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ECOLI:PRPC
Contents
Species (Taxon ID) | Escherichia coli (strain K12). (83333) | |
Gene Name(s) | prpC (synonyms: yahS, yzzD) | |
Protein Name(s) | 2-methylcitrate synthase
Citrate synthase 2 Methylcitrate synthase | |
External Links | ||
UniProt | P31660 | |
EMBL | U73857 U00096 AP009048 | |
PIR | E64760 | |
RefSeq | NP_414867.1 YP_488627.1 | |
ProteinModelPortal | P31660 | |
SMR | P31660 | |
DIP | DIP-10579N | |
IntAct | P31660 | |
STRING | 511145.b0333 | |
EnsemblBacteria | AAC73436 BAE76115 | |
GeneID | 12930815 947528 | |
KEGG | ecj:Y75_p0322 eco:b0333 | |
PATRIC | 32115797 | |
EchoBASE | EB1706 | |
EcoGene | EG11756 | |
eggNOG | COG0372 | |
HOGENOM | HOG000021225 | |
InParanoid | P31660 | |
KO | K01659 | |
OMA | IKGWSKK | |
OrthoDB | EOG6P8TP4 | |
PhylomeDB | P31660 | |
BioCyc | EcoCyc:G6198-MONOMER ECOL316407:JW0324-MONOMER MetaCyc:G6198-MONOMER | |
BRENDA | 2.3.3.5 | |
UniPathway | UPA00946 | |
PRO | PR:P31660 | |
Proteomes | UP000000318 UP000000625 | |
Genevestigator | P31660 | |
GO | GO:0005737 GO:0050440 GO:0004108 GO:0044262 GO:0019679 GO:0006099 | |
Gene3D | 1.10.230.10 1.10.580.10 | |
InterPro | IPR011278 IPR016142 IPR016143 IPR002020 IPR016141 IPR019810 IPR024176 | |
PANTHER | PTHR11739 | |
Pfam | PF00285 | |
PIRSF | PIRSF001369 | |
PRINTS | PR00143 | |
SUPFAM | SSF48256 | |
TIGRFAMs | TIGR01800 | |
PROSITE | PS00480 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
GO:0050440 |
2-methylcitrate synthase activity |
ECO:0000314 |
F |
Table 1 shows a significant increase in 2-methylcitrate synthase activity when the carbon source in the growth medium was propionate. |
complete | |||||
involved_in |
GO:0019679 |
propionate metabolic process, methylcitrate cycle |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0004108 |
citrate (Si)-synthase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0050440 |
2-methylcitrate synthase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0050440 |
2-methylcitrate synthase activity |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG11756 |
F |
Seeded From UniProt |
complete | ||
involved_in |
GO:0019679 |
propionate metabolic process, methylcitrate cycle |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG11756 |
P |
Seeded From UniProt |
complete | ||
involved_in |
GO:0006099 |
tricarboxylic acid cycle |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN000201223 |
P |
Seeded From UniProt |
complete | ||
involved_in |
GO:0005975 |
carbohydrate metabolic process |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN000201223 |
P |
Seeded From UniProt |
complete | ||
part_of |
GO:0005759 |
mitochondrial matrix |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
MGI:MGI:88529 |
C |
Seeded From UniProt |
complete | ||
enables |
GO:0004108 |
citrate (Si)-synthase activity |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG11756 |
F |
Seeded From UniProt |
complete | ||
enables |
GO:0050440 |
2-methylcitrate synthase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0019679 |
propionate metabolic process, methylcitrate cycle |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0050440 |
2-methylcitrate synthase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0004108 |
citrate (Si)-synthase activity |
ECO:0000316 |
genetic interaction evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0004108 |
citrate (Si)-synthase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
part_of |
GO:0005737 |
cytoplasm |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006099 |
tricarboxylic acid cycle |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0046912 |
transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
InterPro:IPR002020 |
F |
Seeded From UniProt |
complete | ||
enables |
GO:0050440 |
2-methylcitrate synthase activity |
ECO:0000501 |
evidence 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 | ||
enables |
GO:0016740 |
transferase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 1.2 1.3 Gerike, U et al. (1998) Citrate synthase and 2-methylcitrate synthase: structural, functional and evolutionary relationships. Microbiology (Reading, Engl.) 144 ( Pt 4) 929-35 PubMed GONUTS page
- ↑ 2.0 2.1 2.2 2.3 Textor, S et al. (1997) Propionate oxidation in Escherichia coli: evidence for operation of a methylcitrate cycle in bacteria. Arch. Microbiol. 168 428-36 PubMed GONUTS page
- ↑ 3.0 3.1 3.2 3.3 3.4 3.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
- ↑ Guzmán, GI et al. (2015) Model-driven discovery of underground metabolic functions in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 112 929-34 PubMed GONUTS page