ID   Q2I2N2_9MICO            Unreviewed;       551 AA.
AC   Q2I2N2;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Cholesterol oxidase {ECO:0000313|EMBL:ABC75776.1};
DE            EC=1.1.3.6 {ECO:0000313|EMBL:ABC75776.1};
GN   Name=choB {ECO:0000313|EMBL:ABC75776.1};
OS   Brevibacterium sp. DGCDC-82.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC   Brevibacterium.
OX   NCBI_TaxID=367828 {ECO:0000313|EMBL:ABC75776.1};
RN   [1] {ECO:0000313|EMBL:ABC75776.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DGCDC-82 {ECO:0000313|EMBL:ABC75776.1};
RX   PubMed=17237971; DOI=10.1007/s10529-006-9295-0;
RA   Wang L., Wang W.;
RT   "Coenzyme precursor-assisted expression of a cholesterol oxidase from
RT   Brevibacterium sp. in Escherichia coli.";
RL   Biotechnol. Lett. 29:761-766(2007).
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|RuleBase:RU003968}.
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DR   EMBL; DQ345780; ABC75776.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2I2N2; -.
DR   SMR; Q2I2N2; -.
DR   BRENDA; 1.1.3.6; 14548.
DR   GO; GO:0016995; F:cholesterol oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
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   3: Inferred from homology;
KW   FAD {ECO:0000256|RuleBase:RU003968};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW   Oxidoreductase {ECO:0000313|EMBL:ABC75776.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..45
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           46..551
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004209864"
FT   DOMAIN          154..177
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
SQ   SEQUENCE   551 AA;  59066 MW;  176757E1895C98CA CRC64;
     MTDSRANRAD ATRGVASVSR RRFLAGAGLT AGAIALSSMS TSASAAPSRT LADGDRVPAL
     VIGSGYGGAV AALRLTQAGI PTQIVEMGRS WDTPGSDGKI FCGMLNPDKR SMRLADKTDQ
     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 MGIDNWADPA APIFAEIAPL PAGLETYVSL
     YLAITKNPER ARFQFNSGTG KVDLTWAQSQ NQKGIDMAKK VFDKINQKEG TIYRTDLFGV
     YKTWGDDFTY HPLGGVLLNK ATDNFGRLPE YPGLYVVDGS LVPGNVGVNP FVTITALAER
     NMDKIISSDI Q
//