Fumarate hydratase class II

Details

Name
Fumarate hydratase class II
Synonyms
  • 4.2.1.2
  • Fumarase C
  • Iron-independent fumarase
Gene Name
fumC
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0011374|Fumarate hydratase class II
MNTVRSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKMPTSLIHALALTKRAAAKVNE
DLGLLSEEKASAIRQAADEVLAGQHDDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGG
VRGMERKVHPNDDVNKSQSSNDVFPTAMHVAALLALRKQLIPQLKTLTQTLNEKSRAFAD
IVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIEYSLPHVAELALGGTAVGTGLNTHP
EYARRVADELAVITCAPFVTAPNKFEALATCDALVQAHGALKGLAASLMKIANDVRWLAS
GPRCGIGEISIPENEPGSSIMPGKVNPTQCEALTMLCCQVMGNDVAINMGGASGNFELNV
FRPMVIHNFLQSVRLLADGMESFNKHCAVGIEPNRERINQLLNESLMLVTALNTHIGYDK
AAEIAKKAHKEGLTLKAAALALGYLSEAEFDSWVRPEQMVGSMKAGR
Number of residues
467
Molecular Weight
50488.44
Theoretical pI
6.57
GO Classification
Functions
fumarate hydratase activity
Processes
fumarate metabolic process / malate metabolic process / protein tetramerization / response to oxidative stress / tricarboxylic acid cycle
Components
cytosol / tricarboxylic acid cycle enzyme complex
General Function
Fumarate hydratase activity
Specific Function
Catalyzes the reversible addition of water to fumarate to give L-malate.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0011375|Fumarate hydratase class II (fumC)
ATGAATACAGTACGCAGCGAAAAAGATTCGATGGGGGCGATTGATGTCCCGGCAGATAAG
CTGTGGGGCGCACAAACTCAACGCTCGCTGGAGCATTTCCGCATTTCGACGGAGAAAATG
CCCACCTCACTGATTCATGCGCTGGCGCTAACCAAGCGTGCAGCGGCAAAAGTTAATGAA
GATTTAGGCTTGTTGTCTGAAGAGAAAGCGAGCGCCATTCGTCAGGCGGCGGATGAAGTA
CTGGCAGGACAGCATGACGACGAATTCCCGCTGGCTATCTGGCAGACCGGCTCCGGCACG
CAAAGTAACATGAACATGAACGAAGTGCTGGCTAACCGGGCCAGTGAATTACTCGGCGGT
GTGCGCGGGATGGAACGTAAAGTTCACCCTAACGACGACGTGAACAAAAGCCAAAGTTCC
AACGATGTCTTTCCGACGGCGATGCACGTTGCGGCGCTGCTGGCGCTGCGCAAGCAACTC
ATTCCTCAGCTTAAAACCCTGACACAGACACTGAATGAGAAATCCCGTGCTTTTGCCGAT
ATCGTCAAAATTGGTCGTACTCACTTGCAGGATGCCACGCCGTTAACGCTGGGGCAGGAG
ATTTCCGGCTGGGTAGCGATGCTCGAGCATAATCTCAAACATATCGAATACAGCCTGCCT
CACGTAGCGGAACTGGCTCTTGGCGGTACAGCGGTGGGTACTGGACTAAATACCCATCCG
GAGTATGCGCGTCGCGTAGCAGATGAACTGGCAGTCATTACCTGTGCACCGTTTGTTACC
GCGCCGAACAAATTTGAAGCGCTGGCGACCTGTGATGCCCTGGTTCAGGCGCACGGCGCG
TTGAAAGGGTTGGCTGCGTCACTGATGAAAATCGCCAATGATGTCCGCTGGCTGGCCTCT
GGCCCGCGCTGCGGAATTGGTGAAATCTCAATCCCGGAAAATGAGCCGGGCAGCTCAATC
ATGCCGGGGAAAGTGAACCCAACACAGTGTGAGGCATTAACCATGCTCTGCTGTCAGGTG
ATGGGGAACGACGTGGCGATCAACATGGGGGGCGCTTCCGGTAACTTTGAACTGAACGTC
TTCCGTCCAATGGTGATCCACAATTTCCTGCAATCGGTGCGCTTGCTGGCAGATGGCATG
GAAAGTTTTAACAAACACTGCGCAGTGGGTATTGAACCGAATCGTGAGCGAATCAATCAA
TTACTCAATGAATCGCTGATGCTGGTGACTGCGCTTAACACCCACATTGGTTATGACAAA
GCCGCCGAGATCGCCAAAAAAGCGCATAAAGAAGGGCTGACCTTAAAAGCTGCGGCCCTT
GCGCTGGGGTATCTTAGCGAAGCCGAGTTTGACAGCTGGGTACGGCCAGAACAGATGGTC
GGCAGTATGAAAGCCGGGCGTTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP05042
UniProtKB Entry NameFUMC_ECOLI
GenBank Protein ID41513
GenBank Gene IDX04065
General References
  1. Woods SA, Miles JS, Roberts RE, Guest JR: Structural and functional relationships between fumarase and aspartase. Nucleotide sequences of the fumarase (fumC) and aspartase (aspA) genes of Escherichia coli K12. Biochem J. 1986 Jul 15;237(2):547-57. [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. Miles JS, Guest JR: Complete nucleotide sequence of the fumarase gene fumA, of Escherichia coli. Nucleic Acids Res. 1984 Apr 25;12(8):3631-42. [Article]
  6. Guest JR, Miles JS, Roberts RE, Woods SA: The fumarase genes of Escherichia coli: location of the fumB gene and discovery of a new gene (fumC). J Gen Microbiol. 1985 Nov;131(11):2971-84. [Article]
  7. Ueda Y, Yumoto N, Tokushige M, Fukui K, Ohya-Nishiguchi H: Purification and characterization of two types of fumarase from Escherichia coli. J Biochem. 1991 May;109(5):728-33. [Article]
  8. Weaver TM, Levitt DG, Banaszak LJ: Purification and crystallization of fumarase C from Escherichia coli. J Mol Biol. 1993 May 5;231(1):141-4. [Article]
  9. Woods SA, Schwartzbach SD, Guest JR: Two biochemically distinct classes of fumarase in Escherichia coli. Biochim Biophys Acta. 1988 Apr 28;954(1):14-26. [Article]
  10. Park SJ, Gunsalus RP: Oxygen, iron, carbon, and superoxide control of the fumarase fumA and fumC genes of Escherichia coli: role of the arcA, fnr, and soxR gene products. J Bacteriol. 1995 Nov;177(21):6255-62. [Article]
  11. VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
  12. Rose IA, Weaver TM: The role of the allosteric B site in the fumarase reaction. Proc Natl Acad Sci U S A. 2004 Mar 9;101(10):3393-7. Epub 2004 Feb 27. [Article]
  13. Puthan Veetil V, Fibriansah G, Raj H, Thunnissen AM, Poelarends GJ: Aspartase/fumarase superfamily: a common catalytic strategy involving general base-catalyzed formation of a highly stabilized aci-carboxylate intermediate. Biochemistry. 2012 May 29;51(21):4237-43. doi: 10.1021/bi300430j. Epub 2012 May 15. [Article]
  14. Weaver T, Banaszak L: Crystallographic studies of the catalytic and a second site in fumarase C from Escherichia coli. Biochemistry. 1996 Nov 5;35(44):13955-65. [Article]
  15. Weaver T, Lees M, Banaszak L: Mutations of fumarase that distinguish between the active site and a nearby dicarboxylic acid binding site. Protein Sci. 1997 Apr;6(4):834-42. [Article]
  16. Estevez M, Skarda J, Spencer J, Banaszak L, Weaver TM: X-ray crystallographic and kinetic correlation of a clinically observed human fumarase mutation. Protein Sci. 2002 Jun;11(6):1552-7. [Article]
  17. Weaver T: Structure of free fumarase C from Escherichia coli. Acta Crystallogr D Biol Crystallogr. 2005 Oct;61(Pt 10):1395-401. Epub 2005 Sep 28. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02749Pyromellitic AcidexperimentalunknownDetails
DB034523-Trimethylsilylsuccinic AcidexperimentalunknownDetails
DB03499D-Malic acidexperimentalunknownDetails
DB04272Citric acidapproved, nutraceutical, vet_approvedunknowninhibitorDetails