ID   A0A139I140_9PEZI        Unreviewed;       696 AA.
AC   A0A139I140;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN   ORFNames=AC579_5609 {ECO:0000313|EMBL:KXT08444.1};
OS   Pseudocercospora musae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT08444.1, ECO:0000313|Proteomes:UP000073492};
RN   [1] {ECO:0000313|EMBL:KXT08444.1, ECO:0000313|Proteomes:UP000073492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT08444.1,
RC   ECO:0000313|Proteomes:UP000073492};
RA   Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT   "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT   link between parallel evolutionary changes in Pseudocercospora fijiensis
RT   and Pseudocercospora eumusae and increased virulence on the banana host.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         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:KXT08444.1}.
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DR   EMBL; LFZO01000444; KXT08444.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139I140; -.
DR   Proteomes; UP000073492; Unassembled WGS sequence.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:UniProt.
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   GO; GO:0006996; P:organelle organization; IEA:UniProt.
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   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   PANTHER; PTHR11552:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 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; PS00624; GMC_OXRED_2; 1.
DR   PROSITE; PS50096; IQ; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Reference proteome {ECO:0000313|Proteomes:UP000073492}.
FT   DOMAIN          381..395
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   ACT_SITE        628
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   ACT_SITE        672
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   BINDING         341
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   696 AA;  77105 MW;  857A928C56B83A33 CRC64;
     MIVVRMIRKI VFIVVSPMYI PPIEILAHMN KYSSCSVKTL TELEKHSVEP VPVQGCATAV
     ASHCIKQPRV GKYGAKERAM ADGTSVDLAA LNRRAWIRVW GAYACATSAC RIEKLTASMA
     ENTWDYVICG GGTCGPVVAG RLSEDPSLKV LILEAGSHSK DMDNVHMSGA WTKNHYGPTD
     WNIVSPPQVG LNGKECRLPR GRFLGGSSGS NGTICVRGVK QDYDDWGFPE WSGDEMFRAM
     RKAETFHPKA WFPHEPSAHG TDGPLHIEPA LPPIPIAERM FESFQSKGLP YKPDMFSTGE
     SSRGCGHAMR TTWQGYRTTA ADYVTKDQER ANVTIKCDVT VDKVILEQGA DGLEAKGAEY
     VDAQGNRYKA FASREVILAG GSYNTPTMLL RSGIGPKKDL EALNIPVQLD LPGVGENLQD
     HQLIFMYYEL SEPELTDDAR VNHDPEAYAN GHKEWLEKKT GWLANFPFGA FGFNRLNDRL
     ERDNAEWRAL PRAPGRDPMG LSENQPNCEF FNTICYGGPP EYTDFPKEGQ WAFSMCCFLC
     GQQSRGHVKL KSLDPFEPPY VDPCYLTDKR DLMMMAEGVR FANEVVMEGA GTKNIVKGGW
     PAGANHHLNK TNEDWQPFVQ KYASTSYHPG GTCKLGKEDD PMAVVDQYLH VYGVKNLRVA
     DCSIMPNLNS GHTQMPAFGI AEKAAEYIQA TYKGQL
//