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
- Functions4 iron, 4 sulfur cluster binding / electron carrier activity / molybdenum ion binding / molybdopterin cofactor binding / NADH dehydrogenase activity / nitrate reductase activityProcessesanaerobic respiration / nitrate assimilation / nitrate metabolic processComponentsintrinsic 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
Resource Link UniProtKB ID P09152 UniProtKB Entry Name NARG_ECOLI GenBank Protein ID 42086 GenBank Gene ID X16181 - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]