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Information on EC 2.5.1.141 - heme o synthase and Organism(s) Homo sapiens and UniProt Accession Q12887

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IUBMB Comments
The enzyme, found in many archaea, bacteria, and eukaryotes, produces heme o, which in many cases is further modified into heme a. In organisms that produce heme a, the enzyme forms a complex with heme a synthase. In some archaeal species the enzyme transfers a geranylgeranyl group instead of a farnesyl group.
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This record set is specific for:
Homo sapiens
UNIPROT: Q12887
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
cox10, heme o synthase, heme a:farnesyltransferase, protoheme ix farnesyltransferase, cyoe protein, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heme A:farnesyltransferase
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protoheme IX farnesyltransferase
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-
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SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesyl-diphosphate:protoheme IX farnesyltranstransferase
The enzyme, found in many archaea, bacteria, and eukaryotes, produces heme o, which in many cases is further modified into heme a. In organisms that produce heme a, the enzyme forms a complex with heme a synthase. In some archaeal species the enzyme transfers a geranylgeranyl group instead of a farnesyl group.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
heme o + diphosphate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
heme o + diphosphate
show the reaction diagram
the enzyme catalyzes the first step in the conversion of protoheme to the heme A prosthetic groups of the cytochrome c oxidase
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-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
Manually annotated by BRENDA team
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
Manually annotated by BRENDA team
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
Manually annotated by BRENDA team
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
Manually annotated by BRENDA team
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
Manually annotated by BRENDA team
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
Manually annotated by BRENDA team
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
Manually annotated by BRENDA team
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
Manually annotated by BRENDA team
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
Manually annotated by BRENDA team
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
Manually annotated by BRENDA team
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
Manually annotated by BRENDA team
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
Manually annotated by BRENDA team
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
Manually annotated by BRENDA team
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
Manually annotated by BRENDA team
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
Manually annotated by BRENDA team
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme catalyzes the first step in the conversion of protoheme to the heme A prosthetic groups of the cytochrome c oxidase
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
COX10_HUMAN
443
4
48910
Swiss-Prot
Mitochondrion (Reliability: 5)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N204K
mutation causing COX-deficiency, disease-causing mutation, the mutant gene is not able to complement the yeast cox10 null strain when expressed in low copy
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the human COX10 homolog does not complement the mutation of a yeast cox10 null mutant as efficiently as the yeast COX10 protein
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Murakami, T.; Reiter, L.T.; Lupski, J.R.
Genomic structure and expression of the human heme A:farnesyltransferase (COX10) gene
Genomics
42
161-164
1997
Homo sapiens (Q12887), Homo sapiens
Manually annotated by BRENDA team
Valnot, I.; von Kleist-Retzow, J.C.; Barrientos, A.; Gorbatyuk, M.; Taanman, J.W.; Mehaye, B.; Rustin, P.; Tzagoloff, A.; Munnich, A.; Rtig, A.
A mutation in the human heme A:farnesyltransferase gene (COX10) causes cytochrome c oxidase deficiency
Hum. Mol. Genet.
9
1245-1249
2000
Homo sapiens (Q12887), Homo sapiens
Manually annotated by BRENDA team
Glerum, D.M.; Tzagoloff, A.
Isolation of a human cDNA for heme A:farnesyltransferase by functional complementation of a yeast cox10 mutant
Proc. Natl. Acad. Sci. USA
91
8452-8456
1994
Homo sapiens (Q12887), Homo sapiens
Manually annotated by BRENDA team