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ECOLI:FUMA

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) fumA (ECO:0000303 with PMID:6328431[1])
Protein Name(s) Fumarate hydratase class I, aerobic (ECO:0000303 with PMID:3282546[2])

Fumarase A (ECO:0000303 with PMID:1329945[3]) Oxaloacetate keto--enol-isomerase (ECO:0000303 with PMID:8422384[4]) OAAKE isomerase (ECO:0000303 with PMID:8422384[4]) Oxaloacetate tautomerase (ECO:0000305 with PMID:8422384[4])

External Links
UniProt P0AC33
EMBL X00522
AP009048
U00096
PIR A03531
RefSeq NP_416129.1
YP_489875.1
ProteinModelPortal P0AC33
SMR P0AC33
DIP DIP-36200N
IntAct P0AC33
MINT MINT-1310290
STRING 511145.b1612
PaxDb P0AC33
PRIDE P0AC33
EnsemblBacteria AAC74684
BAA15360
GeneID 12934128
946826
KEGG ecj:Y75_p1588
eco:b1612
PATRIC 32118526
EchoBASE EB0351
EcoGene EG10356
eggNOG COG1838
HOGENOM HOG000009338
InParanoid P0AC33
KO K01676
OMA QIQTSQC
OrthoDB EOG6TXR10
PhylomeDB P0AC33
BioCyc EcoCyc:FUMA-MONOMER
ECOL316407:JW1604-MONOMER
MetaCyc:FUMA-MONOMER
RETL1328306-WGS:GSTH-2399-MONOMER
SABIO-RK P0AC33
UniPathway UPA00223
PRO PR:P0AC33
Proteomes UP000000318
UP000000625
Genevestigator P0AC33
GO GO:0005829
GO:0051539
GO:0004333
GO:0042802
GO:0046872
GO:0050163
GO:0006099
Gene3D 3.20.130.10
InterPro IPR004646
IPR004647
IPR011167
IPR020557
Pfam PF05681
PF05683
PIRSF PIRSF001394
SUPFAM SSF117457
TIGRFAMs TIGR00722
TIGR00723
PROSITE PS00163

Annotations

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

part_of

GO:0005829

cytosol

PMID:16858726[5]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:24561554[6]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0AC33

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:16858726[5]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0AC33

F

Seeded From UniProt

complete

enables

GO:0004333

fumarate hydratase activity

PMID:11133938[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004333

fumarate hydratase activity

PMID:8203917[8]

ECO:0000303

author statement without traceable support used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0051539

4 iron, 4 sulfur cluster binding

PMID:1329945[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0050163

oxaloacetate tautomerase activity

PMID:8422384[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006099

tricarboxylic acid cycle

PMID:6296045[9]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004333

fumarate hydratase activity

PMID:23405168[10]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004333

fumarate hydratase activity

PMID:1329945[3]

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: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:IPR011167

F

Seeded From UniProt

complete

involved_in

GO:0006091

generation of precursor metabolites and energy

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011167

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:IPR004646

F

Seeded From UniProt

complete

enables

GO:0016836

hydro-lyase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004647
InterPro:IPR036660

F

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

enables

GO:0050163

oxaloacetate tautomerase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:5.3.2.2

F

Seeded From UniProt

complete

enables

GO:0051536

iron-sulfur cluster binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0411

F

Seeded From UniProt

complete

enables

GO:0051539

4 iron, 4 sulfur cluster binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0004

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

enables

GO:0016853

isomerase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0413

F

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

Notes

References

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

  1. Miles, JS & Guest, JR (1984) Complete nucleotide sequence of the fumarase gene fumA, of Escherichia coli. Nucleic Acids Res. 12 3631-42 PubMed GONUTS page
  2. Woods, SA et al. (1988) Two biochemically distinct classes of fumarase in Escherichia coli. Biochim. Biophys. Acta 954 14-26 PubMed GONUTS page
  3. 3.0 3.1 3.2 Flint, DH et al. (1992) Fumarase a from Escherichia coli: purification and characterization as an iron-sulfur cluster containing enzyme. Biochemistry 31 10331-7 PubMed GONUTS page
  4. 4.0 4.1 4.2 4.3 Flint, DH (1993) Escherichia coli fumarase A catalyzes the isomerization of enol and keto oxalacetic acid. Biochemistry 32 799-805 PubMed GONUTS page
  5. 5.0 5.1 Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
  6. Rajagopala, SV et al. (2014) The binary protein-protein interaction landscape of Escherichia coli. Nat. Biotechnol. 32 285-90 PubMed GONUTS page
  7. Tseng, CP et al. (2001) Oxygen- and growth rate-dependent regulation of Escherichia coli fumarase (FumA, FumB, and FumC) activity. J. Bacteriol. 183 461-7 PubMed GONUTS page
  8. Flint, DH (1994) Initial kinetic and mechanistic characterization of Escherichia coli fumarase A. Arch. Biochem. Biophys. 311 509-16 PubMed GONUTS page
  9. Guest, JR & Roberts, RE (1983) Cloning, mapping, and expression of the fumarase gene of Escherichia coli K-12. J. Bacteriol. 153 588-96 PubMed GONUTS page
  10. van Vugt-Lussenburg, BM et al. (2013) Biochemical similarities and differences between the catalytic [4Fe-4S] cluster containing fumarases FumA and FumB from Escherichia coli. PLoS ONE 8 e55549 PubMed GONUTS page