ID   KSHA2_RHORH             Reviewed;         399 AA.
AC   F1CMX6;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 29.
DE   RecName: Full=Probable 3-ketosteroid-9-alpha-monooxygenase, oxygenase component {ECO:0000303|PubMed:21642460};
DE   AltName: Full=Probable 3-ketosteroid-9-alpha-hydroxylase, oxygenase component {ECO:0000303|PubMed:21642460};
DE            Short=KSH {ECO:0000303|PubMed:21642460};
DE            EC=1.14.13.- {ECO:0000305|PubMed:21642460};
DE   AltName: Full=Rieske-type oxygenase {ECO:0000305|PubMed:21642460};
DE            Short=RO {ECO:0000305|PubMed:21642460};
GN   Name=kshA {ECO:0000303|PubMed:21642460};
GN   Synonyms=kshA2 {ECO:0000303|PubMed:21642460};
OS   Rhodococcus rhodochrous.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=1829;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC   STRAIN=DSM 43269;
RX   PubMed=21642460; DOI=10.1128/jb.00274-11;
RA   Petrusma M., Hessels G., Dijkhuizen L., van der Geize R.;
RT   "Multiplicity of 3-ketosteroid-9alpha-hydroxylase enzymes in Rhodococcus
RT   rhodochrous DSM43269 for specific degradation of different classes of
RT   steroids.";
RL   J. Bacteriol. 193:3931-3940(2011).
CC   -!- FUNCTION: Could catalyze the introduction of a 9alpha-hydroxyl moiety
CC       into the ring B of 3-ketosteroid substrates.
CC       {ECO:0000305|PubMed:21642460}.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00628};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU00628};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000250|UniProtKB:F1CMY8};
CC       Note=Binds 1 Fe cation. {ECO:0000250|UniProtKB:F1CMY8};
CC   -!- SUBUNIT: Homotrimer. The two-component system 3-ketosteroid-9-alpha-
CC       monooxygenase is composed of an oxygenase component KshA and a
CC       reductase component KshB. {ECO:0000250|UniProtKB:F1CMY8}.
CC   -!- INDUCTION: By cholic acid. {ECO:0000269|PubMed:21642460}.
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DR   EMBL; HQ425874; ADY18316.1; -; Genomic_DNA.
DR   AlphaFoldDB; F1CMX6; -.
DR   SMR; F1CMX6; -.
DR   BRENDA; 1.14.15.30; 5395.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProt.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR   GO; GO:0008203; P:cholesterol metabolic process; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.102.10.10; -; 1.
DR   InterPro; IPR045605; KshA-like_C.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   Pfam; PF19298; KshA_C; 1.
DR   Pfam; PF00355; Rieske; 1.
DR   SUPFAM; SSF50022; SSF50022; 1.
DR   PROSITE; PS51296; RIESKE; 1.
PE   2: Evidence at transcript level;
KW   2Fe-2S; Iron; Iron-sulfur; Lipid degradation; Lipid metabolism;
KW   Metal-binding; NAD; Oxidoreductase; Steroid metabolism.
FT   CHAIN           1..399
FT                   /note="Probable 3-ketosteroid-9-alpha-monooxygenase,
FT                   oxygenase component"
FT                   /id="PRO_0000438400"
FT   DOMAIN          26..128
FT                   /note="Rieske"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         67
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         69
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         86
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         89
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         175
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:F1CMY8"
FT   BINDING         181
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:F1CMY8"
FT   BINDING         186
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:F1CMY8"
FT   BINDING         307
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:F1CMY8"
SQ   SEQUENCE   399 AA;  44753 MW;  6777F0704FB53D2E CRC64;
     MGSTDTEDQV RTIDVGTPPE RYARGWHCLG LVRDFADGKP HQVDAFGTSL VVFAGEDGKL
     NVLDAYCRHM GGNLAQGSVK GNTIACPFHD WRWRGDGKCA EIPYARRVPP LARTRTWPVA
     EVSGQLFVWH DPQGSKPPAE LAVPEVPTYG DPGWTDWVWN SIEVTGSHCR EIVDNVVDMA
     HFFYVHYGMP TYFRNVFEGH TATQVMRSLP RADAVGVSQA TNYSAESRSD ATYYGPSYMI
     DKLWSAGRDP ESTPNIYLIN CHYPISPTSF RLQYGVMVER PEGVPPEQAE QIAQAVAQGV
     AIGFEQDVEI WKNKSRIDNP LLCEEDGPVY QLRRWYEQFY VDVEDIRPEM VNRFEYEIDT
     TRALTSWQAE VDENVAAGRS AFAPNLTRAR EAASAESGS