| UniProt functional annotation for P80078 | |||
| UniProt code: P80078. |
| Organism: | Clostridium cochlearium. | |
| Taxonomy: | Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae; Clostridium. | |
| Function: | Catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate). {ECO:0000255|HAMAP-Rule:MF_00526, ECO:0000269|PubMed:1315276, ECO:0000269|PubMed:7880251, ECO:0000269|PubMed:8013871}. | |
| Catalytic activity: | Reaction=(2S,3S)-3-methyl-L-aspartate = L-glutamate; Xref=Rhea:RHEA:12857, ChEBI:CHEBI:29985, ChEBI:CHEBI:58724; EC=5.4.99.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00526, ECO:0000269|PubMed:7880251, ECO:0000269|PubMed:8013871}; | |
| Cofactor: | Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408; Evidence={ECO:0000255|HAMAP-Rule:MF_00526, ECO:0000269|PubMed:10467146, ECO:0000269|PubMed:11592143, ECO:0000269|PubMed:1315276, ECO:0000269|PubMed:7880251, ECO:0000269|PubMed:8013871}; | |
| Activity regulation: | Competitively inhibited by (2S,4S)-4- fluoroglutamate, 2-methyleneglutarate, (2R,3RS)-3-fluoroglutamate and (S)-3-methylitaconate. {ECO:0000269|PubMed:1315276, ECO:0000269|PubMed:7880251}. | |
| Pathway: | Amino-acid degradation; L-glutamate degradation via mesaconate pathway; acetate and pyruvate from L-glutamate: step 1/4. {ECO:0000255|HAMAP-Rule:MF_00526}. | |
| Subunit: | Heterotetramer composed of 2 epsilon subunits (GlmE) and 2 sigma subunits (GlmS). GlmE exists as a homodimer and GlmS as a monomer. {ECO:0000255|HAMAP-Rule:MF_00526, ECO:0000269|PubMed:10467146, ECO:0000269|PubMed:11592143, ECO:0000269|PubMed:1315276, ECO:0000269|PubMed:7880251, ECO:0000269|PubMed:8013871}. | |
| Similarity: | Belongs to the methylaspartate mutase GlmS subunit family. {ECO:0000255|HAMAP-Rule:MF_00526}. | |
Annotations taken from UniProtKB at the EBI.