ID   A0A139IS14_9PEZI        Unreviewed;       760 AA.
AC   A0A139IS14;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   22-FEB-2023, entry version 22.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN   ORFNames=AC579_3838 {ECO:0000313|EMBL:KXT17400.1};
OS   Pseudocercospora musae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT17400.1, ECO:0000313|Proteomes:UP000073492};
RN   [1] {ECO:0000313|EMBL:KXT17400.1, ECO:0000313|Proteomes:UP000073492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT17400.1,
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   -!- 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:KXT17400.1}.
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DR   EMBL; LFZO01000021; KXT17400.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139IS14; -.
DR   STRING; 113226.A0A139IS14; -.
DR   Proteomes; UP000073492; 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:SF213; DEHYDROGENASE, PUTATIVE-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   Pfam; PF13450; NAD_binding_8; 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   Reference proteome {ECO:0000313|Proteomes:UP000073492};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..760
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal
FT                   domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007297664"
FT   DOMAIN          393..407
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   REGION          26..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..48
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   760 AA;  82666 MW;  F178F907433FE9A8 CRC64;
     MLYPILHLLL FATAWAAEHI RGKHHRHHTA RQEYQEGDQK HERQHVERQY GQQPQWFGAG
     RAAYPTGYYD YIVIGSGAGG GVVAPRLARY GYSVLLIEAG DDQGNDFNVK VPALQLQSTE
     LITQRWDYYV KHYQDPIQQA RDSKMSYRCP DRIYTGLHPY QGCVPLGVLY PRAGTLGGCT
     QHHAMIMVHP WESDFDNIAT ITGNSSWNAQ TMRQYFVRLE RNQYLPSSVV GHGYSGWLHI
     TVTALTLVAE DLKLASLVVA AATALGKNLI EGLLTTVTGL AHIFATDFNA PGRTRDAEAE
     LWQVPIAVDP TDSTRSGTRR FVVETAQQYP NLHVQMHTFV TKILLDTRGH KPRAYGVQYE
     VGQSLYSADP RWTGARGQPG YAFAIKEVIL SAGSFETPKL LMLSGIGPSE ELSQHGIQTI
     VSSPGVGRNM QDRYEYGVVG KTPTPFSSTK DCTFNYRQPD PCLQQWMNSA TPALKGVYGS
     NGLALAVTLR SSVAAQSEPD VYISGAPAYF RGYYPNYASE AVADPMHWTW IILKAQSRNN
     AGTVTLRSTN PFDMPEIQFN SLAIGGNEDV QAVMDAVDFG RRAFGSLIPL GGDGFTENDP
     GEAQFPSQSS QLAQNIRDRA WGHHACGTAR IGAPGDPYAV LDSDFRVNGV DGLRVVDASI
     WPKIPGFFLA LPIHIIAEKA ADVITGRAPD PYFATPDAGG LLGTLGFGLV GGLVSGLTGQ
     GKSLGTNANP KGLLGSPANL LGGLGLFDNT QPTGDNPPSQ
//