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Information on EC 1.14.13.222 - aurachin C monooxygenase/isomerase and Organism(s) Mycobacterium goodii and UniProt Accession E9RFS9

for references in articles please use BRENDA:EC1.14.13.222
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IUBMB Comments
The aurachin C monooxygenase from the bacterium Stigmatella aurantiaca accepts both NADH and NADPH as cofactor, but has a preference for NADH. It catalyses the initial steps in the conversion of aurachin C to aurachin B. The FAD-dependent monooxygenase catalyses the epoxidation of the C2-C3 double bond of aurachin C, which is followed by a semipinacol rearrangement, causing migration of the farnesyl group from C3 to C4.
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Mycobacterium goodii
UNIPROT: E9RFS9 not found.
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The taxonomic range for the selected organisms is: Mycobacterium goodii
The enzyme appears in selected viruses and cellular organisms
Synonyms
mimabcd, msmeg_1971, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aurachin C monooxygenase
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-
-
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MimABCD
E9RFS9; E9RFT0; E9RFT1; E9RFT2
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SYSTEMATIC NAME
IUBMB Comments
aurachin C:NAD(P)H:oxygen oxidoreductase (4-hydroxy-2-methyl-3-oxo-4-farnesyl-3,4-dihydroquinoline-1-oxide-forming)
The aurachin C monooxygenase from the bacterium Stigmatella aurantiaca accepts both NADH and NADPH as cofactor, but has a preference for NADH. It catalyses the initial steps in the conversion of aurachin C to aurachin B. The FAD-dependent monooxygenase catalyses the epoxidation of the C2-C3 double bond of aurachin C, which is followed by a semipinacol rearrangement, causing migration of the farnesyl group from C3 to C4.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
E9RFS9; E9RFT0; E9RFT1; E9RFT2
a pair of motif sequences (Glu-X-X-His) coordinate to the binuclear iron center at the active site of subunit PrmA
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
E9RFS9 i.e. oxygenase large subunit MimA, E9RFT0 i.e. reductase MimB, E9RFT1 i.e. oxygenase small subunit MimC, E9RFT2 i.e. coupling protein MimD
E9RFS9; E9RFT0; E9RFT1; E9RFT2
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
E9RFS9; E9RFT0; E9RFT1; E9RFT2
binuclear iron monooxygenase gene cluster MimABCD plays essential roles in propane and acetone metabolism. A MimA deletion mutant has lost the ability to grow on propane, acetone or methylethylketone as source of carbon and energy
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Furuya, T.; Hirose, S.; Osanai, H.; Semba, H.; Kino, K.
Identification of the monooxygenase gene clusters responsible for the regioselective oxidation of phenol to hydroquinone in mycobacteria
Appl. Environ. Microbiol.
77
1214-1220
2011
Mycolicibacterium smegmatis (A0QTU8), Mycobacterium goodii (E9RFS9 and E9RFT0 and E9RFT1 and E9RFT2), Mycolicibacterium smegmatis ATCC 700084 (A0QTU8), Mycobacterium goodii 12523 (E9RFS9 and E9RFT0 and E9RFT1 and E9RFT2)
Manually annotated by BRENDA team