NADH-quinone oxidoreductase subunit B (P0AFC7)

Identification
Name:NADH-quinone oxidoreductase subunit B
Synonyms:
  • NADH dehydrogenase I subunit B
  • NDH-1 subunit B
  • NUO2
Gene Name:nuoB
Enzyme Class:
Biological Properties
General Function:Involved in NADH dehydrogenase (ubiquinone) 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 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:Cell inner membrane; Peripheral membrane protein; Cytoplasmic side
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Acceptor ↔ 1.0Thumb+1.0Reduced acceptor
1.0Ubiquinol-8 + 1.0Acceptor ↔ 1.0Ubiquinone-1 + 1.0Reduced acceptor
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0NADH + 1.0Ubiquinone-1 ↔ 1.0NAD + 1.0Ubiquinol-8
ReactionCard
SMPDB Reactions:
1.0Thumb+5.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0NADH + 5.0Hydrogen ion + 1.0Ubiquinone-1 → 1.0Hydrogen ion + 1.0NAD + 1.0Ubiquinol-1
ReactionCard
1.0Thumb+4.0Thumb+2.0Thumb+1.0menaquinone-8 ? 1.0Thumb+1.0Thumb+1.0Thumb+1.0Electron+4.0Thumb
1.0NADH + 4.0Hydrogen ion + 2.0Hydrogen ion + 1.0menaquinone-8 ? 1.0NAD + 1.0Hydrogen ion + 1.0Menaquinol 8 + 1.0Electron + 4.0Hydrogen ion
ReactionCard
1.0a menaquinone+4.0Thumb+1.0Thumb → 1.0a menaquinol+1.0Thumb
1.0a menaquinone + 4.0Hydrogen ion + 1.0NADH → 1.0a menaquinol + 1.0NAD
ReactionCard
Complex Reactions:
1.0Thumb+4.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+3.0Thumb
1.02-Demethylmenaquinone 8 + 4.0Hydrogen ion + 1.0NADH → 1.02-Demethylmenaquinol 8 + 1.0NAD + 3.0Hydrogen ion
ReactionCard
4.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+3.0Thumb
4.0Hydrogen ion + 1.0NADH + 1.0Ubiquinone-8 → 1.0NAD + 1.0Ubiquinol-8 + 3.0Hydrogen ion
ReactionCard
4.0Thumb+1.0Menaquinone 8+1.0Thumb → 1.0Thumb+1.0Thumb+3.0Thumb
4.0Hydrogen ion + 1.0Menaquinone 8 + 1.0NADH → 1.0Menaquinol 8 + 1.0NAD + 3.0Hydrogen ion
ReactionCard
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:
Function
4 iron, 4 sulfur cluster binding
binding
catalytic activity
cofactor binding
iron-sulfur cluster binding
metal cluster binding
NADH dehydrogenase (quinone) activity
NADH dehydrogenase (ubiquinone) activity
NADH dehydrogenase activity
oxidoreductase activity
oxidoreductase activity, acting on NADH or NADPH
quinone binding
Process
metabolic process
oxidation reduction
Gene Properties
Blattner:b2287
Gene OrientationCounterclockwise
Centisome Percentage:51.77
Left Sequence End2401973
Right Sequence End2402635
Gene Sequence:
>663 bp
ATGGAACTGTATCTGGATACTTCAGACGTTGTTGCGGTGAAGGCGCTGTCACGTATTTTT
CCGCTGGCGGGTGTGACCACTAACCCAAGCATTATCGCCGCGGGTAAAAAACCGCTGGAT
GTTGTGCTTCCGCAACTTCATGAAGCGATGGGCGGTCAGGGGCGTCTGTTTGCCCAGGTA
ATGGCTACCACTGCCGAAGGGATGGTTAATGACGCGCTTAAGCTGCGTTCTATTATTGCG
GATATCGTGGTGAAAGTTCCGGTGACCGCCGAGGGGCTGGCAGCTATTAAGATGTTAAAA
GCGGAAGGGATTCCGACGCTGGGAACCGCGGTATATGGCGCAGCACAAGGGCTGCTGTCG
GCGCTGGCAGGTGCGGAATATGTTGCGCCTTACGTTAATCGTATTGATGCTCAGGGCGGT
AGCGGCATTCAGACTGTGACCGACTTACACCAGTTATTGAAAATGCATGCGCCGCAGGCG
AAAGTGCTGGCAGCGAGTTTCAAAACCCCGCGTCAGGCGCTGGACTGCTTACTGGCAGGA
TGTGAATCAATTACTCTGCCACTGGATGTGGCACAACAGATGATTAGCTATCCGGCGGTT
GATGCCGCTGTGGCGAAGTTTGAGCAGGACTGGCAGGGAGCGTTTGGCAGAACGTCGATT
TAA
Protein Properties
Pfam Domain Function:
Protein Residues:220
Protein Molecular Weight:25056
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>NADH-quinone oxidoreductase subunit B
MDYTLTRIDPNGENDRYPLQKQEIVTDPLEQEVNKNVFMGKLNDMVNWGRKNSIWPYNFG
LSCCYVEMVTSFTAVHDVARFGAEVLRASPRQADLMVVAGTCFTKMAPVIQRLYDQMLEP
KWVISMGACANSGGMYDIYSVVQGVDKFIPVDVYIPGCPPRPEAYMQALMLLQESIGKER
RPLSWVVGDQGVYRANMQSERERKRGERIAVTNLRTPDEI
References
External Links:
ResourceLink
Uniprot ID:P0AFC7
Uniprot Name:NUOB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674771
Ecogene ID:EG12083
Ecocyc:EG12083
ColiBase:b2287
Kegg Gene:b2287
EchoBASE ID:EB2008
CCDB:NUOB_ECOLI
BacMap:16130222
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
  • Leif, H., Sled, V. D., Ohnishi, T., Weiss, H., Friedrich, T. (1995). "Isolation and characterization of the proton-translocating NADH: ubiquinone oxidoreductase from Escherichia coli." Eur J Biochem 230:538-548. Pubmed: 7607227
  • 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
  • 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