ID   A0A177BUB7_9PLEO        Unreviewed;       644 AA.
AC   A0A177BUB7;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Glucose-methanol-choline oxidoreductase-like protein {ECO:0000313|EMBL:OAF99042.1};
GN   ORFNames=CC84DRAFT_415273 {ECO:0000313|EMBL:OAF99042.1};
OS   Paraphaeosphaeria sporulosa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC   Paraphaeosphaeria.
OX   NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAF99042.1, ECO:0000313|Proteomes:UP000077069};
RN   [1] {ECO:0000313|EMBL:OAF99042.1, ECO:0000313|Proteomes:UP000077069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAF99042.1,
RC   ECO:0000313|Proteomes:UP000077069};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) 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}.
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DR   EMBL; KV441563; OAF99042.1; -; Genomic_DNA.
DR   RefSeq; XP_018029408.1; XM_018186120.1.
DR   AlphaFoldDB; A0A177BUB7; -.
DR   STRING; 1460663.A0A177BUB7; -.
DR   GeneID; 28769606; -.
DR   InParanoid; A0A177BUB7; -.
DR   OrthoDB; 3215324at2759; -.
DR   Proteomes; UP000077069; 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:SF138; DEHYDROGENASE PKFF-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; 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   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077069};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..644
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008057325"
FT   DOMAIN          328..342
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         278
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         567..568
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   644 AA;  70044 MW;  EB12A03FAD211922 CRC64;
     MPSRQQLTLA LTFFLASTQA WPAYPFTKRQ SSDSPAAQSS DSTFKEEYDF VIAGGGTAGL
     TLANRLTESG RFSVLVLEAG FNPEVVEAYA TPGGNQFLKG SAVDWGFVTT PQEHLGGRTL
     QYLRGKALGG SSVTNGLYYA RGSAEVYDRW VELGNPGWGW EDIYPLFRKS TKINPPNLGQ
     LSEFSQEYKT WDESAYGGGP LELGFQGYVT DSTNDFVVAC SEAADIPIVD DLNLGVGQGV
     KLGTTTTNSV LRRSSSYDSF YQQARNRTNL RVLYNAPVTG IAFSSVEGGN TTYGNATRPR
     ALGVSYIEQS AGFVRQARAR KEVIVSMGAF HTPQLLMVSG IGPSAELEKV GVSPVHINEN
     VGQHLDDHSV FSIMARAQTN ASTTSMSSSP DNLQAAQTEF FTNLTGPYTA PSGVTNGFKK
     LSVEELQSIG AQAVIDAGLA NQSHIEFLFE TVWYPWIPTP YYTALPNESY ISVTASSMVQ
     LSRGNITLRS NSMSDAPLIN PNYYADETDG IMGVHSFRYL RDILRHPSLS QYTIGDNAGE
     VSPGPEVADD DDDAILQYIK NNTMPNWHAS GTARMRPEAD GGVVDSRLKV YGVDGLRVID
     CSIIPVLPDA NILASVYMVA EKGAELIKED WEDVGYERRM KRSA
//