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UniProt functional annotation for P0ACB2 | ||
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| UniProt code: P0ACB2. |
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| Organism: | |
Escherichia coli (strain K12). |
| Taxonomy: | |
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. |
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| Function: | |
Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen. |
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| Catalytic activity: | |
Reaction=2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen; Xref=Rhea:RHEA:24064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58126, ChEBI:CHEBI:356416; EC=4.2.1.24; |
| Cofactor: | |
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:10194344, ECO:0000269|PubMed:11444968, ECO:0000269|PubMed:11909869, ECO:0000269|PubMed:7592604}; Note=Binds 1 zinc ion per monomer. {ECO:0000269|PubMed:10194344, ECO:0000269|PubMed:11444968, ECO:0000269|PubMed:11909869, ECO:0000269|PubMed:7592604}; |
| Activity regulation: | |
Allosteric enzyme. Stimulated by magnesium ions. {ECO:0000269|PubMed:7592604}. |
| Pathway: | |
Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4. |
| Subunit: | |
Homooctamer. {ECO:0000269|PubMed:10194344, ECO:0000269|PubMed:11444968, ECO:0000269|PubMed:11909869}. |
| Similarity: | |
Belongs to the ALAD family. {ECO:0000305}. |
| Sequence caution: | |
Sequence=AAB18092.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; Sequence=BAA12842.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; |
Annotations taken from UniProtKB at the EBI.