| General Information of DME (ID: DME1549) |
| DME Name |
Cytochrome P450 125A3 (cyp125), Mycolicibacterium smegmatis
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| Synonyms |
Cytochrome P450 family 125 subfamily A member 3; Cholest-4-en-3-one 26-monooxygenase 125A3; Cholest-4-en-3-one C26-monooxygenase [(25S)-3-oxocholest-4-en-26-oate forming] 125A3; Cholesterol C26-monooxygenase 125A3; Cholesterol C26-monooxygenase [(25S)-3beta-hydroxycholest-5-en-26-oate forming] 125A3; MSMEG_5995; Steroid C26-monooxygenase 125A3; Steroid C27-monooxygenase 125A3; cyp125A3
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| Gene Name |
cyp125
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| UniProt ID |
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| Gene ID |
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| EC Number |
EC: 1.14.15.29 (Click to Show/Hide the Complete EC Tree)
Oxidoreductase
Oxygen paired donor oxidoreductase
Iron-sulfur protein donor oxidoreductase
EC: 1.14.15.29
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| Lineage |
Species: Mycolicibacterium smegmatis (Click to Show/Hide the Complete Species Lineage)
Kingdom: Bacteria
Phylum: Actinobacteria
Class: Actinobacteria
Order: Corynebacteriales
Family: Mycobacteriaceae
Genus: Mycolicibacterium
Species: Mycolicibacterium smegmatis
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Interactome(loading-time for this interactome depdends on the speed of web connection)
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Interactions between Xenobiotics and DME (XEOTIC)  Jump to Detailed Interactome Data  |
Interactions between Host Protein and DME (HOSPPI) Jump to Detailed Interactome Data |
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Click to Show/Hide the Molecular/Functional Data (Sequence/Structure/Pathway/Function) of This DME
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| Tissue Distribution |
Primarily distributed in human lung.
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| Sequence |
MPTPNIPSDFDFLDATLNLERLPVEELAELRKSEPIHWVDVPGGTGGFGDKGYWLVTKHA
DVKEVSRRSDVFGSSPDGAIPVWPQDMTREAVDLQRAVLLNMDAPQHTRLRKIISRGFTP
RAIGRLEDELRSRAQKIAQTAAAQGAGDFVEQVSCELPLQAIAELLGVPQDDRDKLFRWS
NEMTAGEDPEYADVDPAMSSFELISYAMKMAEERAVNPTEDIVTKLIEADIDGEKLSDDE
FGFFVVMLAVAGNETTRNSITHGMIAFAQNPDQWELYKKERPETAADEIVRWATPVSAFQ
RTALEDVELGGVQIKKGQRVVMSYRSANFDEEVFEDPHTFNILRSPNPHVGFGGTGAHYC
IGANLARMTINLIFNAIADNMPDLKPIGAPERLKSGWLNGIKHWQVDYTGAGKASVSGAP
GTCPVAH
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| Structure |
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| Pathway |
Microbial metabolism in diverse environments (msg01120 ) |
| Steroid degradation (msg00984 ) |
| Function |
This enzyme is a P-450 heme-thiolate protein found in several bacterial pathogens, and it is involved in degradation of the host's cholesterol. The enzyme catalyses the hydroxylation of the C-26 carbon, followed by oxidation of the alcohol to the carboxylic acid via the aldehyde intermediate, initiating the degradation of the alkyl side-chain of cholesterol . The products are exclusively in the (25S) configuration. And it also accepts cholesterol as a substrate.
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