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ECOLI:FUMA
Contents
| 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 |
ECO:0007005 |
high throughput direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0042802 |
identical protein binding |
ECO:0000353 |
physical interaction evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0042802 |
identical protein binding |
ECO:0000353 |
physical interaction evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004333 |
fumarate hydratase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004333 |
fumarate hydratase activity |
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 |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0050163 |
oxaloacetate tautomerase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006099 |
tricarboxylic acid cycle |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004333 |
fumarate hydratase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004333 |
fumarate hydratase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0003824 |
catalytic activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004333 |
fumarate hydratase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006091 |
generation of precursor metabolites and energy |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016829 |
lyase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016836 |
hydro-lyase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004333 |
fumarate hydratase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0050163 |
oxaloacetate tautomerase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0051536 |
iron-sulfur cluster binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0051539 |
4 iron, 4 sulfur cluster binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0046872 |
metal ion binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016853 |
isomerase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016829 |
lyase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006099 |
tricarboxylic acid cycle |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
UniProtKB-KW:KW-0816 |
P |
Seeded From UniProt |
complete | ||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 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
- ↑ Woods, SA et al. (1988) Two biochemically distinct classes of fumarase in Escherichia coli. Biochim. Biophys. Acta 954 14-26 PubMed GONUTS page
- ↑ 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
- ↑ 4.0 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
- ↑ 5.0 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
- ↑ Rajagopala, SV et al. (2014) The binary protein-protein interaction landscape of Escherichia coli. Nat. Biotechnol. 32 285-90 PubMed GONUTS page
- ↑ 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
- ↑ Flint, DH (1994) Initial kinetic and mechanistic characterization of Escherichia coli fumarase A. Arch. Biochem. Biophys. 311 509-16 PubMed GONUTS page
- ↑ 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
- ↑ 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
