Identification
Name:NADH-quinone oxidoreductase subunit G
Synonyms:
  • NADH dehydrogenase I subunit G
  • NDH-1 subunit G
  • NUO7
Gene Name:nuoG
Enzyme Class:
Biological Properties
General Function:Involved in electron carrier activity
Specific Function:NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient
Cellular Location:Cytoplasm. Cell inner membrane; Peripheral membrane protein
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
Thumb+AcceptorThumb+Reduced acceptor
Ubiquinol-8 + Acceptor ↔ Ubiquinone-1 + Reduced acceptor
ReactionCard
Thumb+ThumbThumb+Thumb
SMPDB Reactions:
Thumb+5 Thumb+ThumbThumb+Thumb+Thumb
Thumb+4 Thumb+2 Thumb+menaquinone-8 ? Thumb+Thumb+Thumb+Electron+4 Thumb
"a menaquinone"+4 Thumb+Thumb"a menaquinol"+Thumb
"a menaquinone" + 4 Hydrogen ion + NADH → "a menaquinol" + NAD
ReactionCard
4 Thumb+Thumb+"a menaquinone"Thumb+"a menaquinol"
4 Hydrogen ion + NADH + "a menaquinone" → NAD + "a menaquinol"
ReactionCard
Complex Reactions:
Thumb+4 Thumb+ThumbThumb+Thumb+3 Thumb
4 Thumb+Thumb+ThumbThumb+Thumb+3 Thumb
4 Thumb+Menaquinone 8+ThumbThumb+Thumb+3 Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Metabolites:
ECMDB IDNameView
ECMDB211542-Demethylmenaquinol 8MetaboCard
ECMDB211552-Demethylmenaquinone 8MetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB02434HydroquinoneMetaboCard
ECMDB21245Menaquinol 8MetaboCard
ECMDB00902NADMetaboCard
ECMDB01487NADHMetaboCard
ECMDB23060QuinoneMetaboCard
ECMDB21574Ubiquinol-1MetaboCard
ECMDB01060Ubiquinol-8MetaboCard
ECMDB21438Ubiquinone-1MetaboCard
ECMDB21296Ubiquinone-8MetaboCard
GO Classification:
Component
cell part
membrane
Function
binding
catalytic activity
cation binding
electron carrier activity
ion binding
iron-sulfur cluster binding
metal cluster binding
metal ion binding
molybdenum ion binding
NADH dehydrogenase (quinone) activity
NADH dehydrogenase (ubiquinone) activity
NADH dehydrogenase activity
oxidoreductase activity
oxidoreductase activity, acting on NADH or NADPH
transition metal ion binding
Process
ATP synthesis coupled electron transport
cellular metabolic process
electron transport chain
generation of precursor metabolites and energy
metabolic process
oxidation reduction
respiratory electron transport chain
Gene Properties
Blattner:b2283
Gene OrientationCounterclockwise
Centisome Percentage:51.63
Left Sequence End2395461
Right Sequence End2398187
Gene Sequence:
>2733 bp
ATGCTAATGGCTACAATTCATGTAGACGGCAAAGAATACGAGGTCAACGGAGCGGACAAC
CTGCTGGAAGCTTGTCTGTCTCTGGGCCTTGATATTCCTTACTTTTGCTGGCATCCGGCG
CTGGGAAGTGTCGGTGCTTGCCGCCAGTGTGCGGTGAAGCAATACCAAAACGCGGAAGAC
ACGCGTGGTCGCCTGGTGATGTCCTGTATGACACCGGCTTCCGATGGCACCTTTATTTCC
ATTGACGACGAAGAAGCGAAACAGTTCCGTGAAAGCGTGGTCGAGTGGTTGATGACCAAC
CACCCGCACGACTGTCCGGTATGTGAAGAGGGCGGTAACTGCCATCTTCAGGATATGACT
GTGATGACCGGACACAGCTTCCGTCGCTACCGTTTCACCAAACGTACCCACCGTAATCAG
GATTTGGGGCCATTCATCTCTCACGAAATGAACCGCTGCATCGCCTGCTACCGCTGTGTG
CGTTACTACAAAGATTACGCTGACGGTACAGATCTGGGCGTTTACGGTGCGCACGACAAC
GTCTACTTCGGTCGCCCGGAAGACGGCACGCTGGAAAGCGAATTTTCCGGTAACCTGGTC
GAAATTTGCCCGACCGGCGTATTTACCGACAAAACGCACTCCGAGCGTTACAACCGTAAA
TGGGATATGCAGTTTGCGCCGAGCATCTGCCAGCAATGTTCCATCGGCTGTAACATCAGC
CCCGGTGAACGTTACGGCGAACTGCGTCGTATCGAAAACCGTTACAACGGTACGGTAAAC
CACTACTTCCTCTGCGACCGTGGTCGTTTCGGTTACGGTTACGTCAACCTGAAGGATCGT
CCGCGTCAGCCAGTACAGCGTCGTGGCGATGATTTCATTACCCTCAACGCCGAACAGGCA
ATGCAGGGCGCGGCAGATATTCTGCGTCAGTCGAAGAAAGTGATCGGTATTGGTTCTCCG
CGTGCCAGCGTGGAAAGCAACTTTGCGCTGCGTGAACTGGTGGGCGAAGAAAACTTCTAC
ACCGGTATCGCTCACGGTGAGCAGGAACGTCTGCAACTGGCGCTGAAAGTGCTGCGTGAA
GGCGGCATTTATACTCCGGCTCTGCGCGAAATCGAATCTTACGATGCGGTACTGGTGCTG
GGCGAAGACGTTACCCAGACCGGCGCGCGCGTCGCGCTGGCAGTGCGTCAGGCTGTGAAA
GGTAAAGCGCGCGAAATGGCGGCAGCACAGAAAGTGGCTGACTGGCAGATTGCGGCAATC
CTCAACATCGGTCAACGTGCGAAGCATCCGCTGTTTGTTACCAACGTTGATGACACCCGT
CTGGATGATATCGCGGCGTGGACTTACCGCGCACCGGTTGAAGATCAGGCGCGTTTAGGT
TTTGCCATCGCCCATGCGCTGGATAACTCTGCACCAGCGGTTGACGGTATCGAACCTGAG
CTGCAAAGCAAAATCGACGTCATCGTGCAGGCACTGGCAGGTGCGAAGAAACCGTTGATT
ATCTCCGGGACGAACGCCGGTAGCTTAGAGGTGATTCAGGCGGCGGCTAACGTCGCGAAA
GCCCTGAAAGGTCGCGGCGCTGACGTCGGTATCACCATGATTGCCCGTTCCGTCAACAGC
ATGGGGCTGGGCATTATGGGTGGCGGTTCGCTTGAAGAAGCGTTAACCGAACTGGAAACC
GGACGCGCCGACGCGGTGGTGGTGTTGGAAAACGATCTGCATCGTCACGCTTCTGCTATC
CGCGTGAATGCTGCGCTGGCTAAAGCACCGCTGGTGATGGTGGTTGATCATCAACGCACA
GCGATTATGGAAAACGCCCATCTGGTACTTTCTGCTGCCAGCTTTGCTGAAAGCGACGGT
ACGGTGATCAACAACGAAGGCCGCGCCCAACGTTTCTTCCAGGTTTACGATCCTGCTTAT
TACGACAGCAAAACTGTCATGCTGGAAAGCTGGCGCTGGTTACACTCGCTGCACAGCACC
CTGCTGAGCCGTGAAGTGGACTGGACGCAGCTCGACCATGTGATTGACGCTGTTGTGGCG
AAAATCCCGGAACTGGCAGGTATCAAAGATGCTGCGCCGGATGCGACATTCCGTATTCGT
GGGCAGAAACTGGCCCGTGAACCGCACCGTTACAGCGGTCGTACCGCCATGCGCGCCAAT
ATCAGCGTTCATGAGCCGCGTCAGCCGCAGGATATTGACACCATGTTCACCTTCTCGATG
GAAGGTAACAACCAGCCGACTGCGCACCGTTCGCAAGTGCCGTTTGCCTGGGCGCCGGGC
TGGAACTCCCCGCAGGCGTGGAACAAATTCCAGGACGAAGTGGGCGGCAAACTGCGCTTT
GGCGATCCGGGCGTGCGTCTGTTTGAAACCAGCGAAAATGGTCTGGATTACTTCACCAGC
GTACCGGCACGCTTCCAGCCGCAGGACGGGAAATGGCGTATCGCGCCGTATTACCACCTG
TTTGGCAGCGATGAATTGTCACAGCGTGCTCCGGTCTTCCAGAGCCGTATGCCGCAGCCG
TACATCAAACTCAACCCAGCGGATGCCGCGAAGTTGGGTGTGAACGCAGGTACACGCGTC
TCCTTTAGTTACGATGGCAACACGGTCACGCTGCCGGTTGAAATCGCCGAAGGACTGACG
GCAGGGCAGGTGGGCTTGCCGATGGGTATGTCCGGCATTGCTCCGGTGCTGGCTGGCGCG
CATCTTGAGGATCTCAAGGAGGCACAACAATGA
Protein Properties
Pfam Domain Function:
Protein Residues:908
Protein Molecular Weight:100298
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>NADH-quinone oxidoreductase subunit G
MATIHVDGKEYEVNGADNLLEACLSLGLDIPYFCWHPALGSVGACRQCAVKQYQNAEDTR
GRLVMSCMTPASDGTFISIDDEEAKQFRESVVEWLMTNHPHDCPVCEEGGNCHLQDMTVM
TGHSFRRYRFTKRTHRNQDLGPFISHEMNRCIACYRCVRYYKDYADGTDLGVYGAHDNVY
FGRPEDGTLESEFSGNLVEICPTGVFTDKTHSERYNRKWDMQFAPSICQQCSIGCNISPG
ERYGELRRIENRYNGTVNHYFLCDRGRFGYGYVNLKDRPRQPVQRRGDDFITLNAEQAMQ
GAADILRQSKKVIGIGSPRASVESNFALRELVGEENFYTGIAHGEQERLQLALKVLREGG
IYTPALREIESYDAVLVLGEDVTQTGARVALAVRQAVKGKAREMAAAQKVADWQIAAILN
IGQRAKHPLFVTNVDDTRLDDIAAWTYRAPVEDQARLGFAIAHALDNSAPAVDGIEPELQ
SKIDVIVQALAGAKKPLIISGTNAGSLEVIQAAANVAKALKGRGADVGITMIARSVNSMG
LGIMGGGSLEEALTELETGRADAVVVLENDLHRHASAIRVNAALAKAPLVMVVDHQRTAI
MENAHLVLSAASFAESDGTVINNEGRAQRFFQVYDPAYYDSKTVMLESWRWLHSLHSTLL
SREVDWTQLDHVIDAVVAKIPELAGIKDAAPDATFRIRGQKLAREPHRYSGRTAMRANIS
VHEPRQPQDIDTMFTFSMEGNNQPTAHRSQVPFAWAPGWNSPQAWNKFQDEVGGKLRFGD
PGVRLFETSENGLDYFTSVPARFQPQDGKWRIAPYYHLFGSDELSQRAPVFQSRMPQPYI
KLNPADAAKLGVNAGTRVSFSYDGNTVTLPVEIAEGLTAGQVGLPMGMSGIAPVLAGAHL
EDLKEAQQ
References
External Links:
ResourceLink
Uniprot ID:P33602
Uniprot Name:NUOG_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85675343
Ecogene ID:EG12087
Ecocyc:EG12087
ColiBase:b2283
Kegg Gene:b2283
EchoBASE ID:EB2011
CCDB:NUOG_ECOLI
BacMap:145698290
General Reference:
  • 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
  • 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
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
  • Pruss, B. M., Nelms, J. M., Park, C., Wolfe, A. J. (1994). "Mutations in NADH:ubiquinone oxidoreductase of Escherichia coli affect growth on mixed amino acids." J Bacteriol 176:2143-2150. Pubmed: 8157582
  • Stenberg, F., Chovanec, P., Maslen, S. L., Robinson, C. V., Ilag, L. L., von Heijne, G., Daley, D. O. (2005). "Protein complexes of the Escherichia coli cell envelope." J Biol Chem 280:34409-34419. Pubmed: 16079137
  • Weidner, U., Geier, S., Ptock, A., Friedrich, T., Leif, H., Weiss, H. (1993). "The gene locus of the proton-translocating NADH: ubiquinone oxidoreductase in Escherichia coli. Organization of the 14 genes and relationship between the derived proteins and subunits of mitochondrial complex I." J Mol Biol 233:109-122. Pubmed: 7690854
  • Yamamoto, Y., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kimura, S., Kitagawa, M., Makino, K., Miki, T., Mitsuhashi, N., Mizobuchi, K., Mori, H., Nakade, S., Nakamura, Y., Nashimoto, H., Oshima, T., Oyama, S., Saito, N., Sampei, G., Satoh, Y., Sivasundaram, S., Tagami, H., Horiuchi, T., et, a. l. .. (1997). "Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." DNA Res 4:91-113. Pubmed: 9205837