Formate dehydrogenase-O iron-sulfur subunit (P0AAJ5)

Identification
Name:Formate dehydrogenase-O iron-sulfur subunit
Synonyms:
  • Aerobic formate dehydrogenase iron-sulfur subunit
  • FDH-Z subunit beta
  • Formate dehydrogenase-O subunit beta
Gene Name:fdoH
Enzyme Class:Not Available
Biological Properties
General Function:Involved in electron carrier activity
Specific Function:Allows to use formate as major electron donor during aerobic respiration. The beta chain is an electron transfer unit containing 4 cysteine clusters involved in the formation of iron- sulfur centers. Electrons are transferred from the gamma chain to the molybdenum cofactor of the alpha subunit
Cellular Location:Cell membrane; Single-pass membrane protein
SMPDB Pathways:
KEGG Pathways:
  • Glyoxylate and dicarboxylate metabolism ec00630
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Formic acid + 1.0NAD ↔ 1.0Hydrogen ion + 1.0Carbon dioxide + 1.0NADH
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0menaquinone-8+1.0Electron+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Formic acid + 1.0menaquinone-8 + 1.0Electron + 1.0Hydrogen ion → 1.0Carbon dioxide + 1.0Hydrogen ion + 1.0Menaquinol 8
ReactionCard
Complex Reactions:
2.0Thumb+1.0Menaquinone 8+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
2.0Hydrogen ion + 1.0Menaquinone 8 + 1.0Formic acid → 1.0Menaquinol 8 + 1.0Carbon dioxide + 1.0Hydrogen ion
ReactionCard
2.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
2.0Hydrogen ion + 1.0Ubiquinone-8 + 1.0Formic acid → 1.0Ubiquinol-8 + 1.0Carbon dioxide + 1.0Hydrogen ion
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB04030Carbon dioxideMetaboCard
ECMDB00142Formic acidMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21245Menaquinol 8MetaboCard
ECMDB00902NADMetaboCard
ECMDB01487NADHMetaboCard
ECMDB01060Ubiquinol-8MetaboCard
ECMDB21296Ubiquinone-8MetaboCard
GO Classification:
Component
cell part
integral to membrane
intrinsic to membrane
membrane part
Function
binding
catalytic activity
electron carrier activity
formate dehydrogenase activity
iron-sulfur cluster binding
metal cluster binding
oxidoreductase activity
oxidoreductase activity, acting on the aldehyde or oxo group of donors
oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Process
cellular metabolic process
cellular respiration
energy derivation by oxidation of organic compounds
generation of precursor metabolites and energy
metabolic process
Gene Properties
Blattner:b3893
Gene OrientationCounterclockwise
Centisome Percentage:87.93
Left Sequence End4079880
Right Sequence End4080782
Gene Sequence:
>903 bp
ATGGATGCACCGAGTACCACACCGCATGACGCGGTATTTAAACAATTTTTAATGCATGCG
GAGACGGCTCGCGACTTTCTGGAGATACATTTGCCAGTGGAATTACGCGAACTTTGTGAC
CTCAACACGCTTCATTTAGAGTCGGGGAGTTTCATTGAAGAGAGCCTGAAAGGACACAGC
ACGGACGTGCTCTATTCCGTGCAAATGCAGGGCAATCCCGGTTATCTGCATGTTGTGATT
GAACACCAAAGCAAGCCGGATAAGAAAATGGCCTTTCGCATGATGCGTTATTCTATAGCC
GCCATGCACCGGCATCTGGAGGCTGACCACGATAAGCTGCCGCTGGTGGTGCCGATACTG
TTTTATCAGGGCGAGGCCACACCTTATCCGCTATCAATGTGCTGGTTTGATATGTTTTAC
TCGCCGGAGCTGGCGCGACGCGTCTATAACAGTCCTTTCCCGCTGGTGGATATCACCATC
ACACCGGATGACGAAATCATGCAACATCGGCGGATTGCGATTCTCGAACTACTGCAAAAA
CATATTCGCCAGCGCGACTTAATGTTATTGCTTGAGCAACTGGTCACGCTGATCGACGAA
GGGTACACTAGCGGAAGTCAGTTAGTTGCCATGCAAAACTATATGCTGCAACGCGGTCAT
ACTGAACAAGCGGATTTGTTTTACGGTGTGTTGAGAGACAGGGAAACGGGAGGGGAGTCT
ATGATGACGCTGGCGCAGTGGTTTGAAGAGAAAGGGATTGAGAAGGGGATTCAGCAGGGA
AGACAGGAAGTAAGTCAGGAATTCGCCCAGCGTCTTCTGAGTAAAGGAATGTCTCGGGAA
GACGTTGCAGAGATGGCAAATTTACCTCTTGCTGAGATTGATAAGGTAATTAACCTTATT
TAA
Protein Properties
Pfam Domain Function:
Protein Residues:300
Protein Molecular Weight:33100
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • 261-279
Protein Sequence:
>Formate dehydrogenase-O iron-sulfur subunit
MAYQSQDIIRRSATNGLTPAPQARDFQEEVAKLIDVTTCIGCKACQVACSEWNDIRDTVG
NNIGVYDNPNDLSAKSWTVMRFSEVEQNDKLEWLIRKDGCMHCSDPGCLKACPAEGAIIQ
YANGIVDFQSEQCIGCGYCIAGCPFDIPRLNPEDNRVYKCTLCVDRVVVGQEPACVKTCP
TGAIHFGTKESMKTLASERVAELKTRGYDNAGLYDPAGVGGTHVMYVLHHADKPNLYHGL
PENPEISETVKFWKGIWKPLAAVGFAATFAASIFHYVGVGPNRADEEENNLHEEKDEERK
References
External Links:
ResourceLink
Uniprot ID:P0AAJ5
Uniprot Name:FDOH_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674347
Ecogene ID:EG11857
Ecocyc:EG11857
ColiBase:b3893
Kegg Gene:b3893
EchoBASE ID:EB1803
CCDB:FDOH_ECOLI
BacMap:16131733
General Reference:
  • Abaibou, H., Pommier, J., Benoit, S., Giordano, G., Mandrand-Berthelot, M. A. (1995). "Expression and characterization of the Escherichia coli fdo locus and a possible physiological role for aerobic formate dehydrogenase." J Bacteriol 177:7141-7149. Pubmed: 8522521
  • Benoit, S., Abaibou, H., Mandrand-Berthelot, M. A. (1998). "Topological analysis of the aerobic membrane-bound formate dehydrogenase of Escherichia coli." J Bacteriol 180:6625-6634. Pubmed: 9852007
  • 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
  • Plunkett, G. 3rd, Burland, V., Daniels, D. L., Blattner, F. R. (1993). "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes." Nucleic Acids Res 21:3391-3398. Pubmed: 8346018