ID   A0A199AY29_9ACTN        Unreviewed;       478 AA.
AC   A0A199AY29;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Cholesterol oxidase {ECO:0000313|EMBL:OAV77922.1};
GN   ORFNames=AYO52_14505 {ECO:0000313|EMBL:OAV77922.1};
OS   Dietzia sp. 111N12-1.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Dietziaceae;
OC   Dietzia.
OX   NCBI_TaxID=1785156 {ECO:0000313|EMBL:OAV77922.1, ECO:0000313|Proteomes:UP000092558};
RN   [1] {ECO:0000313|EMBL:OAV77922.1, ECO:0000313|Proteomes:UP000092558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=111N12-1 {ECO:0000313|EMBL:OAV77922.1,
RC   ECO:0000313|Proteomes:UP000092558};
RA   Yu M.;
RT   "Draft genome sequence of Dietzia sp.111N12-1 isolated from South China Sea
RT   with petroleum hydrocarbons degradation activity.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|RuleBase:RU003968}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAV77922.1}.
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DR   EMBL; LSSV01000033; OAV77922.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A199AY29; -.
DR   STRING; 1785156.AYO52_14505; -.
DR   Proteomes; UP000092558; Unassembled WGS sequence.
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   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}.
FT   DOMAIN          82..105
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
SQ   SEQUENCE   478 AA;  51277 MW;  1FC8129FE684DA62 CRC64;
     MRLTQAGIAT HIVEMGRSWD TPGPDGKIFS GMLNPDKRST WLADTTSQPV SNFMGFGIDT
     KVERYVGILD AEKFSGVKVY QGRGVGGSSL VNGGMAVTPK RSHFEHILPN VDSAQMYATY
     FPRANAALGV NHVDQAWFES TPWYQFARVG RKTAHRSGFA TTFVPNVYDF DHMKREAAGT
     APASALGGEV IYGNNAGKKS LDKTYLAQAA ATGRLTISPL HRVTAVTPAT GGGYSVTIEQ
     IDEQGAVIAT KNVTADKVFF AAGSIGTSKL LVSMKAQGLL PNLSNQVGEG WGNNGNIMVG
     RANHMWDATG SKQSTIPTLG IDNWADPTAS IFAEIAPLPA GLETYVSLYL AIANNPERAR
     FQFNSATGKV DLTWSASQNQ PGIAMAKRVF DKINKKEGTV YRTDLFGVYK TWGDDFTYHP
     LGGCLLGKAT DNHGRLHEYP GLYVVDGSLV PGNVGVNPFV TITALAEPNM DAIVANDL
//