General Information of DME (ID: DME1550) |
DME Name |
Cytochrome P450 142A2 (cyp142), Mycolicibacterium smegmatis
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Synonyms |
Cytochrome P450 family 142 subfamily A member 2; Cholest-4-en-3-one C26-monooxygenase 142A2; Cholest-4-en-3-one C26-monooxygenase [(25R)-3-oxocholest-4-en-26-oate forming] 142A2; Cholesterol C26-monooxygenase 142A2; Cholesterol C26-monooxygenase [(25R)-3beta-hydroxycholest-5-en-26-oate forming] 142A2; MSMEG_5918; Steroid C26-monooxygenase 142A2; Steroid C27-monooxygenase 142A2; cyp142A2
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Gene Name |
cyp142
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UniProt ID |
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Gene ID |
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EC Number |
EC: 1.14.15.28 (Click to Show/Hide the Complete EC Tree)
Oxidoreductase
Oxygen paired donor oxidoreductase
Iron-sulfur protein donor oxidoreductase
EC: 1.14.15.28
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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)
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Interactions between Host Protein and DME (HOSPPI)
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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 |
MTQMLTRPDVDLVNGMFYADGGAREAYRWMRANEPVFRDRNGLAAATTYQAVLDAERNPE LFSSTGGIRPDQPGMPYMIDMDDPQHLLRRKLVNAGFTRKRVMDKVDSIGRLCDTLIDAV CERGECDFVRDIAAPLPMAVIGDMLGVLPTERDMLLKWSDDLVCGLSSHVDEAAIQKLMD TFAAYTEFTKDVITKRRAEPTDDLFSVLVNSEVEGQRMSDDEIVFETLLILIGGDETTRH TLSGGTEQLLRHRDQWDALVADVDLLPGAIEEMLRWTSPVKNMCRTLTADTVFHGTELRA GEKIMLMFESANFDESVFGDPDNFRIDRNPNSHVAFGFGTHFCLGNQLARLELRLMTERV LRRLPDLRLADDAPVPLRPANFVSGPESMPVVFTPSAPVLA
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Structure |
2YOO
; 3ZBY
; 4TRI
; 4UAX
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Pathway |
Microbial metabolism in diverse environments (msb01120 ) |
Steroid degradation (msb00984 ) |
Function |
This enzyme is a P-450 heme-thiolate protein, and it is involved in the utilization of cholesterol as the sole carbon and energy source by degrading the side chain. Primarily catalyzes the sequential oxidation of the terminal methyl of cholest-4-en-3-one into (25R)-26-hydroxycholest-4-en-3-one (alcohol), (25R)-26-oxocholest-4-en-3-one (aldehyde), to finally yield the carboxylic acid (25R)-3-oxocholest-4-en-26-oate. Also able to sequentially oxidize cholesterol itself, not only cholest-4-en-3-one.
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