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Literature summary extracted from
- Heme A biosynthesis (2012), Biochim. Biophys. Acta, 1817, 920-927 .
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.17.99.9 | C191A/C197A | low activity | Bacillus subtilis |
| 1.17.99.9 | C35A | low activity | Bacillus subtilis |
| 1.17.99.9 | C35A/C42A | no detectable activity | Bacillus subtilis |
| 1.17.99.9 | H123L | no detectable activity | Bacillus subtilis |
| 1.17.99.9 | H123M | no detectable activity | Bacillus subtilis |
| 1.17.99.9 | H216L | no detectable activity | Bacillus subtilis |
| 1.17.99.9 | H216M | low activity | Bacillus subtilis |
| 1.17.99.9 | H278L | low activity | Bacillus subtilis |
| 1.17.99.9 | H278M | low activity | Bacillus subtilis |
| 1.17.99.9 | H60L | no detectable activity | Bacillus subtilis |
| 1.17.99.9 | H60M | low activity | Bacillus subtilis |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.17.99.9 | cytoplasm | - |
Saccharomyces cerevisiae | 5737 | - |
| 1.17.99.9 | cytoplasm | - |
Bacillus subtilis | 5737 | - |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.17.99.9 | ferroheme o + H2O + 2 acceptor | Bacillus subtilis | overall reaction. The enzyme is involved in biosynthesis of heme A, an obligatory cofactor in eukaryotic cytochrome c oxidase. The enzyme catalyses the conversion of heme o to heme a by two successive hydroxylations of the methyl group at C-8, using water as the oxygen source. The first hydroxylation forms heme i, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme a | ferroheme a + 2 reduced acceptor | - |
? |  |
| 1.17.99.9 | ferroheme o + H2O + 2 acceptor | Bacillus subtilis 168 | overall reaction. The enzyme is involved in biosynthesis of heme A, an obligatory cofactor in eukaryotic cytochrome c oxidase. The enzyme catalyses the conversion of heme o to heme a by two successive hydroxylations of the methyl group at C-8, using water as the oxygen source. The first hydroxylation forms heme i, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme a | ferroheme a + 2 reduced acceptor | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.17.99.9 | Aeropyrum pernix | - |
- |
- |
| 1.17.99.9 | Bacillus subtilis | P12946 | - |
- |
| 1.17.99.9 | Bacillus subtilis 168 | P12946 | - |
- |
| 1.17.99.9 | Halobacterium salinarum | - |
- |
- |
| 1.17.99.9 | Saccharomyces cerevisiae | - |
- |
- |
| 1.17.99.9 | Schizosaccharomyces pombe | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.17.99.9 | ferroheme i + H2O + acceptor | the enzyme catalyses the conversion of heme o to heme a by two successive hydroxylations of the methyl group at C-8, using water as the oxygen source. The first hydroxylation forms heme i, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group | Bacillus subtilis | hydroxyferroheme i + reduced acceptor | - |
? | |
| 1.17.99.9 | ferroheme i + H2O + acceptor | the enzyme catalyses the conversion of heme o to heme a by two successive hydroxylations of the methyl group at C-8, using water as the oxygen source. The first hydroxylation forms heme i, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group | Bacillus subtilis 168 | hydroxyferroheme i + reduced acceptor | - |
? | |
| 1.17.99.9 | ferroheme o + H2O + 2 acceptor | overall reaction. The enzyme is involved in biosynthesis of heme A, an obligatory cofactor in eukaryotic cytochrome c oxidase. The enzyme catalyses the conversion of heme o to heme a by two successive hydroxylations of the methyl group at C-8, using water as the oxygen source. The first hydroxylation forms heme i, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme a | Bacillus subtilis | ferroheme a + 2 reduced acceptor | - |
? | |
| 1.17.99.9 | ferroheme o + H2O + 2 acceptor | overall reaction. The enzyme catalyses the conversion of heme o to heme a by two successive hydroxylations of the methyl group at C-8, using water as the oxygen source. The first hydroxylation forms heme i, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme a | Bacillus subtilis | ferroheme a + 2 reduced acceptor | - |
? | |
| 1.17.99.9 | ferroheme o + H2O + 2 acceptor | overall reaction. The enzyme is involved in biosynthesis of heme A, an obligatory cofactor in eukaryotic cytochrome c oxidase. The enzyme catalyses the conversion of heme o to heme a by two successive hydroxylations of the methyl group at C-8, using water as the oxygen source. The first hydroxylation forms heme i, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme a | Bacillus subtilis 168 | ferroheme a + 2 reduced acceptor | - |
? | |
| 1.17.99.9 | ferroheme o + H2O + 2 acceptor | overall reaction. The enzyme catalyses the conversion of heme o to heme a by two successive hydroxylations of the methyl group at C-8, using water as the oxygen source. The first hydroxylation forms heme i, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme a | Bacillus subtilis 168 | ferroheme a + 2 reduced acceptor | - |
? | |
| 1.17.99.9 | ferroheme o + H2O + acceptor | the enzyme catalyses the conversion of heme o to heme a by two successive hydroxylations of the methyl group at C-8, using water as the oxygen source. The first hydroxylation forms heme i, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group | Bacillus subtilis | ferroheme i + reduced acceptor | - |
? | |
| 1.17.99.9 | ferroheme o + H2O + acceptor | the enzyme catalyses the conversion of heme o to heme a by two successive hydroxylations of the methyl group at C-8, using water as the oxygen source. The first hydroxylation forms heme i, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group | Bacillus subtilis 168 | ferroheme i + reduced acceptor | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.17.99.9 | homodimer | - |
Halobacterium salinarum |
| 1.17.99.9 | homodimer | - |
Aeropyrum pernix |
| 1.17.99.9 | homodimer | - |
Bacillus subtilis |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.17.99.9 | COX15 | - |
Saccharomyces cerevisiae |
| 1.17.99.9 | COX15 | - |
Schizosaccharomyces pombe |
| 1.17.99.9 | ctaA | - |
Halobacterium salinarum |
| 1.17.99.9 | ctaA | - |
Schizosaccharomyces pombe |
| 1.17.99.9 | ctaA | - |
Aeropyrum pernix |
| 1.17.99.9 | ctaA | - |
Bacillus subtilis |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.17.99.9 | heme | - |
Aeropyrum pernix | |
| 1.17.99.9 | heme a | between 0.2 and 1.95 mol heme B per mol CtaA polypeptide and up to 0.2 mol heme A per mol enzyme (CtaA) | Bacillus subtilis | |
| 1.17.99.9 | heme b | between 0.2 and 1.95 mol heme B per mol CtaA polypeptide and up to 0.2 mol heme A per mol enzyme (CtaA) | Bacillus subtilis | |
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Release 2023.1 (January 2023)
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