Formate dehydrogenase H (P07658)

Identification
Name:Formate dehydrogenase H
Synonyms:
  • Formate dehydrogenase-H subunit alpha
  • FDH-H
  • Formate-hydrogen-lyase-linked, selenocysteine-containing polypeptide
Gene Name:fdhF
Enzyme Class:
Biological Properties
General Function:Involved in formate dehydrogenase (NAD+) activity
Specific Function:Decomposes formic acid to hydrogen and carbon dioxide under anaerobic conditions in the absence of exogenous electron acceptors
Cellular Location:Not Available
SMPDB Pathways:Not Available
KEGG Pathways:
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
EcoCyc Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Formic acid + 1.0Hydrogen ion → 1.0Carbon dioxide + 1.0Hydrogen (gas)
ReactionCard
1.0Thumb+1.0an oxidized electron acceptor+1.0Thumb → 1.0Thumb+1.0a reduced electron acceptor
1.0Formic acid + 1.0an oxidized electron acceptor + 1.0Hydrogen ion → 1.0Carbon dioxide + 1.0a reduced electron acceptor
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Formic acid + 1.0NAD → 1.0Carbon dioxide + 1.0NADH
ReactionCard
1.0Thumb+1.0acceptor → 1.0Thumb+1.0reduced acceptor
1.0Formic acid + 1.0acceptor → 1.0Carbon dioxide + 1.0reduced acceptor
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB04030Carbon dioxideMetaboCard
ECMDB00142Formic acidMetaboCard
ECMDB01362Hydrogen (gas)MetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00902NADMetaboCard
ECMDB01487NADHMetaboCard
GO Classification:
Component
formate dehydrogenase complex
macromolecular complex
protein complex
Function
binding
catalytic activity
cation binding
electron carrier activity
formate dehydrogenase activity
ion binding
metal ion binding
molybdenum ion 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
transition metal ion binding
Process
carboxylic acid metabolic process
cellular metabolic process
formate metabolic process
metabolic process
monocarboxylic acid metabolic process
organic acid metabolic process
oxidation reduction
oxoacid metabolic process
Gene Properties
Blattner:b4079
Gene OrientationCounterclockwise
Centisome Percentage:92.58
Left Sequence End4295242
Right Sequence End4297389
Gene Sequence:
>2148 bp
ATGAAAAAAGTCGTCACGGTTTGCCCCTATTGCGCATCAGGTTGCAAAATCAACCTGGTC
GTCGATAACGGCAAAATCGTCCGGGCGGAGGCAGCGCAGGGGAAAACCAACCAGGGTACC
CTGTGTCTGAAGGGTTATTATGGCTGGGACTTCATTAACGATACCCAGATCCTGACCCCG
CGCCTGAAAACCCCCATGATCCGTCGCCAGCGTGGCGGCAAACTCGAACCTGTTTCCTGG
GATGAGGCACTGAATTACGTTGCCGAGCGCCTGAGCGCCATCAAAGAGAAGTACGGTCCG
GATGCCATCCAGACGACCGGCTCCTCGCGTGGTACGGGTAACGAAACCAACTATGTAATG
CAAAAATTTGCGCGCGCCGTTATTGGTACCAATAACGTTGACTGCTGCGCTCGTGTCTGA
CACGGCCCATCGGTTGCAGGTCTGCACCAATCGGTCGGTAATGGCGCAATGAGCAATGCT
ATTAACGAAATTGATAATACCGATTTAGTGTTCGTTTTCGGGTACAACCCGGCGGATTCC
CACCCAATCGTGGCGAATCACGTAATTAACGCTAAACGTAACGGGGCGAAAATTATCGTC
TGCGATCCGCGCAAAATTGAAACCGCGCGCATTGCTGACATGCACATTGCACTGAAAAAC
GGCTCGAACATCGCGCTGTTGAATGCGATGGGCCATGTCATTATTGAAGAAAATCTGTAC
GACAAAGCGTTCGTCGCTTCACGTACAGAAGGCTTTGAAGAGTATCGTAAAATCGTTGAA
GGCTACACGCCGGAGTCGGTTGAAGATATCACCGGCGTCAGCGCCAGTGAGATTCGTCAG
GCGGCACGGATGTATGCCCAGGCGAAAAGCGCCGCCATCCTGTGGGGCATGGGTGTAACC
CAGTTCTACCAGGGCGTGGAAACCGTGCGTTCTCTGACCAGCCTCGCGATGCTGACCGGT
AACCTCGGTAAGCCGCATGCGGGTGTTAACCCGGTTCGTGGTCAGAACAACGTTCAGGGT
GCCTGCGATATGGGCGCGCTGCCGGATACGTATCCGGGATACCAGTACGTGAAAGATCCG
GCTAACCGCGAGAAATTCGCCAAAGCCTGGGGCGTGGAAAGCCTGCCAGCGCATACCGGC
TATCGCATCAGCGAGCTGCCGCACCGCGCAGCGCATGGCGAAGTGCGTGCCGCGTACATT
ATGGGCGAAGATCCGCTACAAACTGACGCGGAGCTGTCGGCAGTACGTAAAGCCTTTGAA
GATCTGGAACTGGTTATCGTTCAGGACATCTTTATGACCAAAACCGCGTCGGCGGCGGAT
GTTATTTTACCGTCAACGTCGTGGGGCGAGCATGAAGGCGTGTTTACTGCGGCTGACCGT
GGCTTCCAGCGTTTCTTCAAGGCGGTTGAACCGAAATGGGATCTGAAAACGGACTGGCAA
ATCATCAGTGAAATCGCCACCCGTATGGGTTATCCGATGCACTACAACAACACCCAGGAG
ATCTGGGATGAGTTGCGTCATCTGTGCCCGGATTTCTACGGTGCGACTTACGAGAAAATG
GGCGAACTGGGCTTCATTCAGTGGCCTTGCCGCGATACTTCAGATGCCGATCAGGGGACT
TCTTATCTGTTTAAAGAGAAGTTTGATACCCCGAACGGTCTGGCGCAGTTCTTCACCTGC
GACTGGGTAGCGCCAATCGACAAACTCACCGACGAGTACCCGATGGTACTGTCAACGGTG
CGTGAAGTTGGTCACTACTCTTGCCGTTCGATGACCGGTAACTGTGCGGCACTGGCGGCG
CTGGCTGATGAACCTGGCTACGCACAAATCAATACCGAAGACGCCAAACGTCTGGGTATT
GAAGATGAGGCATTGGTTTGGGTGCACTCGCGTAAAGGCAAAATTATCACCCGTGCGCAG
GTCAGCGATCGTCCGAACAAAGGGGCGATTTACATGACCTACCAGTGGTGGATTGGTGCC
TGTAACGAGCTGGTTACCGAAAACTTAAGCCCGATTACGAAAACGCCGGAGTACAAATAC
TGCGCCGTTCGCGTCGAGCCGATCGCCGATCAGCGCGCCGCCGAGCAGTACGTGATTGAC
GAGTACAACAAGTTGAAAACTCGCCTGCGCGAAGCGGCACTGGCGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:715
Protein Molecular Weight:79373
Protein Theoretical pI:6
PDB File:1FDO
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Formate dehydrogenase H
MKKVVTVCPYCASGCKINLVVDNGKIVRAEAAQGKTNQGTLCLKGYYGWDFINDTQILTP
RLKTPMIRRQRGGKLEPVSWDEALNYVAERLSAIKEKYGPDAIQTTGSSRGTGNETNYVM
QKFARAVIGTNNVDCCARVUHGPSVAGLHQSVGNGAMSNAINEIDNTDLVFVFGYNPADS
HPIVANHVINAKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAMGHVIIEENLY
DKAFVASRTEGFEEYRKIVEGYTPESVEDITGVSASEIRQAARMYAQAKSAAILWGMGVT
QFYQGVETVRSLTSLAMLTGNLGKPHAGVNPVRGQNNVQGACDMGALPDTYPGYQYVKDP
ANREKFAKAWGVESLPAHTGYRISELPHRAAHGEVRAAYIMGEDPLQTDAELSAVRKAFE
DLELVIVQDIFMTKTASAADVILPSTSWGEHEGVFTAADRGFQRFFKAVEPKWDLKTDWQ
IISEIATRMGYPMHYNNTQEIWDELRHLCPDFYGATYEKMGELGFIQWPCRDTSDADQGT
SYLFKEKFDTPNGLAQFFTCDWVAPIDKLTDEYPMVLSTVREVGHYSCRSMTGNCAALAA
LADEPGYAQINTEDAKRLGIEDEALVWVHSRKGKIITRAQVSDRPNKGAIYMTYQWWIGA
CNELVTENLSPITKTPEYKYCAVRVEPIADQRAAEQYVIDEYNKLKTRLREAALA
References
External Links:
ResourceLink
Uniprot ID:P07658
Uniprot Name:FDHF_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85676831
PDB ID:1FDO
Ecogene ID:EG10285
Ecocyc:EG10285
ColiBase:b4079
Kegg Gene:b4079
EchoBASE ID:EB0281
CCDB:FDHF_ECOLI
BacMap:16131905
General Reference:
  • Axley, M. J., Grahame, D. A., Stadtman, T. C. (1990). "Escherichia coli formate-hydrogen lyase. Purification and properties of the selenium-dependent formate dehydrogenase component." J Biol Chem 265:18213-18218. Pubmed: 2211698
  • Blattner, F. R., Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L. (1993). "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Nucleic Acids Res 21:5408-5417. Pubmed: 8265357
  • 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
  • Boyington, J. C., Gladyshev, V. N., Khangulov, S. V., Stadtman, T. C., Sun, P. D. (1997). "Crystal structure of formate dehydrogenase H: catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster." Science 275:1305-1308. Pubmed: 9036855
  • 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
  • Zinoni, F., Birkmann, A., Stadtman, T. C., Bock, A. (1986). "Nucleotide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyase-linked) from Escherichia coli." Proc Natl Acad Sci U S A 83:4650-4654. Pubmed: 2941757