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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//