Function

Involved in the utilization of cholesterol as the sole carbon and energy source by degrading the side chain during infection (PubMed:20843794). 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 (PubMed:20843794, PubMed:20889498). In vitro, Cyp142 catalyzes with equal preference the oxidation of both (25R)- and (25S)-26-hydroxycholest-4-en-3-one diastereomers to the corresponding carboxylic acid which is a prerequisite for entry into the beta-oxidation pathway (PubMed:20843794). Also able to sequentially oxidize cholesterol itself, not only cholest-4-en-3-one (PubMed:20843794). {ECO:0000269|PubMed:20843794, ECO:0000269|PubMed:20889498, ECO:0000269|PubMed:25210044}.

Family

Cytochrome P450 family

GO

• heme binding GO:0020037 molecular_function
• pathogenesis GO:0009405 biological_process
• cholesterol 26-hydroxylase activity GO:0031073 molecular_function
• cell wall GO:0005618 cellular_component
• iron ion binding GO:0005506 molecular_function
• steroid hydroxylase activity GO:0008395 molecular_function
• cholest-4-en-3-one 26-monooxygenase activity GO:0036199 molecular_function
• cholesterol catabolic process GO:0006707 biological_process

InterPro

• IPR036396
• IPR017972
• IPR002397
• IPR001128

UniProt

P9WPL5

GenBank

Rv3518c

EnsemblBacteria

Rv3518c

Mycobrowser

Rv3518c

Rv3518c doesn't seem to be a targeted by any drug.

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  Steroid degradation mtu00984

  mtu00984

  PATHWAY_MAP mtu00984 Steroid degradation