NADH-quinone oxidoreductase subunit F (P31979)

Identification
Name:NADH-quinone oxidoreductase subunit F
Synonyms:
  • NADH dehydrogenase I subunit F
  • NDH-1 subunit F
  • NUO6
Gene Name:nuoF
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 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:Not Available
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
FMN binding
iron-sulfur cluster binding
metal cluster binding
NAD or NADH binding
NADH dehydrogenase (quinone) activity
NADH dehydrogenase (ubiquinone) activity
NADH dehydrogenase activity
nucleotide binding
oxidoreductase activity
oxidoreductase activity, acting on NADH or NADPH
Process
metabolic process
oxidation reduction
Gene Properties
Blattner:b2284
Gene OrientationCounterclockwise
Centisome Percentage:51.69
Left Sequence End2398240
Right Sequence End2399577
Gene Sequence:
>1338 bp
ATGAAAAACATTATCCGTACTCCCGAAACGCATCCGCTGACCTGGCGTCTGCGCGATGAC
AAACAGCCAGTGTGGCTGGACGAATACCGCAGCAAAAACGGTTACGAAGGCGCGCGTAAG
GCGCTGACCGGGCTGTCTCCGGACGAAATCGTTAATCAGGTAAAAGACGCTGGTCTGAAA
GGGCGCGGCGGCGCGGGCTTCTCGACTGGCCTGAAATGGAGCCTGATGCCGAAAGACGAA
TCCATGAACATCCGTTACCTGCTGTGTAATGCCGATGAAATGGAGCCGGGCACCTATAAA
GACCGCCTGTTGATGGAGCAACTGCCGCACCTGCTGGTGGAAGGTATGCTCATCTCCGCG
TTTGCGCTGAAAGCTTACCGTGGCTACATCTTCCTGCGTGGCGAATATATCGAAGCGGCA
GTTAATCTGCGCCGTGCCATTGCCGAAGCCACCGAAGCGGGTCTGCTTGGCAAAAACATT
ATGGGAACAGGTTTCGATTTCGAACTGTTCGTCCATACCGGGGCAGGGCGCTACATCTGC
GGGGAAGAAACAGCGTTAATCAACTCCCTGGAAGGACGTCGTGCTAACCCACGCTCGAAG
CCACCCTTCCCGGCAACCTCCGGCGCATGGGGTAAACCGACCTGTGTCAACAACGTCGAA
ACCCTGTGTAACGTTCCGGCGATCCTCGCTAACGGCGTGGAGTGGTATCAGAACATCTCG
AAAAGTAAAGATGCTGGCACCAAGCTGATGGGCTTCTCCGGTCGGGTGAAAAATCCGGGA
CTGTGGGAACTGCCGTTCGGCACCACCGCACGCGAGATCCTCGAAGATTACGCCGGTGGT
ATGCGTGATGGTCTGAAATTTAAAGCCTGGCAGCCAGGCGGCGCGGGGACTGACTTCCTG
ACCGAAGCGCACCTTGATCTGCCGATGGAATTCGAAAGTATCGGTAAAGCGGGCAGCCGT
CTGGGTACGGCGCTGGCGATGGCGGTTGACCATGAGATCAACATGGTGTCGCTGGTGCGT
AACCTGGAAGAGTTTTTCGCCCGTGAGTCCTGCGGCTGGTGTACGCCGTGCCGCGACGGT
CTGCCGTGGAGCGTGAAAATTCTGCGTGCGCTGGAGCGTGGTGAAGGTCAGCCGGGCGAT
ATCGAAACACTTGAGCAACTGTGTCGATTCTTAGGCCCGGGTAAAACTTTCTGTGCCCAC
GCACCTGGTGCAGTGGAGCCGTTACAGAGCGCCATCAAATATTTCCGCGAAGAATTTGAG
GCGGGAATCAAACAGCCGTTCAGCAATACCCATTTGATTAATGGGATTCAGCCGAACCTG
CTGAAAGAGCGCTGGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:445
Protein Molecular Weight:49292
Protein Theoretical pI:7
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>NADH-quinone oxidoreductase subunit F
MKNIIRTPETHPLTWRLRDDKQPVWLDEYRSKNGYEGARKALTGLSPDEIVNQVKDAGLK
GRGGAGFSTGLKWSLMPKDESMNIRYLLCNADEMEPGTYKDRLLMEQLPHLLVEGMLISA
FALKAYRGYIFLRGEYIEAAVNLRRAIAEATEAGLLGKNIMGTGFDFELFVHTGAGRYIC
GEETALINSLEGRRANPRSKPPFPATSGAWGKPTCVNNVETLCNVPAILANGVEWYQNIS
KSKDAGTKLMGFSGRVKNPGLWELPFGTTAREILEDYAGGMRDGLKFKAWQPGGAGTDFL
TEAHLDLPMEFESIGKAGSRLGTALAMAVDHEINMVSLVRNLEEFFARESCGWCTPCRDG
LPWSVKILRALERGEGQPGDIETLEQLCRFLGPGKTFCAHAPGAVEPLQSAIKYFREEFE
AGIKQPFSNTHLINGIQPNLLKERW
References
External Links:
ResourceLink
Uniprot ID:P31979
Uniprot Name:NUOF_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1799645
Ecogene ID:EG11774
Ecocyc:EG11774
ColiBase:b2284
Kegg Gene:b2284
EchoBASE ID:EB1723
CCDB:NUOF_ECOLI
BacMap:16130219
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
  • 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
  • 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
  • Zambrano, M. M., Kolter, R. (1993). "Escherichia coli mutants lacking NADH dehydrogenase I have a competitive disadvantage in stationary phase." J Bacteriol 175:5642-5647. Pubmed: 8366049