Formate dehydrogenase, nitrate-inducible, cytochrome b556(Fdn) subunit

Details

Name
Formate dehydrogenase, nitrate-inducible, cytochrome b556(Fdn) subunit
Synonyms
  • Anaerobic formate dehydrogenase cytochrome b556 subunit
  • FDH-N subunit gamma
  • Formate dehydrogenase-N subunit gamma
Gene Name
fdnI
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0012873|Formate dehydrogenase, nitrate-inducible, cytochrome b556(Fdn) subunit
MSKSKMIVRTKFIDRACHWTVVICFFLVALSGISFFFPTLQWLTQTFGTPQMGRILHPFF
GIAIFVALMFMFVRFVHHNIPDKKDIPWLLNIVEVLKGNEHKVADVGKYNAGQKMMFWSI
MSMIFVLLVTGVIIWRPYFAQYFPMQVVRYSLLIHAAAGIILIHAILIHMYMAFWVKGSI
KGMIEGKVSRRWAKKHHPRWYREIEKAEAKKESEEGI
Number of residues
217
Molecular Weight
25368.34
Theoretical pI
10.58
GO Classification
Functions
electron carrier activity / formate dehydrogenase (NAD+) activity / formate dehydrogenase (quinone) activity / heme binding / metal ion binding
Processes
anaerobic respiration / formate oxidation / respiratory electron transport chain
Components
formate dehydrogenase complex / integral component of plasma membrane / plasma membrane
General Function
Metal ion binding
Specific Function
Formate dehydrogenase allows E.coli to use formate as major electron donor during anaerobic respiration, when nitrate is used as electron acceptor. Subunit gamma is the cytochrome b556 component of the formate dehydrogenase-N, and also contains a menaquinone reduction site that receives electrons from the beta subunit (FdnH), through its hemes. Formate dehydrogenase-N is part of a system that generates proton motive force, together with the dissimilatory nitrate reductase (Nar).
Pfam Domain Function
Transmembrane Regions
12-36 53-74 111-134 151-175
Cellular Location
Cell inner membrane
Gene sequence
>lcl|BSEQ0012874|Formate dehydrogenase, nitrate-inducible, cytochrome b556(Fdn) subunit (fdnI)
ATGAGTAAGTCGAAAATGATTGTGCGCACCAAATTTATTGATCGCGCCTGTCACTGGACC
GTGGTGATTTGCTTCTTCCTGGTGGCGCTGTCCGGGATTTCGTTCTTCTTCCCGACGCTG
CAATGGCTGACGCAAACCTTCGGTACGCCGCAGATGGGACGCATTTTGCACCCGTTCTTC
GGCATTGCGATTTTCGTCGCACTGATGTTTATGTTTGTGCGTTTTGTGCATCACAACATC
CCGGATAAGAAAGATATTCCGTGGCTGTTGAACATTGTCGAAGTATTGAAAGGCAATGAG
CATAAAGTGGCGGATGTCGGTAAGTACAACGCCGGGCAAAAGATGATGTTCTGGTCGATC
ATGAGCATGATTTTCGTGCTGCTGGTGACCGGGGTGATTATCTGGCGTCCGTACTTTGCG
CAGTACTTCCCGATGCAGGTTGTTCGCTACAGCCTGCTGATCCACGCGGCTGCGGGTATC
ATCCTGATCCACGCCATCCTGATCCATATGTATATGGCATTTTGGGTGAAAGGATCGATT
AAAGGGATGATCGAAGGGAAGGTAAGTCGTCGCTGGGCGAAGAAACACCATCCGCGCTGG
TATCGTGAAATCGAGAAGGCAGAAGCGAAAAAAGAGAGTGAAGAAGGGATATAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0AEK7
UniProtKB Entry NameFDNI_ECOLI
GenBank Gene IDM75029
General References
  1. Berg BL, Li J, Heider J, Stewart V: Nitrate-inducible formate dehydrogenase in Escherichia coli K-12. I. Nucleotide sequence of the fdnGHI operon and evidence that opal (UGA) encodes selenocysteine. J Biol Chem. 1991 Nov 25;266(33):22380-5. [Article]
  2. Aiba H, Baba T, Hayashi K, Inada T, Isono K, Itoh T, Kasai H, Kashimoto K, Kimura S, Kitakawa M, Kitagawa M, Makino K, Miki T, Mizobuchi K, Mori H, Mori T, Motomura K, Nakade S, Nakamura Y, Nashimoto H, Nishio Y, Oshima T, Saito N, Sampei G, Horiuchi T, et al.: A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map. DNA Res. 1996 Dec 31;3(6):363-77. [Article]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  4. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  5. Berg BL, Stewart V: Structural genes for nitrate-inducible formate dehydrogenase in Escherichia coli K-12. Genetics. 1990 Aug;125(4):691-702. [Article]
  6. Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G: Global topology analysis of the Escherichia coli inner membrane proteome. Science. 2005 May 27;308(5726):1321-3. [Article]
  7. Jormakka M, Tornroth S, Byrne B, Iwata S: Molecular basis of proton motive force generation: structure of formate dehydrogenase-N. Science. 2002 Mar 8;295(5561):1863-8. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB079182-heptyl-4-hydroxyquinoline N-oxideexperimentalunknownDetails