Identification
Name:Respiratory nitrate reductase 1 alpha chain
Synonyms:
  • Nitrate reductase A subunit alpha
  • Quinol-nitrate oxidoreductase subunit alpha
Gene Name:narG
Enzyme Class:
Biological Properties
General Function:Involved in oxidoreductase 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
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
binding
catalytic activity
cation binding
electron carrier activity
ion binding
metal ion binding
molybdenum ion binding
nitrate reductase activity
oxidoreductase activity
oxidoreductase activity, acting on other nitrogenous compounds as donors
transition metal ion binding
Process
metabolic process
nitrate metabolic process
nitrogen compound metabolic process
oxidation reduction
Gene Properties
Blattner:b1224
Gene OrientationClockwise
Centisome Percentage:27.57
Left Sequence End1279087
Right Sequence End1282830
Gene Sequence:
>3744 bp
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
Protein Properties
Pfam Domain Function:
Protein Residues:1247
Protein Molecular Weight:140489
Protein Theoretical pI:6
PDB File:1Q16
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>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
References
External Links:
ResourceLink
Uniprot ID:P09152
Uniprot Name:NARG_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4062800
PDB ID:1Q16
Ecogene ID:EG10638
Ecocyc:EG10638
ColiBase:b1224
Kegg Gene:b1224
EchoBASE ID:EB0632
CCDB:NARG_ECOLI
BacMap:16129187
General Reference:
  • 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., Dos Santos, J. P., Magalon, A., Frixon, C., Guigliarelli, B., Santini, C. L., Giordano, G. (1998). "NarJ is a specific chaperone required for molybdenum cofactor assembly in nitrate reductase A of Escherichia coli." Mol Microbiol 28:435-447. Pubmed: 9632249
  • 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
  • Blasco, F., Iobbi, C., Ratouchniak, J., Bonnefoy, V., Chippaux, M. (1990). "Nitrate reductases of Escherichia coli: sequence of the second nitrate reductase and comparison with that encoded by the narGHJI operon." Mol Gen Genet 222:104-111. Pubmed: 2233673
  • 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
  • Chan, C. S., Howell, J. M., Workentine, M. L., Turner, R. J. (2006). "Twin-arginine translocase may have a role in the chaperone function of NarJ from Escherichia coli." Biochem Biophys Res Commun 343:244-251. Pubmed: 16540088
  • 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
  • Li, S. F., DeMoss, J. A. (1987). "Promoter region of the nar operon of Escherichia coli: nucleotide sequence and transcription initiation signals." J Bacteriol 169:4614-4620. Pubmed: 3308846
  • Li, S., Rabi, T., DeMoss, J. A. (1985). "Delineation of two distinct regulatory domains in the 5' region of the nar operon of Escherichia coli." J Bacteriol 164:25-32. Pubmed: 2995309
  • Magalon, A., Asso, M., Guigliarelli, B., Rothery, R. A., Bertrand, P., Giordano, G., Blasco, F. (1998). "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 37:7363-7370. Pubmed: 9585550
  • McPherson, M. J., Baron, A. J., Pappin, D. J., Wootton, J. C. (1984). "Respiratory nitrate reductase of Escherichia coli. Sequence identification of the large subunit gene." FEBS Lett 177:260-264. Pubmed: 6094247
  • Noji, S., Nohno, T., Saito, T., Taniguchi, S. (1989). "The narK gene product participates in nitrate transport induced in Escherichia coli nitrate-respiring cells." FEBS Lett 252:139-143. Pubmed: 2668029
  • 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
  • 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
  • Vergnes, A., Pommier, J., Toci, R., Blasco, F., Giordano, G., Magalon, A. (2006). "NarJ chaperone binds on two distinct sites of the aponitrate reductase of Escherichia coli to coordinate molybdenum cofactor insertion and assembly." J Biol Chem 281:2170-2176. Pubmed: 16286471
  • Zakian, S., Lafitte, D., Vergnes, A., Pimentel, C., Sebban-Kreuzer, C., Toci, R., Claude, J. B., Guerlesquin, F., Magalon, A. (2010). "Basis of recognition between the NarJ chaperone and the N-terminus of the NarG subunit from Escherichia coli nitrate reductase." FEBS J 277:1886-1895. Pubmed: 20236317