KSHA_MYCS2
ID KSHA_MYCS2 Reviewed; 383 AA.
AC A0R4R3; I7GFV9;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=3-ketosteroid-9-alpha-monooxygenase, oxygenase component {ECO:0000303|PubMed:17021205};
DE AltName: Full=3-ketosteroid-9-alpha-hydroxylase, oxygenase component {ECO:0000303|PubMed:17021205};
DE Short=KSH {ECO:0000303|PubMed:17021205};
DE AltName: Full=Androsta-1,4-diene-3,17-dione 9-alpha-hydroxylase {ECO:0000250|UniProtKB:P71875};
DE EC=1.14.15.30 {ECO:0000250|UniProtKB:P71875};
DE AltName: Full=Rieske-type oxygenase {ECO:0000250|UniProtKB:P71875};
DE Short=RO {ECO:0000250|UniProtKB:P71875};
GN Name=kshA; OrderedLocusNames=MSMEG_5925, MSMEI_5766;
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).
RN [4]
RP FUNCTION AS A 3-KETOSTEROID-9-ALPHA-HYDROXYLASE, AND DISRUPTION PHENOTYPE.
RX PubMed=17021205; DOI=10.1128/aem.00941-06;
RA Andor A., Jekkel A., Hopwood D.A., Jeanplong F., Ilkoy E., Konya A.,
RA Kurucz I., Ambrus G.;
RT "Generation of useful insertionally blocked sterol degradation pathway
RT mutants of fast-growing mycobacteria and cloning, characterization, and
RT expression of the terminal oxygenase of the 3-ketosteroid 9alpha-
RT hydroxylase in Mycobacterium smegmatis mc(2)155.";
RL Appl. Environ. Microbiol. 72:6554-6559(2006).
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:0000269|PubMed:17021205}.
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:P71875};
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:P71875};
CC Note=Binds 1 Fe cation. {ECO:0000250|UniProtKB:P71875};
CC -!- PATHWAY: Lipid metabolism; steroid biosynthesis.
CC {ECO:0000250|UniProtKB:P71875}.
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:P71875}.
CC -!- INDUCTION: Induced by KstR. {ECO:0000250|UniProtKB:P71875}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene form 4-androstene-3,17-
CC dione and 1,4-androstadiene-3,17-dione from sitosterol.
CC {ECO:0000269|PubMed:17021205}.
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DR EMBL; CP000480; ABK69965.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP42199.1; -; Genomic_DNA.
DR RefSeq; WP_003897322.1; NZ_SIJM01000017.1.
DR RefSeq; YP_890151.1; NC_008596.1.
DR AlphaFoldDB; A0R4R3; -.
DR SMR; A0R4R3; -.
DR STRING; 246196.MSMEI_5766; -.
DR EnsemblBacteria; ABK69965; ABK69965; MSMEG_5925.
DR EnsemblBacteria; AFP42199; AFP42199; MSMEI_5766.
DR GeneID; 66737212; -.
DR KEGG; msg:MSMEI_5766; -.
DR KEGG; msm:MSMEG_5925; -.
DR PATRIC; fig|246196.19.peg.5765; -.
DR eggNOG; COG4638; Bacteria.
DR OMA; AVYQMRR; -.
DR OrthoDB; 691776at2; -.
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:0050292; F:steroid 9-alpha-monooxygenase activity; IMP:UniProtKB.
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; IMP:UniProtKB.
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; Cholesterol metabolism; Iron; Iron-sulfur; Lipid degradation;
KW Lipid metabolism; Metal-binding; Oxidoreductase; Reference proteome;
KW Steroid metabolism; Sterol metabolism.
FT CHAIN 1..383
FT /note="3-ketosteroid-9-alpha-monooxygenase, oxygenase
FT component"
FT /id="PRO_0000404099"
FT DOMAIN 24..126
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 65
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
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 84
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 87
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 173
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:F1CMY8"
FT BINDING 179
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P71875"
FT BINDING 184
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P71875"
FT BINDING 302
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P71875"
SQ SEQUENCE 383 AA; 43668 MW; 8FB2C36D92D6D590 CRC64;
MATETVGIRE IDTGALPDRY ARGWHCLGPV KNFSDGKPHS VNIFGTKLVV FADSKGELNV
LDAYCRHMGG DLSKGTVKGD EVACPFHDWR WGGDGKCKLV PYAKRTPRLA RTRSWHTDVR
GGLLFVWHDH EGNPPQPEVR IPEIPEWHSG EWTDWKWNSM LIEGSNCREI IDNVTDMAHF
FYIHFGLPTY FKNVFEGHIA SQYLHNVGRP DVNDLGTAYG EAKLDSEASY FGPSFMINWL
HNTYGEFKAE SILINCHYPV TQDSFVLQWG VIVEKPKGLD DATTEKLADA FTEGVSKGFL
QDVEIWKHKT RIDNPLLVEE DGAVYQMRRW YQQFYVDVAD ITPDMTDRFE MEVDTTAAVE
KWNIEVQENL KAQAEAEKAE QSS
