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Database: UniProt
Entry: A0A0F4YUY8_TALEM
LinkDB: A0A0F4YUY8_TALEM
Original site: A0A0F4YUY8_TALEM 
ID   A0A0F4YUY8_TALEM        Unreviewed;       541 AA.
AC   A0A0F4YUY8;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   22-FEB-2023, entry version 25.
DE   SubName: Full=Choline oxidase {ECO:0000313|EMBL:KKA22107.1};
DE            EC=1.1.3.17 {ECO:0000313|EMBL:KKA22107.1};
GN   ORFNames=T310_3847 {ECO:0000313|EMBL:KKA22107.1};
OS   Rasamsonia emersonii CBS 393.64.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX   NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA22107.1, ECO:0000313|Proteomes:UP000053958};
RN   [1] {ECO:0000313|EMBL:KKA22107.1, ECO:0000313|Proteomes:UP000053958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA22107.1,
RC   ECO:0000313|Proteomes:UP000053958};
RA   Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA   Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL   Submitted (APR-2015) 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}.
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:KKA22107.1}.
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DR   EMBL; LASV01000157; KKA22107.1; -; Genomic_DNA.
DR   RefSeq; XP_013328719.1; XM_013473265.1.
DR   AlphaFoldDB; A0A0F4YUY8; -.
DR   STRING; 1408163.A0A0F4YUY8; -.
DR   GeneID; 25316196; -.
DR   OrthoDB; 3714148at2759; -.
DR   Proteomes; UP000053958; Unassembled WGS sequence.
DR   GO; GO:0033713; F:choline:oxygen 1-oxidoreductase 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   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};
KW   Oxidoreductase {ECO:0000313|EMBL:KKA22107.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053958}.
FT   DOMAIN          265..279
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         94
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         229
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   541 AA;  59998 MW;  993D2E17017502BE CRC64;
     MATTTVLPLS DVDSYDYVIV GGGTAGCVIA SRLAEYLPKK RILLIEAGPS DFMDDRVLKL
     KDWLKLLGSD LDYDYPTTEQ PMGNSHIRHS RAKVLGGCSS HNTLISFRPF EYDCRLWEEM
     GCRGWSFDMF MRVLDNLRNT VQPVHSRHRN QLCKDWVQAC SKALNIPIID DFNREIRSKG
     QLTEGVGFLS VAYNPDDGRR SSASVAYIHP ILRGEEKRPN LTILTNAWVS KVNVSGDTVT
     GVTLTLQSGE KRTLRAKAET ILCAGAIDTP RLLLLSGIGP QEQLRSLGIP VVKDLPGVGE
     NLLDHPETII IWELNQPVPS ETTMDSDAGI FLRREPPNAA GSDGRAADLM MHCYQIPFCV
     NTSRLGYDTP KHAFCMTPNI PRPRSRGRLY LTSADPNVKP ALDFRYFTDP EGYDAATIVA
     GLKAARKVAQ QAPFKNWIKR EVAPGPNVVT DEQLSEYGRK VHHTVYHPAG TTKMGDIERD
     PLAVVDPQLK IRGLKKVRIA DAGIFPTMTS INPMLTVLGI GERAAELIAE EAGWRQNQPK
     L
//
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