Identification
Name:Fumarate hydratase class II
Synonyms:
  • Fumarase C
Gene Name:fumC
Enzyme Class:
Biological Properties
General Function:Involved in fumarate hydratase activity
Specific Function:(S)-malate = fumarate + H(2)O
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
Thumb+ThumbThumb
ThumbThumb+Thumb
SMPDB Reactions:
Thumb+ThumbL-Malic acid+Thumb
EcoCyc Reactions:
Thumb+ThumbThumb
Complex Reactions:
ThumbThumb+Thumb
Metabolites:
ECMDB IDNameView
ECMDB00176Fumaric acidMetaboCard
ECMDB00156L-Malic acidMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Component
macromolecular complex
protein complex
tricarboxylic acid cycle enzyme complex
Function
carbon-oxygen lyase activity
catalytic activity
fumarate hydratase activity
hydro-lyase activity
lyase activity
Process
acetyl-CoA catabolic process
acetyl-CoA metabolic process
carboxylic acid metabolic process
cellular metabolic process
coenzyme metabolic process
cofactor metabolic process
dicarboxylic acid metabolic process
fumarate metabolic process
metabolic process
organic acid metabolic process
oxoacid metabolic process
tricarboxylic acid cycle
Gene Properties
Blattner:b1611
Gene OrientationCounterclockwise
Centisome Percentage:36.28
Left Sequence End1683209
Right Sequence End1684612
Gene Sequence:
>1404 bp
ATGCAAACAACACAACAAAATGCGCCACTGAAGCGCACAATGAAAACGCGTCACCTGATT
ATGCTTTCCTTGGGCGGCGTGATTGGCACAGGATTATTCTTCAATACCGGGTACATCATT
TCCACCACTGGAGCGGCGGGAACGCTGCTGGCCTATCTGATTGGTGCGCTGGTGGTCTGG
CTGGTTATGCAGTGTCTGGGCGAGCTGTCGGTCGCGATGCCGGAGACCGGAGCGTTTCAC
GTTTATGCCGCGCGCTATCTTGGTCCGGCTACCGGGTATACCGTGGCCTGGCTTTACTGG
CTGACCTGGACCGTGGCGCTGGGTTCGAGCTTTACCGCCGCTGGATTCTGTATGCAGTAC
TGGTTTCCACAGGTGCCGGTATGGGTCTGGTGCGTGGTGTTCTGCGCGATTATTTTTGGT
CTGAATGTTATCTCCACGCGCTTTTTTGCCGAAGGGGAGTTCTGGTTCTCGCTGGTCAAA
GTGGTCACTATCATCGCCTTTATCATCCTCGGTGGGGCGGCGATTTTCGGCTTTATTCCG
ATGCAGGATGGCTCGCCCGCGCCGGGGCTGAGTAATATCACGGCAGAAGGCTGGTTCCCG
CACGGTGGCTTACCGATTTTGATGACTATGGTGGCAGTGAACTTTGCTTTTTCGGGTACC
GAGCTTATCGGCATTGCCGCCGGTGAAACGGAAAACCCGCGCAAAGTTATCCCGGTAGCG
ATTCGTACTACCATCGCGCGACTGATTATTTTCTTTATCGGCACCGTGTTTGTGCTGGCA
GCGCTGATCCCGATGCAGCAGGTGGGCGTGGAGAAAAGCCCGTTTGTGCTGGTATTTGAG
AAAGTAGGGATCCCGTACGCCGCTGATATTTTTAACTTCGTGATCCTGACGGCTATTCTT
TCTGCAGCGAACTCCGGGTTATATGCCTCCGGGCGCATGCTGTGGTCGTTGTCGAATGAA
CGTACGCTACCGGCCTGTTTTGCGCGAGTAACGAAAAACGGCGTGCCACTGACGGCGCTG
TCGGTCAGTATGCTCGGTGGTGTGCTGGCGCTGTTTTCCAGCGTGGTGGCCCCGGACACG
GTATTTGTTGCGCTGTCGGCAATCTCCGGGTTTGCGGTGGTAGCGGTGTGGCTGAGTATC
TGCGCCTCGCATTTTGTTTTTCGTCGCCGTCATCTGCAACAAGGTAAGGCATTGAGTGAA
TTACATTATCGCGCGCCGTGGTATCCGCTGGTGCCAGTATTAGGTTTTGTGCTGTGCCTG
GTGGCCTGTGTTGGGCTGGCATTCGATCCAGCGCAGAGAATTGCGTTGTGGTGCGGGTTA
CCGTTTGTTGCGTTGTGCTATGGTGCTTATTTCCTTACTCAACCCCGAAACGCAAAACAG
GAGCCAGAACATGTCGCAGAATAA
Protein Properties
Pfam Domain Function:
Protein Residues:467
Protein Molecular Weight:50488
Protein Theoretical pI:7
PDB File:1FUO
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Fumarate hydratase class II
MNTVRSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKMPTSLIHALALTKRAAAKVNE
DLGLLSEEKASAIRQAADEVLAGQHDDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGG
VRGMERKVHPNDDVNKSQSSNDVFPTAMHVAALLALRKQLIPQLKTLTQTLNEKSRAFAD
IVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIEYSLPHVAELALGGTAVGTGLNTHP
EYARRVADELAVITCAPFVTAPNKFEALATCDALVQAHGALKGLAASLMKIANDVRWLAS
GPRCGIGEISIPENEPGSSIMPGKVNPTQCEALTMLCCQVMGNDVAINMGGASGNFELNV
FRPMVIHNFLQSVRLLADGMESFNKHCAVGIEPNRERINQLLNESLMLVTALNTHIGYDK
AAEIAKKAHKEGLTLKAAALALGYLSEAEFDSWVRPEQMVGSMKAGR
References
External Links:
ResourceLink
Uniprot ID:P05042
Uniprot Name:FUMC_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674404
PDB ID:1FUO
Ecogene ID:EG10358
Ecocyc:EG10358
ColiBase:b1611
Kegg Gene:b1611
EchoBASE ID:EB0353
CCDB:FUMC_ECOLI
BacMap:16129569
General Reference:
  • 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, a. l. .. (1996). "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 3:363-377. Pubmed: 9097039
  • 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
  • Estevez, M., Skarda, J., Spencer, J., Banaszak, L., Weaver, T. M. (2002). "X-ray crystallographic and kinetic correlation of a clinically observed human fumarase mutation." Protein Sci 11:1552-1557. Pubmed: 12021453
  • Guest, J. R., Miles, J. S., Roberts, R. E., Woods, S. A. (1985). "The fumarase genes of Escherichia coli: location of the fumB gene and discovery of a new gene (fumC)." J Gen Microbiol 131:2971-2984. Pubmed: 3005475
  • 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
  • Miles, J. S., Guest, J. R. (1984). "Complete nucleotide sequence of the fumarase gene fumA, of Escherichia coli." Nucleic Acids Res 12:3631-3642. Pubmed: 6328431
  • Rose, I. A., Weaver, T. M. (2004). "The role of the allosteric B site in the fumarase reaction." Proc Natl Acad Sci U S A 101:3393-3397. Pubmed: 14990798
  • Ueda, Y., Yumoto, N., Tokushige, M., Fukui, K., Ohya-Nishiguchi, H. (1991). "Purification and characterization of two types of fumarase from Escherichia coli." J Biochem 109:728-733. Pubmed: 1917897
  • Weaver, T. M., Levitt, D. G., Banaszak, L. J. (1993). "Purification and crystallization of fumarase C from Escherichia coli." J Mol Biol 231:141-144. Pubmed: 8496960
  • Weaver, T., Banaszak, L. (1996). "Crystallographic studies of the catalytic and a second site in fumarase C from Escherichia coli." Biochemistry 35:13955-13965. Pubmed: 8909293
  • Weaver, T., Lees, M., Banaszak, L. (1997). "Mutations of fumarase that distinguish between the active site and a nearby dicarboxylic acid binding site." Protein Sci 6:834-842. Pubmed: 9098893
  • Woods, S. A., Miles, J. S., Roberts, R. E., Guest, J. R. (1986). "Structural and functional relationships between fumarase and aspartase. Nucleotide sequences of the fumarase (fumC) and aspartase (aspA) genes of Escherichia coli K12." Biochem J 237:547-557. Pubmed: 3541901
  • Woods, S. A., Schwartzbach, S. D., Guest, J. R. (1988). "Two biochemically distinct classes of fumarase in Escherichia coli." Biochim Biophys Acta 954:14-26. Pubmed: 3282546