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ECOLI:FUMC

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) fumC
Protein Name(s) Fumarate hydratase class II

Fumarase C Iron-independent fumarase

External Links
UniProt P05042
EMBL X04065
U00096
AP009048
X00522
PIR S07138
RefSeq NP_416128.1
YP_489874.1
PDB 1FUO
1FUP
1FUQ
1FUR
1KQ7
1YFE
2FUS
PDBsum 1FUO
1FUP
1FUQ
1FUR
1KQ7
1YFE
2FUS
ProteinModelPortal P05042
SMR P05042
DIP DIP-9719N
IntAct P05042
STRING 511145.b1611
PaxDb P05042
PRIDE P05042
EnsemblBacteria AAC74683
BAA15349
GeneID 12934129
946147
KEGG ecj:Y75_p1587
eco:b1611
PATRIC 32118524
EchoBASE EB0353
EcoGene EG10358
eggNOG COG0114
HOGENOM HOG000061736
InParanoid P05042
KO K01679
OMA NTPKGYD
OrthoDB EOG6V1M4M
PhylomeDB P05042
BioCyc EcoCyc:FUMC-MONOMER
ECOL316407:JW1603-MONOMER
MetaCyc:FUMC-MONOMER
SABIO-RK P05042
UniPathway UPA00223
EvolutionaryTrace P05042
PRO PR:P05042
Proteomes UP000000318
UP000000625
Genevestigator P05042
GO GO:0045239
GO:0004333
GO:0006106
GO:0006979
GO:0006099
Gene3D 1.10.275.10
HAMAP MF_00743
InterPro IPR005677
IPR024083
IPR018951
IPR020557
IPR000362
IPR022761
IPR008948
PANTHER PTHR11444
Pfam PF10415
PF00206
PRINTS PR00149
SUPFAM SSF48557
TIGRFAMs TIGR00979
PROSITE PS00163

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

enables

GO:0004333

fumarate hydratase activity

PMID:3282546[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004333

fumarate hydratase activity

PMID:1917897[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006108

malate metabolic process

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000154499
RGD:2614

P

Seeded From UniProt

complete

involved_in

GO:0006106

fumarate metabolic process

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000154499
RGD:2614
SGD:S000006183
UniProtKB:Q9FI53

P

Seeded From UniProt

complete

involved_in

GO:0006099

tricarboxylic acid cycle

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000154499
RGD:2614
SGD:S000006183

P

Seeded From UniProt

complete

enables

GO:0004333

fumarate hydratase activity

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10358
PANTHER:PTN000154499
RGD:2614
SGD:S000006183
UniProtKB:P07954
UniProtKB:Q9FI53

F

Seeded From UniProt

complete

involved_in

GO:0006979

response to oxidative stress

PMID:1631070[4]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004333

fumarate hydratase activity

PMID:8496960[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR008948
InterPro:IPR020557

F

Seeded From UniProt

complete

enables

GO:0004333

fumarate hydratase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005677

F

Seeded From UniProt

complete

involved_in

GO:0006099

tricarboxylic acid cycle

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR018951

P

Seeded From UniProt

complete

involved_in

GO:0006106

fumarate metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005677

P

Seeded From UniProt

complete

enables

GO:0016829

lyase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR018951

F

Seeded From UniProt

complete

part_of

GO:0045239

tricarboxylic acid cycle enzyme complex

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005677

C

Seeded From UniProt

complete

enables

GO:0004333

fumarate hydratase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:4.2.1.2

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000099076

C

Seeded From UniProt

complete

enables

GO:0004333

fumarate hydratase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000099076

F

Seeded From UniProt

complete

involved_in

GO:0006099

tricarboxylic acid cycle

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000099076

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

involved_in

GO:0008152

metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0021

P

Seeded From UniProt

complete

enables

GO:0016829

lyase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0456

F

Seeded From UniProt

complete

involved_in

GO:0006099

tricarboxylic acid cycle

GO_REF:0000037
GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0816
UniPathway:UPA00223

P

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0021

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Woods, SA et al. (1988) Two biochemically distinct classes of fumarase in Escherichia coli. Biochim. Biophys. Acta 954 14-26 PubMed GONUTS page
  2. Ueda, Y et al. (1991) Purification and characterization of two types of fumarase from Escherichia coli. J. Biochem. 109 728-33 PubMed GONUTS page
  3. 3.0 3.1 3.2 3.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  4. Liochev, SI & Fridovich, I (1992) Fumarase C, the stable fumarase of Escherichia coli, is controlled by the soxRS regulon. Proc. Natl. Acad. Sci. U.S.A. 89 5892-6 PubMed GONUTS page
  5. Weaver, TM et al. (1993) Purification and crystallization of fumarase C from Escherichia coli. J. Mol. Biol. 231 141-4 PubMed GONUTS page