ID   A0A1P8YG91_9NOCA        Unreviewed;       492 AA.
AC   A0A1P8YG91;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Cholesterol oxidase {ECO:0000313|EMBL:AQA22953.1};
DE            EC=5.3.3.1 {ECO:0000313|EMBL:AQA22953.1};
GN   ORFNames=BTZ20_5052 {ECO:0000313|EMBL:AQA22953.1};
OS   Rhodococcus sp. MTM3W5.2.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1805827 {ECO:0000313|EMBL:AQA22953.1, ECO:0000313|Proteomes:UP000187995};
RN   [1] {ECO:0000313|EMBL:AQA22953.1, ECO:0000313|Proteomes:UP000187995}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MTM3W5.2 {ECO:0000313|EMBL:AQA22953.1,
RC   ECO:0000313|Proteomes:UP000187995};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|RuleBase:RU003968}.
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DR   EMBL; CP019572; AQA22953.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1P8YG91; -.
DR   STRING; 1805827.BTZ20_5052; -.
DR   Proteomes; UP000187995; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   GO; GO:0004769; F:steroid delta-isomerase activity; IEA:UniProtKB-EC.
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   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.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|RuleBase:RU003968};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW   Isomerase {ECO:0000313|EMBL:AQA22953.1}.
FT   DOMAIN          96..119
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
SQ   SEQUENCE   492 AA;  52529 MW;  2B7159042C1E7DDE CRC64;
     MPALIIGSGY GGSVTALRLA QAGIDAHIVE MGRDWGTAGS GVFTSTTSPD KRGFWLRDRT
     AQPVSHFMGV SIDKPIEKYV GILDCENMGG VNVYQGRGVG GGSLVNGGMA VTPRRGYFEE
     ILPSVDSNEM YNVFFPRATA GLGVNNIDQA WFESTEWYKF ARTGRKTAER SGFKTTFVPN
     VYDMNYMKQE AAGSVPKSAL AGEVIFGNHA GKKSLPKTYL AQAASTGKVT ITTLHRVTKV
     VPSGAGYSVE MEQINEQGGV VATKTVTADK VFFAAGSVGT SKLLVAMKAQ GHLPNLSGEV
     GQGWGNNGNV MVARANHLWD ATGGKQSSIP TMGIDNWDDA GGPAFAEIAP FPAGADLFIS
     LYLSITKNPE RAQFQYNSST GKVGLSWQTS QNQPAINMAK RIFDKINSKE GTIYRTDMFG
     GYKVWGDNLT YHPLGGAILN KATDNHGRLH GHPGLYVMDG ALVPGNLGVN PFVTITALAE
     RNIAAIVAND MH
//