGTCATTACAAACGTGCTGAAACC
GTTGACGGTAAAGTTGATACCCGTGCGCTGGAAGAGGTCGGTCTGACCGAAGCCCAGGCA
CAGGAGATGTACCGTTATCTGGCGATTGCTAACTACGAAGATCGCTTTGTGGTGCCGAGT
AGTCATCGTGAACTGGCACGGGAAGCCTTCCCGGAGAAAAATGGCTGCGGCTTTACCTTT
GGTGATGGCTGCCACGGTTCAGATACCAAATTCAATCTGTTCAACAGCCGTCGTATCGAT
GCCATCGATGTGACCAGCAAAACGGAGCCGCATCCATGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP11349
UniProtKB Entry NameNARH_ECOLI
GenBank Protein ID146919
GenBank Gene IDM20147
General References
  1. Blasco F, Iobbi C, Giordano G, Chippaux M, Bonnefoy V: 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. 1989 Aug;218(2):249-56. [Article]
  2. 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 al.: 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. 1996 Jun 30;3(3):137-55. [Article]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  4. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  5. Sodergren EJ, DeMoss JA: narI region of the Escherichia coli nitrate reductase (nar) operon contains two genes. J Bacteriol. 1988 Apr;170(4):1721-9. [Article]
  6. Sodergren EJ, Hsu PY, DeMoss JA: Roles of the narJ and narI gene products in the expression of nitrate reductase in Escherichia coli. J Biol Chem. 1988 Nov 5;263(31):16156-62. [Article]
  7. Guigliarelli B, Asso M, More C, Augier V, Blasco F, Pommier J, Giordano G, Bertrand P: 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. 1992 Jul 1;207(1):61-8. [Article]
  8. Augier V, Guigliarelli B, Asso M, Bertrand P, Frixon C, Giordano G, Chippaux M, Blasco F: 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. 1993 Mar 2;32(8):2013-23. [Article]
  9. Augier V, Asso M, Guigliarelli B, More C, Bertrand P, Santini CL, Blasco F, Chippaux M, Giordano G: 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. 1993 May 18;32(19):5099-108. [Article]
  10. Guigliarelli B, Magalon A, Asso M, Bertrand P, Frixon C, Giordano G, Blasco F: 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. 1996 Apr 16;35(15):4828-36. [Article]
  11. Rothery RA, Magalon A, Giordano G, Guigliarelli B, Blasco F, Weiner JH: The molybdenum cofactor of Escherichia coli nitrate reductase A (NarGHI). Effect of a mobAB mutation and interactions with [Fe-S] clusters. J Biol Chem. 1998 Mar 27;273(13):7462-9. [Article]
  12. Bertero MG, Rothery RA, Palak M, Hou C, Lim D, Blasco F, Weiner JH, Strynadka NC: Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A. Nat Struct Biol. 2003 Sep;10(9):681-7. Epub 2003 Aug 10. [Article]
  13. Jormakka M, Richardson D, Byrne B, Iwata S: Architecture of NarGH reveals a structural classification of Mo-bisMGD enzymes. Structure. 2004 Jan;12(1):95-104. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB07349(1S)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PENTANOYLOXY)METHYL]ETHYL OCTANOATEexperimentalunknownDetails
DB04464N-FormylmethionineexperimentalunknownDetails