ID   CHOD_MYCTO              Reviewed;         578 AA.
AC   P9WMV8; L0TFA8; Q57307; Q799Z3; Q7D5K5;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Cholesterol oxidase;
DE            EC=1.1.3.6 {ECO:0000250|UniProtKB:P9WMV9};
DE   AltName: Full=Cholesterol isomerase;
DE            EC=5.3.3.1 {ECO:0000250|UniProtKB:P9WMV9};
GN   Name=choD; OrderedLocusNames=MT3517;
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: Likely catalyzes the oxidation and isomerization of
CC       cholesterol to cholestenone (4-cholesten-3-one), which is an initial
CC       step in the cholesterol degradation process. Required for virulence.
CC       {ECO:0000250|UniProtKB:P9WMV9}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cholesterol + O2 = cholest-5-en-3-one + H2O2;
CC         Xref=Rhea:RHEA:32183, ChEBI:CHEBI:15379, ChEBI:CHEBI:16113,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:63906; EC=1.1.3.6;
CC         Evidence={ECO:0000250|UniProtKB:P9WMV9};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32184;
CC         Evidence={ECO:0000250|UniProtKB:P9WMV9};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cholest-5-en-3-one = cholest-4-en-3-one; Xref=Rhea:RHEA:32187,
CC         ChEBI:CHEBI:16175, ChEBI:CHEBI:63906; EC=5.3.3.1;
CC         Evidence={ECO:0000250|UniProtKB:P9WMV9};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32188;
CC         Evidence={ECO:0000250|UniProtKB:P9WMV9};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- PATHWAY: Steroid metabolism; cholesterol degradation.
CC       {ECO:0000250|UniProtKB:P9WMV9}.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family. Highly divergent.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK47855.1; -; Genomic_DNA.
DR   PIR; F70736; F70736.
DR   RefSeq; WP_003418002.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WMV8; -.
DR   SMR; P9WMV8; -.
DR   EnsemblBacteria; AAK47855; AAK47855; MT3517.
DR   GeneID; 45427405; -.
DR   KEGG; mtc:MT3517; -.
DR   PATRIC; fig|83331.31.peg.3775; -.
DR   HOGENOM; CLU_002483_2_0_11; -.
DR   UniPathway; UPA01058; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0016995; F:cholesterol oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004769; F:steroid delta-isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006707; P:cholesterol catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.50.50.60; -; 3.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   3: Inferred from homology;
KW   Cholesterol metabolism; FAD; Flavoprotein; Isomerase; Lipid metabolism;
KW   Oxidoreductase; Steroid metabolism; Sterol metabolism; Virulence.
FT   CHAIN           1..578
FT                   /note="Cholesterol oxidase"
FT                   /id="PRO_0000427234"
FT   REGION          529..551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        470
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P12676"
SQ   SEQUENCE   578 AA;  63024 MW;  E72695DF493397C5 CRC64;
     MKPDYDVLII GSGFGGSVTA LRLTEKGYRV GVLEAGRRFS DEEFAKTSWD LRKFLWAPRL
     GCYGIQRIHP LRNVMILAGA GVGGGSLNYA NTLYVPPEPF FADQQWSHIT DWRGELMPHY
     QQAQRMLGVV QNPTFTDADR IVKEVADEMG FGDTWVPTPV GVFFGPDGTK TPGKTVPDPY
     FGGAGPARTG CLECGCCMTG CRHGAKNTLV KNYLGLAESA GAQVIPMTTV KGFERRSDGL
     WEVRTVRTGS WLRRDRRTFT ATQLVLAAGT WGTQHLLFKM RDRGRLPGLS KRLGVLTRTN
     SESIVGAATL KVNPDLDLTH GVAITSSIHP TADTHIEPVR YGKGSNAMGL LQTLMTDGSG
     PQGTDVPRWR QLLQTASQDP RGTIRMLNPR QWSERTVIAL VMQHLDNSIT TFTKRGKLGI
     RWYSSKQGHG EPNPTWIPIG NQVTRRIAAK IDGVAGGTWG ELFNIPLTAH FLGGAVIGDD
     PEHGVIDPYH RVYGYPTLYV VDGAAISANL GVNPSLSIAA QAERAASLWP NKGETDRRPP
     QGEPYRRLAP IQPAHPVVPA DAPGALRWLP IDPVSNAG