KSHB_MYCS2
ID KSHB_MYCS2 Reviewed; 353 AA.
AC A0R525; I7GFB3;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=kshB; Synonyms=hmp; OrderedLocusNames=MSMEG_6039, MSMEI_5878;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
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; CP000480; ABK72126.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP42311.1; -; Genomic_DNA.
DR RefSeq; WP_011730993.1; NZ_SIJM01000017.1.
DR RefSeq; YP_890263.1; NC_008596.1.
DR AlphaFoldDB; A0R525; -.
DR SMR; A0R525; -.
DR STRING; 246196.MSMEI_5878; -.
DR PRIDE; A0R525; -.
DR EnsemblBacteria; ABK72126; ABK72126; MSMEG_6039.
DR EnsemblBacteria; AFP42311; AFP42311; MSMEI_5878.
DR GeneID; 66737323; -.
DR KEGG; msg:MSMEI_5878; -.
DR KEGG; msm:MSMEG_6039; -.
DR PATRIC; fig|246196.19.peg.5875; -.
DR eggNOG; COG1018; Bacteria.
DR OMA; ILACQSH; -.
DR OrthoDB; 1885467at2; -.
DR UniPathway; UPA00062; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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 Reference proteome; Steroid metabolism; Sterol metabolism.
FT CHAIN 1..353
FT /note="3-ketosteroid-9-alpha-monooxygenase, ferredoxin
FT reductase component"
FT /id="PRO_0000404101"
FT DOMAIN 8..117
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT DOMAIN 264..353
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 300
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
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 308
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 338
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 353 AA; 37562 MW; F6098EB48B4C98F3 CRC64;
MTDEPLGSHV LELQVAEVVE ETSDARSLVF TVPEGAEIAA DRLRYSPGQF LTLRVPSDRT
GSVARCYSLS SSPTTDDRLT VTVKRTADGY ASNWLCDNAH AGMRIHVLAP SGTFVPKDLD
TDFLLLAAGS GITPMMAICK SALAEGTGNV VLIYANRDEN SVIFAGALRE LAAKYPDRLT
VVHWLETVQG LPTAAGLGAL AKPFAGREAF ICGPGPFMTA AEDALRAAGT PDDHIHIEVF
KSLESDPFAA VVIPEDDGDD QGPATAVVTL DGTTHEIRWP RSAKLLDVLL DKGLDAPFSC
REGHCGACAV LKKSGEVHME INDVLEPSDL EEGLILGCQA TPVSDSVEVT YDE
