CHOD_BREST
ID CHOD_BREST Reviewed; 552 AA.
AC P22637;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Cholesterol oxidase {ECO:0000303|PubMed:9535702};
DE Short=CHOD;
DE EC=1.1.3.6;
DE AltName: Full=Cholesterol isomerase;
DE EC=5.3.3.1;
DE Flags: Precursor;
GN Name=choB;
OS Brevibacterium sterolicum.
OC Bacteria; Actinobacteria; Micrococcales; Brevibacteriaceae; Brevibacterium.
OX NCBI_TaxID=1702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 46-55.
RC STRAIN=ATCC 21387 / NCIB 11161;
RX PubMed=1879703; DOI=10.1016/0378-1119(91)90397-t;
RA Ohta T., Fujishiro K., Yamaguchi K., Tamura Y., Aisaka K., Uwajima T.,
RA Hasegawa M.;
RT "Sequence of gene choB encoding cholesterol oxidase of Brevibacterium
RT sterolicum: comparison with choA of streptomyces sp. SA-COO.";
RL Gene 103:93-96(1991).
RN [2]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 46-552, AND PARTIAL
RP PROTEIN SEQUENCE.
RC STRAIN=ATCC 21387 / NCIB 11161;
RX PubMed=2271066; DOI=10.1016/0006-291x(90)90734-5;
RA Fujishiro K., Ota T., Hasegawa M., Yamaguchi K., Mizukami T., Uwajima T.;
RT "Isolation and identification of the gene of cholesterol oxidase from
RT Brevibacterium sterolicum ATCC 21387, a widely used enzyme in clinical
RT analysis.";
RL Biochem. Biophys. Res. Commun. 172:721-727(1990).
RN [3]
RP ERRATUM OF PUBMED:2271066.
RA Fujishiro K., Ota T., Hasegawa M., Yamaguchi K., Mizukami T., Uwajima T.;
RL Biochem. Biophys. Res. Commun. 173:1384-1384(1990).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9535702; DOI=10.1006/prep.1997.0855;
RA Sampson N.S., Chen X.;
RT "Increased expression of Brevibacterium sterolicum cholesterol oxidase in
RT Escherichia coli by genetic modification.";
RL Protein Expr. Purif. 12:347-352(1998).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=2051487; DOI=10.1016/0022-2836(91)90192-9;
RA Vrielink A., Lloyld L.F., Blow D.M.;
RT "Crystal structure of cholesterol oxidase from Brevibacterium sterolicum
RT refined at 1.8-A resolution.";
RL J. Mol. Biol. 219:533-554(1991).
CC -!- FUNCTION: Catalyzes the oxidation and isomerization of cholesterol to
CC cholestenone (4-cholesten-3-one), which is an initial step in the
CC cholesterol degradation process. {ECO:0000305|PubMed:9535702}.
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:9535702};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32184;
CC Evidence={ECO:0000305};
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:9535702};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32188;
CC Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- PATHWAY: Steroid metabolism; cholesterol degradation.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has been experimentally proven.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR EMBL; D00712; BAA00617.1; -; Genomic_DNA.
DR PIR; JQ1193; JQ1193.
DR PDB; 1COY; X-ray; 1.80 A; A=46-552.
DR PDB; 3COX; X-ray; 1.80 A; A=46-552.
DR PDBsum; 1COY; -.
DR PDBsum; 3COX; -.
DR AlphaFoldDB; P22637; -.
DR SMR; P22637; -.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR DrugBank; DB01708; Prasterone.
DR BioCyc; MetaCyc:MON-16891; -.
DR BRENDA; 1.1.3.6; 978.
DR UniPathway; UPA01058; -.
DR EvolutionaryTrace; P22637; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016995; F:cholesterol oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
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; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR InterPro; IPR006311; TAT_signal.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cholesterol metabolism; Direct protein sequencing; FAD;
KW Flavoprotein; Isomerase; Lipid metabolism; Oxidoreductase; Secreted;
KW Signal; Steroid metabolism; Sterol metabolism.
FT SIGNAL 1..45
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT ECO:0000269|PubMed:1879703"
FT CHAIN 46..552
FT /note="Cholesterol oxidase"
FT /id="PRO_0000012332"
FT ACT_SITE 406
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P12676"
FT ACT_SITE 492
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P12676"
FT BINDING 66..67
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P12676"
FT BINDING 86
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P12676"
FT BINDING 160
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P12676"
FT BINDING 164..167
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P12676"
FT BINDING 295
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P12676"
FT BINDING 491
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P12676"
FT BINDING 520
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P12676"
FT BINDING 532
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P12676"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:1COY"
FT HELIX 66..77
FT /evidence="ECO:0007829|PDB:1COY"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:1COY"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:1COY"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:1COY"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:1COY"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:1COY"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:1COY"
FT HELIX 173..179
FT /evidence="ECO:0007829|PDB:1COY"
FT HELIX 185..190
FT /evidence="ECO:0007829|PDB:1COY"
FT HELIX 192..200
FT /evidence="ECO:0007829|PDB:1COY"
FT HELIX 207..212
FT /evidence="ECO:0007829|PDB:1COY"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:1COY"
FT HELIX 217..228
FT /evidence="ECO:0007829|PDB:1COY"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:1COY"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:1COY"
FT HELIX 242..249
FT /evidence="ECO:0007829|PDB:1COY"
FT TURN 257..260
FT /evidence="ECO:0007829|PDB:1COY"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:1COY"
FT TURN 273..276
FT /evidence="ECO:0007829|PDB:1COY"
FT HELIX 277..283
FT /evidence="ECO:0007829|PDB:1COY"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:1COY"
FT STRAND 292..300
FT /evidence="ECO:0007829|PDB:1COY"
FT STRAND 302..313
FT /evidence="ECO:0007829|PDB:1COY"
FT STRAND 319..332
FT /evidence="ECO:0007829|PDB:1COY"
FT HELIX 335..348
FT /evidence="ECO:0007829|PDB:1COY"
FT TURN 357..360
FT /evidence="ECO:0007829|PDB:1COY"
FT STRAND 368..374
FT /evidence="ECO:0007829|PDB:1COY"
FT STRAND 391..394
FT /evidence="ECO:0007829|PDB:1COY"
FT STRAND 403..408
FT /evidence="ECO:0007829|PDB:1COY"
FT STRAND 418..425
FT /evidence="ECO:0007829|PDB:1COY"
FT STRAND 433..436
FT /evidence="ECO:0007829|PDB:1COY"
FT TURN 437..440
FT /evidence="ECO:0007829|PDB:1COY"
FT STRAND 441..444
FT /evidence="ECO:0007829|PDB:1COY"
FT HELIX 448..451
FT /evidence="ECO:0007829|PDB:1COY"
FT HELIX 452..469
FT /evidence="ECO:0007829|PDB:1COY"
FT STRAND 484..486
FT /evidence="ECO:0007829|PDB:1COY"
FT STRAND 488..491
FT /evidence="ECO:0007829|PDB:1COY"
FT TURN 499..501
FT /evidence="ECO:0007829|PDB:1COY"
FT STRAND 515..517
FT /evidence="ECO:0007829|PDB:1COY"
FT HELIX 520..522
FT /evidence="ECO:0007829|PDB:1COY"
FT HELIX 532..549
FT /evidence="ECO:0007829|PDB:1COY"
SQ SEQUENCE 552 AA; 59358 MW; 74913FAED74B4F09 CRC64;
MTDSRANRAD ATRGVASVSR RRFLAGAGLT AGAIALSSMS TSASAAPSRT LADGDRVPAL
VIGSGYGGAV AALRLTQAGI PTQIVEMGRS WDTPGSDGKI FCGMLNPDKR SMWLADKTDQ
PVSNFMGFGI NKSIDRYVGV LDSERFSGIK VYQGRGVGGG SLVNGGMAVT PKRNYFEEIL
PSVDSNEMYN KYFPRANTGL GVNNIDQAWF ESTEWYKFAR TGRKTAQRSG FTTAFVPNVY
DFEYMKKEAA GQVTKSGLGG EVIYGNNAGK KSLDKTYLAQ AAATGKLTIT TLHRVTKVAP
ATGSGYSVTM EQIDEQGNVV ATKVVTADRV FFAAGSVGTS KLLVSMKAQG HLPNLSSQVG
EGWGNNGNIM VGRANHMWDA TGSKQATIPT MGIDNWADPT APIFAEIAPL PAGLETYVSL
YLAITKNPER ARFQFNSGTG KVDLTWAQSQ NQKGIDMAKK VFDKINQKEG TIYRTDLFGV
YFKTWGDDFT YHPLGGVLLN KATDNFGRLP EYPGLYVVDG SLVPGNVGVN PFVTITRLAE
RNMDKIISSD IQ
