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 27-MAR-2024, entry version 136. 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; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae; OC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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:MONOMER-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; FAD/NAD(P)-binding domain; 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 PANTHER; PTHR47470; CHOLESTEROL OXIDASE; 1. DR PANTHER; PTHR47470:SF1; FAD-DEPENDENT OXIDOREDUCTASE 2 FAD BINDING DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF05199; GMC_oxred_C; 1. DR Pfam; PF00732; GMC_oxred_N; 1. DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 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 //