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UniProt functional annotation for Q70AC7 | ||
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| UniProt code: Q70AC7. |
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| Organism: | |
Propionibacterium freudenreichii subsp. shermanii. |
| Taxonomy: | |
Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae; Propionibacterium. |
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| Function: | |
The 5S subunit specifically catalyzes the transfer of the carboxyl group from biotin of the 1.3S subunit to pyruvate to form oxaloacetate and 1.3S biotin. |
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| Catalytic activity: | |
Reaction=(S)-methylmalonyl-CoA + pyruvate = oxaloacetate + propanoyl- CoA; Xref=Rhea:RHEA:20764, ChEBI:CHEBI:15361, ChEBI:CHEBI:16452, ChEBI:CHEBI:57327, ChEBI:CHEBI:57392; EC=2.1.3.1; |
| Cofactor: | |
Name=Co(2+); Xref=ChEBI:CHEBI:48828; Note=Binds 1 Co(2+) ion per subunit.; |
| Subunit: | |
Homodimer. Transcarboxylase is composed of three subunits: 1.3S, 5S, and 12S. The core of the enzyme is composed of six 12S subunits. On each side of the core there are three pairs of 5S subunits. Each 5S dimer is attached to the core by two 1.3S subunits. Thus the total number of chains is 30 (6 + 12 + 12). {ECO:0000269|PubMed:15329673}. |
| Ptm: | |
Lys-184 is carboxylated in the free enzyme and helps to coordinate the cobalt ion. Lys-184 is partially carboxylated in the complex with pyruvate, but is not carboxylated in the oxaloacetate-bound form. {ECO:0000269|PubMed:15329673}. |
| Sequence caution: | |
Sequence=AAA03174.1; Type=Frameshift; Evidence={ECO:0000305}; |
Annotations taken from UniProtKB at the EBI.