UniProt ID: Q9YHT4 |
FUNCTION: Catalyzes the pyridoxal 5'-phosphate (PLP)-dependent condensation of succinyl-CoA and glycine to form aminolevulinic acid (ALA), with CoA and CO2 as by-products (By similarity). Contributes significantly to heme formation during erythropoiesis (By similarity). {ECO:0000250|UniProtKB:P22557}. CATALYTIC ACTIVITY: Reaction=glycine + H(+) + succinyl-CoA = 5-aminolevulinate + CO2 + CoA; Xref=Rhea:RHEA:12921, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:57305, ChEBI:CHEBI:356416; EC=2.3.1.37; Evidence={ECO:0000250|UniProtKB:P22557}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12922; Evidence={ECO:0000250|UniProtKB:P22557}; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P22557}; PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from glycine: step 1/1. {ECO:0000250|UniProtKB:P22557}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P22557}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P22557}; Peripheral membrane protein {ECO:0000250|UniProtKB:P22557}. Note=Localizes to the matrix side of the mitochondrion inner membrane. {ECO:0000250|UniProtKB:P22557}. DOMAIN: C-terminus is a mobile self-inhibitory loop which interferes directly with active site. {ECO:0000250|UniProtKB:P22557}. SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. {ECO:0000305}. SEQUENCE CAUTION: Sequence=AAH67149.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; |
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