ID   A0A0G2FRS8_9PEZI        Unreviewed;       552 AA.
AC   A0A0G2FRS8;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Putative choline oxidase {ECO:0000313|EMBL:KKY36684.1};
GN   ORFNames=UCDDA912_g03356 {ECO:0000313|EMBL:KKY36684.1};
OS   Diaporthe ampelina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX   NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY36684.1, ECO:0000313|Proteomes:UP000034680};
RN   [1] {ECO:0000313|EMBL:KKY36684.1, ECO:0000313|Proteomes:UP000034680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA912 {ECO:0000313|EMBL:KKY36684.1};
RA   Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT   "Distinctive expansion of gene families associated with plant cell wall
RT   degradation and secondary metabolism in the genomes of grapevine trunk
RT   pathogens.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY36684.1, ECO:0000313|Proteomes:UP000034680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA912 {ECO:0000313|EMBL:KKY36684.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAY-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:KKY36684.1}.
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DR   EMBL; LCUC01000112; KKY36684.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2FRS8; -.
DR   STRING; 1214573.A0A0G2FRS8; -.
DR   OrthoDB; 3714148at2759; -.
DR   Proteomes; UP000034680; 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; 3.30.410.40; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000034680}.
FT   DOMAIN          264..278
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         93
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         228
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   552 AA;  61731 MW;  4DBEA50C7E2EB162 CRC64;
     MTTTYLAPHE TDRFDYVVVG GGTAGCVIAS RLAEYLPHKR ILMIEAGPSD FMDDRVLDLR
     QWLALLGGEF DYDYPTTEQP MGNSHIRHSR AKVLGGCSSH NTLISFRPFE YDLKIWESLG
     AKGWEFKDFM RIMDRLRNSV QPVHARHRNQ LCKDWVLACS DAMNIPVIPN YNEEITKTGA
     LRQGVGFFNI SYNPDDHRRS SASVAYIHPI LRGEEQRPNL TILTNAWVDR INVHNDTAKG
     VNVVLRDGSR RSISARTETI LSAGAVDTPR LMLLSGLGPK DQLQGLGIPV FKDIPGVGEN
     LQDHPESIIM WELNKPVPQG QTTMDSDAGI FLRREKPDAA AYKQPANPKA LPDGDIADVM
     MHCYQIPFTF NTERLGYEKV ADGYAFCMTP NIPRPRSRGR LYLTSADPSV KPALDFRYFT
     DPEGYDAATL VYGIKAARKI AETEPFRGWI KREVAPGPRV QSDEDISYYA RKVAHTVYHP
     AGTTRMGDVD ADELAVVDAR LRVRGLRRLR IADAGVFPTI PTINPMLTVL GVAERAAELI
     AEEAGWQHSA RL
//