CHOD_MYCTU
ID CHOD_MYCTU Reviewed; 578 AA.
AC P9WMV9; 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 47.
DE RecName: Full=Cholesterol oxidase {ECO:0000303|PubMed:17651430};
DE EC=1.1.3.6 {ECO:0000305|PubMed:17651430};
DE AltName: Full=Cholesterol isomerase;
DE EC=5.3.3.1 {ECO:0000305|PubMed:17651430};
GN Name=choD {ECO:0000303|PubMed:17651430}; OrderedLocusNames=Rv3409c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Av-Gay Y., Lim W., Davies J.E.;
RT "M.tuberculosis cholesterol oxidase.";
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [3]
RP FUNCTION IN CHOLESTEROL DEGRADATION, CATALYTIC ACTIVITY, DISRUPTION
RP PHENOTYPE, AND PATHWAY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=17651430; DOI=10.1111/j.1574-6968.2007.00865.x;
RA Brzostek A., Dziadek B., Rumijowska-Galewicz A., Pawelczyk J., Dziadek J.;
RT "Cholesterol oxidase is required for virulence of Mycobacterium
RT tuberculosis.";
RL FEMS Microbiol. Lett. 275:106-112(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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:0000269|PubMed:17651430}.
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:0000305|PubMed:17651430};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32184;
CC Evidence={ECO:0000305|PubMed:17651430};
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:0000305|PubMed:17651430};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32188;
CC Evidence={ECO:0000305|PubMed:17651430};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- PATHWAY: Steroid metabolism; cholesterol degradation.
CC {ECO:0000305|PubMed:17651430}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show attenuated
CC pathogenicity in peritoneal macrophages. {ECO:0000269|PubMed:17651430}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. Highly divergent.
CC {ECO:0000305}.
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DR EMBL; X99343; CAA67723.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP46231.1; -; Genomic_DNA.
DR PIR; F70736; F70736.
DR RefSeq; NP_217926.1; NC_000962.3.
DR RefSeq; WP_003418002.1; NZ_NVQJ01000027.1.
DR AlphaFoldDB; P9WMV9; -.
DR SMR; P9WMV9; -.
DR STRING; 83332.Rv3409c; -.
DR SwissLipids; SLP:000001277; -.
DR PaxDb; P9WMV9; -.
DR DNASU; 887502; -.
DR GeneID; 45427405; -.
DR GeneID; 887502; -.
DR KEGG; mtu:Rv3409c; -.
DR TubercuList; Rv3409c; -.
DR eggNOG; COG2303; Bacteria.
DR OMA; WAPRLGM; -.
DR PhylomeDB; P9WMV9; -.
DR BioCyc; MetaCyc:G185E-7686-MON; -.
DR BRENDA; 1.1.3.6; 3445.
DR UniPathway; UPA01058; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016995; F:cholesterol oxidase activity; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Cholesterol metabolism; FAD; Flavoprotein; Isomerase; Lipid metabolism;
KW Oxidoreductase; Reference proteome; Steroid metabolism; Sterol metabolism;
KW Virulence.
FT CHAIN 1..578
FT /note="Cholesterol oxidase"
FT /id="PRO_0000405326"
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
