P71875 · KSHA_MYCTU
- Protein3-ketosteroid-9-alpha-monooxygenase, oxygenase component
- GenekshA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids386 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in the degradation of cholesterol. Catalyzes the introduction of a 9a-hydroxyl moiety into 1,4-androstadiene-3,17-dione (ADD) to yield the 9alpha-hydroxy-1,4-androstadiene-3,17-dione (9OHADD) intermediate which spontaneously form 3-hydroxy-9,10-seconandrost-1,3,510-triene-9,17-dione (HSA) via the meta-cleavage of ring B with concomitant aromatization of ring A. KSH is also able to use 4-androstene-3,17-dione (AD), 3-oxo-23,24-bisnorcholesta-4-en-22-oate (4-BNC), 3-oxo-23,24-bisnorcholesta-1,4-dien-22-oate (1,4-BNC), 3-oxo-23,24-bisnorcholesta-4-en-22-oyl-coenzyme A thioester (4-BNC-CoA) and 3-oxo-23,24-bisnorcholesta-1,4-dien-22-oyl-coenzyme A thioester (1,4-BNC-CoA) as substrates.
Catalytic activity
- androsta-1,4-diene-3,17-dione + 2 reduced [2Fe-2S]-[ferredoxin] + O2 + 2 H+ = 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized [2Fe-2S]-[ferredoxin] + H2OThis reaction proceeds in the forward direction.
- androst-4-ene-3,17-dione + NADH + O2 + H+ = 9alpha-hydroxy-androst-4-ene-3,17-dione + NAD+ + H2OThis reaction proceeds in the forward direction.
- 3-oxochol-4-en-22-oate + NADH + O2 + H+ = 9alpha-hydroxy-3-oxochol-4-en-22-oate + NAD+ + H2OThis reaction proceeds in the forward direction.
- 3-oxochola-1,4-dien-22-oate + NADH + O2 + H+ = 9alpha-hydroxy-3-oxochola-1,4-dien-22-oate + NAD+ + H2OThis reaction proceeds in the forward direction.
- 3-oxochol-4-en-22-oyl-CoA + NADH + O2 + H+ = 9alpha-hydroxy-3-oxochol-4-en-22-oyl-CoA + NAD+ + H2OThis reaction proceeds in the forward direction.
- 3-oxochola-1,4-dien-22-oyl-CoA + NADH + O2 + H+ = 9alpha-hydroxy-3-oxochola-1,4-dien-22-oyl-CoA + NAD+ + H2OThis reaction proceeds in the forward direction.
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 [2Fe-2S] cluster per subunit.
Note: Binds 1 Fe cation.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
3 μM | 4-BNC | 7 | 22 | |||
6.8 μM | 4-BNC-CoA | 7 | 22 | |||
17 μM | 1,4-BNC-CoA | 7 | 22 | |||
24 μM | AD | 7 | 25 | |||
70 μM | 1,4-BNC | 7 | 22 | |||
110 μM | ADD | 7 | 25 |
kcat is 2.7 sec-1 for 1,4-BNC-CoA as substrate (at pH 7 and at 22 degrees Celsius) (PubMed:21987574).
kcat is 0.8 sec-1 for ADD as substrate (at pH 7 and at 25 degrees Celsius) (PubMed:19234303).
kcat is 0.61 sec-1 for 4-BNC-CoA as substrate (at pH 7 and at 22 degrees Celsius) (PubMed:21987574).
kcat is 0.25 sec-1 for 1,4-BNC as substrate (at pH 7 and at 22 degrees Celsius) (PubMed:21987574).
kcat is 0.08 sec-1 for 4-BNC as substrate (at pH 7 and at 22 degrees Celsius) (PubMed:21987574).
kcat is 0.07 sec-1 for AD as substrate (at pH 7 and at 25 degrees Celsius) (PubMed:19234303).
kcat is 0.8 sec-1 for ADD as substrate (at pH 7 and at 25 degrees Celsius) (PubMed:19234303).
kcat is 0.61 sec-1 for 4-BNC-CoA as substrate (at pH 7 and at 22 degrees Celsius) (PubMed:21987574).
kcat is 0.25 sec-1 for 1,4-BNC as substrate (at pH 7 and at 22 degrees Celsius) (PubMed:21987574).
kcat is 0.08 sec-1 for 4-BNC as substrate (at pH 7 and at 22 degrees Celsius) (PubMed:21987574).
kcat is 0.07 sec-1 for AD as substrate (at pH 7 and at 25 degrees Celsius) (PubMed:19234303).
Pathway
Lipid metabolism; steroid biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 67 | [2Fe-2S] cluster (UniProtKB | ChEBI) | |||
Binding site | 69 | [2Fe-2S] cluster (UniProtKB | ChEBI) | |||
Binding site | 86 | [2Fe-2S] cluster (UniProtKB | ChEBI) | |||
Binding site | 89 | [2Fe-2S] cluster (UniProtKB | ChEBI) | |||
Binding site | 175 | Fe cation (UniProtKB | ChEBI) | |||
Binding site | 181 | Fe cation (UniProtKB | ChEBI) | |||
Binding site | 186 | Fe cation (UniProtKB | ChEBI) | |||
Binding site | 304 | Fe cation (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 2 iron, 2 sulfur cluster binding | |
Molecular Function | 3-ketosteroid 9-alpha-monooxygenase activity | |
Molecular Function | iron ion binding | |
Molecular Function | ketosteroid monooxygenase activity | |
Molecular Function | oxidoreductase activity | |
Biological Process | cholesterol catabolic process | |
Biological Process | protein homotrimerization | |
Biological Process | response to cholesterol | |
Biological Process | steroid biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Chemistry
Names & Taxonomy
Protein names
- Recommended name3-ketosteroid-9-alpha-monooxygenase, oxygenase component
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium > Mycobacterium tuberculosis complex
Accessions
- Primary accessionP71875
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000404098 | 1-386 | 3-ketosteroid-9-alpha-monooxygenase, oxygenase component | ||
Proteomic databases
Expression
Induction
Induced by KstR.
Structure
Sequence
- Sequence statusComplete
- Length386
- Mass (Da)44,268
- Last updated1997-07-01 v2
- MD5 Checksum10002F3D8860021E0D543571049511FD
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL123456 EMBL· GenBank· DDBJ | CCP46348.1 EMBL· GenBank· DDBJ | Genomic DNA |