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Database: UniProt
Entry: A0A1W2FSD9_9PSEU
LinkDB: A0A1W2FSD9_9PSEU
Original site: A0A1W2FSD9_9PSEU 
ID   A0A1W2FSD9_9PSEU        Unreviewed;       489 AA.
AC   A0A1W2FSD9;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:SMD24835.1};
GN   ORFNames=SAMN05660733_07916 {ECO:0000313|EMBL:SMD24835.1};
OS   Lentzea albidocapillata.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Lentzea.
OX   NCBI_TaxID=40571 {ECO:0000313|EMBL:SMD24835.1, ECO:0000313|Proteomes:UP000192840};
RN   [1] {ECO:0000313|Proteomes:UP000192840}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44073 {ECO:0000313|Proteomes:UP000192840};
RA   Varghese N., Submissions S.;
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; FWYC01000023; SMD24835.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W2FSD9; -.
DR   STRING; 40571.SAMN05660733_07916; -.
DR   eggNOG; COG2303; Bacteria.
DR   Proteomes; UP000192840; 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   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR11552:SF152; OXIDASE (CODA), PUTATIVE (AFU_ORTHOLOGUE AFUA_8G04090)-RELATED; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 2.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2}.
FT   DOMAIN          236..250
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         82
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   489 AA;  53748 MW;  23F60D7FCA17EB69 CRC64;
     MTAYDYVIVG GGTAGCVLAA RLTEDENVTV AVIEGGPSDV GDEKILNLRN WINLLETEYD
     YDYPTVEQPR GNSHIRHSRA KVLGGCSSHN TLICFQPLPQ DLDGWGHGWT WDAVGPYYDK
     VQLNIIPVVE KDRNPIAKDF VAAAQQATGV PEIENFNAKP FEDGVGFFSI AYHPEKNNQR
     SSASTAYVHP ILDRRNLTLL LDTWAGRIEF DGTRAIGVHT DKGYIEANKE VLLCAGAIDT
     PRLMMLSGIG DAEHLSSIGI EPRHDLPGVG ENLLDHPESV IVWETTKPLP ENSVMDSDAG
     LFIRRDESDP RPDLMFHFYQ IPFTTNTERL GYPAVEHGVC MTPNIPRPRS LGRLWLKSSD
     PTEKPALDFG YFTDPGGYDE QTLVDGFRIA RGIAEQEPLK SWLKREIAPG PDVTSDEALS
     EYGRKAAHTV YHPAGTCAIG SVVDGDLKVI GLEGLRVVDA SVFPTMPTVN PMVTVLMIGE
     RAADLIKEA
//
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