ID   A0A139IBP7_9PEZI        Unreviewed;       787 AA.
AC   A0A139IBP7;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   22-FEB-2023, entry version 21.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN   ORFNames=AC579_2427 {ECO:0000313|EMBL:KXT12167.1};
OS   Pseudocercospora musae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT12167.1, ECO:0000313|Proteomes:UP000073492};
RN   [1] {ECO:0000313|EMBL:KXT12167.1, ECO:0000313|Proteomes:UP000073492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT12167.1,
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:KXT12167.1}.
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DR   EMBL; LFZO01000162; KXT12167.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139IBP7; -.
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; 3.30.410.40; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR003953; FAD-binding_2.
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; PF00890; FAD_binding_2; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 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   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000073492};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..787
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal
FT                   domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007297304"
FT   DOMAIN          405..419
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   REGION          23..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   787 AA;  85934 MW;  D2C0BF7DD73DB593 CRC64;
     MLLRQVFHFA LLATGWASDA HLHHQHHNER RQHEEQTRDD SKLEESKNEH VKRGGGWGHG
     QYPSWYGCKT CSYPGGWYDY IVVGSGPGGG PVACRLARAG FNVLLIEAGD DSSAYSFATT
     TPVFQLQATE EPEQEWDYYV SHYTDPRQQA RDSKTSYACP DKIYTGLYPY AGCVMLGVLY
     PRAGALGGCS QHHSMIMVYP WEADWEHLQQ ITGNWTWSPD AMRSYFVKLE RNEYIPSSVV
     GHGYRGWLHL SLTALTLVLE DFKIASLIVA AATAMGKNIV EGLLDTVTGL AHILLTDLNA
     PGRSRDEEEN IFQVPISVDP STSKRAGVRD FIVATAQQYP NLHVQLNTFV TKVLIDHRGY
     GGRPRAYGVQ YEVGRAIYQA DPRWTGARGR PGYAFAVRET IISGGSFETP KLLKLSGIGP
     AAELQHFGIP VIVNNPYVGT NLQDRYEYSV VGEAPTPFVL TKDCTFGYSS PDPCKDRYLA
     GNNPASRGVY ATNGLAFAVT LRSSVAETRI PDVYISGAPA YFQGYYKGSW RSNCNAGEHA
     DAEPCSGYAH DTFSDAKHWL YLILKAQSRN NAGTVTLRST NALERPQINF NSLAIGGDKD
     VQAVMDAVAF ARRAYHAALP LTLESVTEID PGEQKYPDHS PQLAQNIRDR TWGHHASCTC
     PIGLVLDGDF RVMGVDGLRV VDASAFNKIP GFFLCLPTYI LSEKAADAIL GQSPDPYFSV
     PDAGGLLGTL GNGLVAGVVT SFGGSGKQFG TDANTVGLLG DAGSILGLGL IKNTNPLPPK
     IKRTDEL
//