KSHB_MYCTO
ID KSHB_MYCTO Reviewed; 358 AA.
AC P9WJ92; L0TD71; P96853; Q7D594;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=3-ketosteroid-9-alpha-monooxygenase, ferredoxin reductase component {ECO:0000250|UniProtKB:P9WJ93};
DE AltName: Full=3-ketosteroid-9-alpha-hydroxylase, ferredoxin reductase component {ECO:0000250|UniProtKB:P9WJ93};
DE Short=KSH {ECO:0000250|UniProtKB:P9WJ93};
DE AltName: Full=Androsta-1,4-diene-3,17-dione 9-alpha-hydroxylase {ECO:0000250|UniProtKB:P9WJ93};
DE EC=1.14.15.30 {ECO:0000250|UniProtKB:P9WJ93};
DE AltName: Full=Rieske-type oxygenase {ECO:0000250|UniProtKB:P9WJ93};
DE Short=RO {ECO:0000250|UniProtKB:P9WJ93};
GN Name=hmp; Synonyms=kshB; OrderedLocusNames=MT3676;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Involved in the degradation of cholesterol. Catalyzes the
CC introduction of a 9a-hydroxyl moiety into 1,4-androstadiene-3,17-dione
CC (ADD) to yield the 9alpha-hydroxy-1,4-androstadiene-3,17-dione (9OHADD)
CC intermediate which spontaneously form 3-hydroxy-9,10-seconandrost-
CC 1,3,5(10)-triene-9,17-dione (HSA) via the meta-cleavage of ring B with
CC concomitant aromatization of ring A. {ECO:0000250|UniProtKB:P9WJ93}.
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:0000250|UniProtKB:P9WJ93};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P9WJ93};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P9WJ93};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00465};
CC Note=Binds 1 2Fe-2S cluster. {ECO:0000255|PROSITE-ProRule:PRU00465};
CC -!- PATHWAY: Lipid metabolism; steroid biosynthesis.
CC {ECO:0000250|UniProtKB:P9WJ93}.
CC -!- SUBUNIT: Monomer. 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:P9WJ93}.
CC -!- INDUCTION: Induced by KstR. {ECO:0000250|UniProtKB:P9WJ93}.
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DR EMBL; AE000516; AAK48035.1; -; Genomic_DNA.
DR PIR; A70606; A70606.
DR RefSeq; WP_003900102.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WJ92; -.
DR SMR; P9WJ92; -.
DR EnsemblBacteria; AAK48035; AAK48035; MT3676.
DR KEGG; mtc:MT3676; -.
DR PATRIC; fig|83331.31.peg.3958; -.
DR HOGENOM; CLU_003827_14_1_11; -.
DR UniPathway; UPA00062; -.
DR Proteomes; UP000001020; Chromosome.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW 2Fe-2S; Cholesterol metabolism; FAD; Flavoprotein; Iron; Iron-sulfur;
KW Lipid degradation; Lipid metabolism; Metal-binding; Oxidoreductase;
KW Steroid metabolism; Sterol metabolism.
FT CHAIN 1..358
FT /note="3-ketosteroid-9-alpha-monooxygenase, ferredoxin
FT reductase component"
FT /id="PRO_0000427870"
FT DOMAIN 12..124
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT DOMAIN 269..358
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 305
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 310
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 313
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 343
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 358 AA; 38265 MW; 182A799D00ADC8B2 CRC64;
MTEAIGDEPL GDHVLELQIA EVVDETDEAR SLVFAVPDGS DDPEIPPRRL RYAPGQFLTL
RVPSERTGSV ARCYSLCSSP YTDDALAVTV KRTADGYASN WLCDHAQVGM RIHVLAPSGN
FVPTTLDADF LLLAAGSGIT PIMSICKSAL AEGGGQVTLL YANRDDRSVI FGDALRELAA
KYPDRLTVLH WLESLQGLPS ASALAKLVAP YTDRPVFICG PGPFMQAARD ALAALKVPAQ
QVHIEVFKSL ESDPFAAVKV DDSGDEAPAT AVVELDGQTH TVSWPRTAKL LDVLLAAGLD
APFSCREGHC GACACTLRAG KVNMGVNDVL EQQDLDEGLI LACQSRPESD SVEVTYDE
