KSHA3_RHORH
ID KSHA3_RHORH Reviewed; 382 AA.
AC F1CMX8;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=3-ketosteroid-9-alpha-monooxygenase, oxygenase component {ECO:0000303|PubMed:21642460};
DE AltName: Full=3-ketosteroid-9-alpha-hydroxylase, oxygenase component {ECO:0000303|PubMed:21642460};
DE Short=KSH {ECO:0000303|PubMed:21642460};
DE AltName: Full=Androsta-1,4-diene-3,17-dione 9-alpha-hydroxylase {ECO:0000303|PubMed:21642460};
DE EC=1.14.15.30 {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=kshA3 {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, CATALYTIC ACTIVITY, INDUCTION,
RP AND SUBSTRATE SPECIFICITY.
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: In vitro, catalyzes the introduction of a 9alpha-hydroxyl
CC moiety into the ring B of 3-ketosteroid substrates such as 1,4-
CC androstadiene-3,17-dione (ADD), 4-androstene-3,17-dione (AD), 4-
CC androstene-17beta-ol-3-one (testosterone), 4-pregnene-3,20-dione
CC (progesterone), 23,24-bisnorcholesta-4-ene-22-oate and 23,24-
CC bisnorcholesta-1,4-diene-22-oate. {ECO:0000269|PubMed:21642460}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=androsta-1,4-diene-3,17-dione + 2 H(+) + O2 + 2 reduced [2Fe-
CC 2S]-[ferredoxin] = 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + H2O
CC + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:32199, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738, ChEBI:CHEBI:40799, ChEBI:CHEBI:63641;
CC EC=1.14.15.30; Evidence={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 4-androstene-3,17-dione (AD).
CC {ECO:0000269|PubMed:21642460}.
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DR EMBL; HQ425875; ADY18318.1; -; Genomic_DNA.
DR RefSeq; WP_059382556.1; NZ_LT906450.1.
DR AlphaFoldDB; F1CMX8; -.
DR SMR; F1CMX8; -.
DR GeneID; 66793291; -.
DR BRENDA; 1.14.15.30; 5395.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0036200; F:3-ketosteroid 9-alpha-monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
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 1: Evidence at protein level;
KW 2Fe-2S; Iron; Iron-sulfur; Lipid degradation; Lipid metabolism;
KW Metal-binding; Oxidoreductase; Steroid metabolism.
FT CHAIN 1..382
FT /note="3-ketosteroid-9-alpha-monooxygenase, oxygenase
FT component"
FT /id="PRO_0000438401"
FT DOMAIN 20..122
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 61
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 63
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 80
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 83
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 169
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:F1CMY8"
FT BINDING 175
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:F1CMY8"
FT BINDING 180
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:F1CMY8"
FT BINDING 298
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:F1CMY8"
SQ SEQUENCE 382 AA; 43954 MW; 79F3CF17B5675600 CRC64;
MAQIREIDVG EVRTRFARGW HCLGLSRTFK DGKPHAVEAF GTKLVVWADS NGEPKVLDAY
CRHMGGDLSQ GEIKGDSVAC PFHDWRWGGN GKCTDIPYAR RVPPLARTRS WITMEKHGQL
FVWNDPEGNT PPPEVTIPEI EQYGSDEWTD WTWNQIRIEG SNCREIIDNV VDMAHFFYIH
YAFPTFFKNV FEGHIAEQYL NTRGRPDKGM ATQYGLESTL ESYAAYYGPS YMINPLKNNY
GGYQTESVLI NCHYPITHDS FMLQYGIIVK KPQGMSPEQS DVLAAKLTEG VGEGFLQDVE
IWKNKTKIEN PLLCEEDGPV YQLRRWYEQF YVDVADVTEK MTGRFEFEVD TAKANEAWEK
EVAENLERKK REEEQGKQEA EV
