ID   A0A260X258_9NOCA        Unreviewed;       496 AA.
AC   A0A260X258;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Cholesterol oxidase {ECO:0000313|EMBL:OZF55271.1};
GN   ORFNames=CH292_04710 {ECO:0000313|EMBL:OZF55271.1};
OS   Rhodococcus sp. 14-2470-1a.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=2023150 {ECO:0000313|EMBL:OZF55271.1, ECO:0000313|Proteomes:UP000215821};
RN   [1] {ECO:0000313|Proteomes:UP000215821}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=14-2470-1a {ECO:0000313|Proteomes:UP000215821};
RA   Savory E.A., Fuller S.J., Weisberg A.J., Thomas W.J., Gordon M.I.,
RA   Stevens D.M., Creason A.L., Belcher M.S., Wiseman M., Putnam M.L.,
RA   Grunwald N.J., Chang J.H.;
RT   "Evolutionary transitions between beneficial and phytopathogenic
RT   Rhodococcus challenge disease management.";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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:OZF55271.1}.
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DR   EMBL; NPFZ01000010; OZF55271.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A260X258; -.
DR   Proteomes; UP000215821; 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   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
FT   DOMAIN          85..295
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          425..483
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   496 AA;  52840 MW;  B0F205C3F4B5AB74 CRC64;
     MNRVPLVRED HRVVVVGSGF GGGVASLRLA EAGVPVTVLE RGMRWPTGPN AETFPHAANP
     DKRILWHRSN PQFFGRPVAF DPYAGLLEAV VGDNMTALCA AGVGGGSLVY QGMTLQPAEH
     VFDANFPDGL DWRTLDRVHY PRVARMLGLA TAPDELIDSP NYQAARVFAR NAEREGFPVS
     KIPMPIDWNY ALAELRGEMA PSYTNGDGAL GVNNGGKNSV DVTYIAAAEA TGLVTVEVLH
     EVRDVERAPD GRWTLYVDRT DLSGVVLENK ILTTDTLVMA AGSTNTTKLL LRASASGRIP
     DMPDALGEGW GTNADRIYVW TDIVNGFGPQ QGGPVVYGSL QWDDPNAAFT IIQASFPPLG
     LDGRSTTMVG YGVSEGRGRF VYDSAVDDAV LRWPWEGDSG IQLSKIGPAA HRLAGPSGVL
     TDTNALVPTT WHPLGGANMG SVCDLEGRVL GQRGLYVLDG ALLPGNAAAC NPSMTIAAIA
     ERALDRLVTE DVGTII
//