Respiratory nitrate reductase 1 alpha chain

Details

Name
Respiratory nitrate reductase 1 alpha chain
Synonyms
  • 1.7.99.4
  • bisD
  • narC
  • Nitrate reductase A subunit alpha
  • Quinol-nitrate oxidoreductase subunit alpha
Gene Name
narG
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0012658|Respiratory nitrate reductase 1 alpha chain
MSKFLDRFRYFKQKGETFADGHGQLLNTNRDWEDGYRQRWQHDKIVRSTHGVNCTGSCSW
KIYVKNGLVTWETQQTDYPRTRPDLPNHEPRGCPRGASYSWYLYSANRLKYPMMRKRLMK
MWREAKALHSDPVEAWASIIEDADKAKSFKQARGRGGFVRSSWQEVNELIAASNVYTIKN
YGPDRVAGFSPIPAMSMVSYASGARYLSLIGGTCLSFYDWYCDLPPASPQTWGEQTDVPE
SADWYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTVAVTPDYAEIAKLCDLWLAPKQ
GTDAAMALAMGHVMLREFHLDNPSQYFTDYVRRYTDMPMLVMLEERDGYYAAGRMLRAAD
LVDALGQENNPEWKTVAFNTNGEMVAPNGSIGFRWGEKGKWNLEQRDGKTGEETELQLSL
LGSQDEIAEVGFPYFGGDGTEHFNKVELENVLLHKLPVKRLQLADGSTALVTTVYDLTLA
NYGLERGLNDVNCATSYDDVKAYTPAWAEQITGVSRSQIIRIAREFADNADKTHGRSMII
VGAGLNHWYHLDMNYRGLINMLIFCGCVGQSGGGWAHYVGQEKLRPQTGWQPLAFALDWQ
RPARHMNSTSYFYNHSSQWRYETVTAEELLSPMADKSRYTGHLIDFNVRAERMGWLPSAP
QLGTNPLTIAGEAEKAGMNPVDYTVKSLKEGSIRFAAEQPENGKNHPRNLFIWRSNLLGS
SGKGHEFMLKYLLGTEHGIQGKDLGQQGGVKPEEVDWQDNGLEGKLDLVVTLDFRLSSTC
LYSDIILPTATWYEKDDMNTSDMHPFIHPLSAAVDPAWEAKSDWEIYKAIAKKFSEVCVG
HLGKETDIVTLPIQHDSAAELAQPLDVKDWKKGECDLIPGKTAPHIMVVERDYPATYERF
TSIGPLMEKIGNGGKGIAWNTQSEMDLLRKLNYTKAEGPAKGQPMLNTAIDAAEMILTLA
PETNGQVAVKAWAALSEFTGRDHTHLALNKEDEKIRFRDIQAQPRKIISSPTWSGLEDEH
VSYNAGYTNVHELIPWRTLSGRQQLYQDHQWMRDFGESLLVYRPPIDTRSVKEVIGQKSN
GNQEKALNFLTPHQKWGIHSTYSDNLLMLTLGRGGPVVWLSEADAKDLGIADNDWIEVFN
SNGALTARAVVSQRVPAGMTMMYHAQERIVNLPGSEITQQRGGIHNSVTRITPKPTHMIG
GYAHLAYGFNYYGTVGSNRDEFVVVRKMKNIDWLDGEGNDQVQESVK
Number of residues
1247
Molecular Weight
140488.49
Theoretical pI
6.47
GO Classification
Functions
4 iron, 4 sulfur cluster binding / electron carrier activity / molybdenum ion binding / molybdopterin cofactor binding / NADH dehydrogenase activity / nitrate reductase activity
Processes
anaerobic respiration / nitrate assimilation / nitrate metabolic process
Components
intrinsic component of membrane / intrinsic component of the cytoplasmic side of the plasma membrane / membrane / NarGHI complex
General Function
Nitrate reductase activity
Specific Function
The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The alpha chain is the actual site of nitrate reduction.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cell membrane
Gene sequence
>lcl|BSEQ0012659|Respiratory nitrate reductase 1 alpha chain (narG)
ATGAGTAAATTCCTGGACCGGTTTCGCTACTTCAAACAGAAGGGTGAAACCTTTGCCGAT
GGGCATGGCCAGCTTCTCAATACCAACCGTGACTGGGAGGATGGATATCGCCAGCGTTGG
CAGCATGACAAAATCGTCCGCTCTACCCACGGGGTAAACTGCACCGGCTCCTGCAGCTGG
AAAATCTACGTCAAAAACGGTCTGGTCACCTGGGAAACCCAGCAGACTGACTATCCGCGT
ACCCGTCCGGATCTGCCAAACCATGAACCTCGCGGCTGCCCGCGCGGTGCCAGCTACTCC
TGGTATCTTTACAGTGCCAACCGCCTGAAATACCCGATGATGCGCAAACGCCTGATGAAA
ATGTGGCGTGAAGCGAAGGCGCTGCATAGCGATCCGGTTGAGGCATGGGCTTCTATCATT
GAAGACGCCGATAAAGCGAAAAGCTTTAAGCAGGCGCGTGGACGCGGTGGATTTGTTCGT
TCTTCCTGGCAGGAGGTGAACGAACTGATCGCCGCATCTAACGTTTACACCATCAAAAAC
TACGGCCCGGACCGTGTTGCTGGTTTCTCGCCAATTCCGGCAATGTCGATGGTTTCTTAC
GCATCGGGTGCACGCTATCTCTCGCTGATTGGCGGTACTTGCTTAAGCTTCTACGACTGG
TACTGCGACTTGCCTCCTGCGTCTCCGCAAACCTGGGGCGAGCAAACTGACGTACCGGAA
TCTGCTGACTGGTACAACTCCAGCTACATCATCGCCTGGGGGTCAAACGTGCCGCAGACG
CGTACCCCGGATGCTCACTTCTTTACTGAAGTGCGTTACAAAGGGACCAAAACTGTTGCC
GTCACACCAGACTACGCTGAAATCGCCAAACTGTGCGATCTGTGGCTGGCACCGAAACAG
GGCACCGATGCGGCAATGGCGCTGGCGATGGGCCACGTAATGCTGCGTGAATTCCACCTC
GACAACCCAAGCCAGTATTTCACCGACTATGTGCGTCGCTACACCGACATGCCGATGCTG
GTGATGCTGGAAGAACGCGACGGTTACTACGCTGCAGGTCGTATGCTGCGCGCTGCTGAT
CTGGTTGATGCGCTGGGCCAGGAAAACAATCCGGAATGGAAAACTGTCGCCTTTAATACC
AATGGCGAAATGGTTGCGCCGAACGGTTCTATTGGCTTCCGCTGGGGCGAGAAGGGCAAA
TGGAATCTTGAGCAGCGCGACGGCAAAACTGGCGAAGAAACCGAGCTGCAACTGAGCCTG
CTGGGTAGCCAGGATGAGATCGCTGAGGTAGGCTTCCCGTACTTTGGTGGCGACGGCACG
GAACACTTCAACAAAGTGGAACTGGAAAACGTGCTGCTGCACAAACTGCCGGTGAAACGC
CTGCAACTGGCTGATGGCAGCACCGCCCTGGTGACCACCGTTTATGATCTGACGCTGGCA
AACTACGGTCTGGAACGTGGCCTGAACGACGTTAACTGTGCAACCAGCTATGACGATGTG
AAAGCTTATACCCCGGCCTGGGCCGAGCAGATTACCGGCGTTTCTCGCAGCCAGATTATT
CGCATCGCCCGTGAATTTGCCGATAACGCTGATAAAACGCACGGTCGTTCGATGATTATC
GTCGGTGCGGGGCTGAACCACTGGTATCACCTCGATATGAACTATCGTGGTCTGATCAAC
ATGCTGATTTTCTGCGGCTGTGTCGGTCAGAGCGGGGGCGGCTGGGCGCACTATGTAGGT
CAGGAAAAACTGCGTCCGCAAACCGGCTGGCAGCCGCTGGCGTTTGCCCTTGACTGGCAG
CGTCCGGCGCGTCACATGAACAGCACTTCTTATTTCTATAACCACTCCAGCCAGTGGCGT
TATGAAACCGTCACGGCGGAAGAGTTGCTGTCACCGATGGCGGACAAATCCCGCTATACC
GGACACTTGATCGACTTTAACGTCCGTGCGGAACGCATGGGCTGGCTGCCGTCTGCACCG
CAGTTAGGCACTAACCCGCTGACTATCGCTGGCGAAGCGGAAAAAGCCGGGATGAATCCG
GTGGACTATACGGTGAAATCCCTGAAAGAGGGTTCCATCCGTTTTGCGGCAGAACAACCA
GAAAACGGTAAAAACCACCCGCGCAACCTGTTCATCTGGCGTTCTAACCTGCTCGGTTCT
TCCGGTAAAGGTCATGAGTTTATGCTCAAGTACCTGCTGGGGACGGAGCACGGTATCCAG
GGTAAAGATCTGGGGCAACAGGGCGGCGTGAAGCCGGAAGAAGTGGACTGGCAGGACAAT
GGTCTGGAAGGCAAGCTGGATCTGGTGGTTACGCTGGACTTCCGTCTGTCGAGCACCTGT
CTCTATTCCGACATCATTTTGCCGACGGCGACCTGGTACGAAAAAGACGACATGAATACT
TCGGATATGCATCCGTTTATTCACCCGCTGTCTGCGGCGGTCGATCCGGCCTGGGAAGCG
AAAAGCGACTGGGAAATCTACAAAGCCATCGCGAAGAAATTCTCCGAAGTGTGCGTCGGC
CATCTGGGTAAAGAAACCGACATCGTCACGCTGCCTATCCAGCATGACTCTGCCGCTGAA
CTGGCGCAGCCGCTGGATGTGAAAGACTGGAAAAAAGGCGAGTGCGACCTGATCCCAGGT
AAAACCGCGCCACACATTATGGTCGTAGAGCGCGATTATCCGGCGACTTACGAACGCTTT
ACCTCTATCGGCCCGCTGATGGAGAAAATCGGTAATGGCGGTAAAGGGATTGCCTGGAAC
ACCCAGAGCGAGATGGATCTGCTGCGTAAGCTCAACTACACCAAAGCGGAAGGTCCGGCG
AAAGGCCAGCCGATGCTGAACACCGCAATTGATGCGGCAGAGATGATCCTGACACTGGCA
CCGGAAACCAACGGTCAGGTAGCCGTGAAAGCCTGGGCTGCCCTGAGCGAATTTACCGGT
CGTGACCATACGCATCTGGCGCTGAATAAAGAAGACGAGAAGATCCGCTTCCGCGATATT
CAGGCACAGCCGCGCAAAATTATCTCCAGCCCGACCTGGTCTGGTCTGGAAGATGAACAC
GTTTCTTACAACGCCGGTTACACCAACGTTCACGAGCTGATCCCATGGCGTACGCTCTCT
GGTCGTCAGCAACTGTATCAGGATCACCAGTGGATGCGTGATTTCGGTGAAAGCCTGCTG
GTTTATCGTCCGCCGATCGACACCCGTTCGGTGAAAGAAGTGATAGGCCAGAAATCCAAC
GGCAACCAGGAAAAAGCGCTCAACTTCCTGACGCCGCACCAGAAGTGGGGTATCCACTCC
ACCTACAGCGACAACCTGCTGATGCTGACTTTAGGTCGCGGTGGTCCGGTGGTCTGGTTG
AGTGAAGCCGATGCCAAAGATCTGGGTATCGCCGATAACGACTGGATTGAAGTCTTCAAC
AGCAACGGTGCTCTGACTGCCCGTGCGGTTGTCAGCCAGCGTGTTCCGGCAGGGATGACC
ATGATGTACCACGCGCAGGAACGTATCGTTAACCTGCCTGGTTCGGAAATTACCCAACAG
CGTGGTGGTATCCATAACTCGGTCACCCGTATCACGCCGAAACCGACGCATATGATCGGC
GGCTATGCCCATCTGGCATACGGCTTTAACTACTATGGCACCGTAGGTTCTAACCGCGAT
GAGTTTGTTGTAGTGCGTAAGATGAAGAACATTGACTGGTTAGATGGCGAAGGCAATGAC
CAGGTACAGGAGAGCGTAAAATGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP09152
UniProtKB Entry NameNARG_ECOLI
GenBank Protein ID42086
GenBank Gene IDX16181
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. Blasco F, Iobbi C, Ratouchniak J, Bonnefoy V, Chippaux M: Nitrate reductases of Escherichia coli: sequence of the second nitrate reductase and comparison with that encoded by the narGHJI operon. Mol Gen Genet. 1990 Jun;222(1):104-11. [Article]
  3. 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]
  4. 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]
  5. 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]
  6. McPherson MJ, Baron AJ, Pappin DJ, Wootton JC: Respiratory nitrate reductase of Escherichia coli. Sequence identification of the large subunit gene. FEBS Lett. 1984 Nov 19;177(2):260-4. [Article]
  7. Li S, Rabi T, DeMoss JA: Delineation of two distinct regulatory domains in the 5' region of the nar operon of Escherichia coli. J Bacteriol. 1985 Oct;164(1):25-32. [Article]
  8. Noji S, Nohno T, Saito T, Taniguchi S: The narK gene product participates in nitrate transport induced in Escherichia coli nitrate-respiring cells. FEBS Lett. 1989 Jul 31;252(1-2):139-43. [Article]
  9. Li SF, DeMoss JA: Promoter region of the nar operon of Escherichia coli: nucleotide sequence and transcription initiation signals. J Bacteriol. 1987 Oct;169(10):4614-20. [Article]
  10. 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]
  11. Magalon A, Asso M, Guigliarelli B, Rothery RA, Bertrand P, Giordano G, Blasco F: Molybdenum cofactor properties and [Fe-S] cluster coordination in Escherichia coli nitrate reductase A: investigation by site-directed mutagenesis of the conserved his-50 residue in the NarG subunit. Biochemistry. 1998 May 19;37(20):7363-70. [Article]
  12. Blasco F, Dos Santos JP, Magalon A, Frixon C, Guigliarelli B, Santini CL, Giordano G: NarJ is a specific chaperone required for molybdenum cofactor assembly in nitrate reductase A of Escherichia coli. Mol Microbiol. 1998 May;28(3):435-47. [Article]
  13. Chan CS, Howell JM, Workentine ML, Turner RJ: Twin-arginine translocase may have a role in the chaperone function of NarJ from Escherichia coli. Biochem Biophys Res Commun. 2006 Apr 28;343(1):244-51. Epub 2006 Mar 3. [Article]
  14. Vergnes A, Pommier J, Toci R, Blasco F, Giordano G, Magalon A: NarJ chaperone binds on two distinct sites of the aponitrate reductase of Escherichia coli to coordinate molybdenum cofactor insertion and assembly. J Biol Chem. 2006 Jan 27;281(4):2170-6. Epub 2005 Nov 14. [Article]
  15. Zakian S, Lafitte D, Vergnes A, Pimentel C, Sebban-Kreuzer C, Toci R, Claude JB, Guerlesquin F, Magalon A: Basis of recognition between the NarJ chaperone and the N-terminus of the NarG subunit from Escherichia coli nitrate reductase. FEBS J. 2010 Apr;277(8):1886-95. doi: 10.1111/j.1742-4658.2010.07611.x. Epub 2010 Mar 2. [Article]
  16. 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]
  17. 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