ID   A0A0D2JQX5_9EURO        Unreviewed;       662 AA.
AC   A0A0D2JQX5;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623};
GN   ORFNames=Z520_11345 {ECO:0000313|EMBL:KIX92869.1};
OS   Fonsecaea multimorphosa CBS 102226.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIX92869.1, ECO:0000313|Proteomes:UP000053411};
RN   [1] {ECO:0000313|EMBL:KIX92869.1, ECO:0000313|Proteomes:UP000053411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 102226 {ECO:0000313|EMBL:KIX92869.1,
RC   ECO:0000313|Proteomes:UP000053411};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Fonsecaea multimorphosa CBS 102226.";
RL   Submitted (JAN-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, ECO:0000256|RuleBase:RU003968}.
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DR   EMBL; KN848099; KIX92869.1; -; Genomic_DNA.
DR   RefSeq; XP_016626992.1; XM_016781834.1.
DR   AlphaFoldDB; A0A0D2JQX5; -.
DR   STRING; 1442371.A0A0D2JQX5; -.
DR   GeneID; 27717091; -.
DR   VEuPathDB; FungiDB:Z520_11345; -.
DR   OrthoDB; 858083at2759; -.
DR   Proteomes; UP000053411; 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:SF115; DEHYDROGENASE XPTC-RELATED; 1.
DR   PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 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; PS00623; GMC_OXRED_1; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053411};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..662
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal
FT                   domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002245105"
FT   DOMAIN          110..133
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   ACT_SITE        588
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   ACT_SITE        631
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   BINDING         262
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   662 AA;  71687 MW;  C73FD3D04E55FB86 CRC64;
     MKLVLFLSLL VTRFTACLPF TPRNTLNNGT AETYDYVVVG CGIAGLVVAA RLSEDPTVSV
     VCIEAGSLDN YEDSIEIPVY IGERPAEYEW DVSTTPQRQL DGKPRVLAMG KGVGGGSLIN
     GMLWNRGDQN DFNIWAVLGN PGWDWANLLP YFKKSEHYTP RYYQGLESQP VTFVEGMHGF
     FGPVNVSYPE YFWPQTNNWF EALEALHIPT CADPNDGLPC SGSYFLPSSL DSVNQTRSDA
     RRAYHDMASG RANYYLITHA RVERVLFDSE GDGNSNSTRT GPGGAAVRAV GVQVLNLLDN
     TTCTVQATRE VVLAAGGIHT PQVLELSGIG NASLLASLGI SVVQDLPGVG SNLQDHPMIH
     LDYPFQNTSV PTPGWLLTNS SFNSAAELEY FSSRTGPWTS KPSTAVAFPS LAEMTNSTHC
     ISLIRDAMEC FGLQPNLSTL PPEYYYSDPL CADQSGGNLT VLEVGYGMQH NLVAASLLLN
     TTPAYEILND NSGGLDLALM HPLSRGTVHI TSPDIRVDPS VNPNWLSHAV DFEILVLAVR
     FNQRILSTWS MDCLEPAFAP DPQGSIERNV TREQIESMLR QGIGTEFHYA GTAAMLPREV
     GGVVDTNLTV YGTQNLRVVD TSVFPVIPGA HLQAVAYAVA ERASDIIKGV AVDVNAGVGG
     PV
//