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UniProt functional annotation for P0AB77 | ||
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| UniProt code: P0AB77. |
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| Organism: | |
Escherichia coli (strain K12). |
| Taxonomy: | |
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. |
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| Function: | |
Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA. {ECO:0000255|HAMAP-Rule:MF_00985, ECO:0000269|PubMed:2104756}. |
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| Catalytic activity: | |
Reaction=acetyl-CoA + glycine = (2S)-2-amino-3-oxobutanoate + CoA; Xref=Rhea:RHEA:20736, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57305, ChEBI:CHEBI:78948; EC=2.3.1.29; Evidence={ECO:0000255|HAMAP-Rule:MF_00985, ECO:0000269|PubMed:2104756}; |
| Cofactor: | |
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000255|HAMAP-Rule:MF_00985, ECO:0000269|PubMed:2104756}; Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000255|HAMAP- Rule:MF_00985, ECO:0000269|PubMed:2104756}; |
| Pathway: | |
Amino-acid degradation; L-threonine degradation via oxydo- reductase pathway; glycine from L-threonine: step 2/2. {ECO:0000255|HAMAP-Rule:MF_00985}. |
| Subunit: | |
Homodimer. {ECO:0000255|HAMAP-Rule:MF_00985, ECO:0000269|PubMed:11318637, ECO:0000269|PubMed:2104756}. |
| Similarity: | |
Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. {ECO:0000255|HAMAP-Rule:MF_00985}. |
Annotations taken from UniProtKB at the EBI.