ID   A0A2B7Y2A1_9EURO        Unreviewed;       594 AA.
AC   A0A2B7Y2A1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623};
GN   ORFNames=AJ80_05470 {ECO:0000313|EMBL:PGH15606.1};
OS   Polytolypa hystricis UAMH7299.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Polytolypa.
OX   NCBI_TaxID=1447883 {ECO:0000313|EMBL:PGH15606.1, ECO:0000313|Proteomes:UP000224634};
RN   [1] {ECO:0000313|EMBL:PGH15606.1, ECO:0000313|Proteomes:UP000224634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH7299 {ECO:0000313|EMBL:PGH15606.1,
RC   ECO:0000313|Proteomes:UP000224634};
RA   Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT   "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL   Submitted (OCT-2017) 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, ECO:0000256|RuleBase:RU003968}.
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:PGH15606.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; PDNA01000081; PGH15606.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B7Y2A1; -.
DR   STRING; 1447883.A0A2B7Y2A1; -.
DR   OrthoDB; 858083at2759; -.
DR   Proteomes; UP000224634; 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; 4.10.450.10; Glucose Oxidase, domain 2; 1.
DR   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR027424; Glucose_Oxidase_domain_2.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR11552:SF201; GLUCOSE-METHANOL-CHOLINE OXIDOREDUCTASE N-TERMINAL DOMAIN-CONTAINING PROTEIN; 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|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003968};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000224634}.
FT   DOMAIN          100..123
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   ACT_SITE        531
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   ACT_SITE        574
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   BINDING         106
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         251
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   594 AA;  64799 MW;  AA59BCEA922DF36C CRC64;
     MRAGELILPL LYGATRAAAV DSFDYIIVGA GTAGLVVANR LTEDPSVTVG VIEPGTDQRD
     NPDVSDWRRA SVPLGTAVDW NYTTTKQSGA NDRELEANQG KAWGGTSAIN GMFYIRGDAA
     QFDAWEDLGN PGWNWDSLFP YFKKSEKHTV PSDAQLAGGA TYEPQHHGFE GYVHTGYPLA
     LRNSSFASTM LQTFKGLDVP HNPDFNGGDV YGFTAVPQTL DTKLDIRWDA ARAYLYPIEQ
     RSNLKIIQGT VTRILWESEK ADRSSCGSDC SFARGVQFVT DDGEGHTLDA KKEVIISAGV
     YRTPLVLEGS GIGNPRILEA LGIKTEVDLP GVGENLQDRS NNYLAFAGYM GASASAYMHF
     YKASDLFGSK ITGIEASTRA SLSKWAQAIV DASGSSALQV TAIEKLLRVQ HDLLFKHNVT
     AAEILTGVAP LGVELFGSSF WTLMPFSRGN VHLQSTENIH KPLIDPRFFL IDFDLTTAVA
     LGKLARKFWL SKRVNEFTKT QVVPPVNILP KDATDAQWES FMRANSTDNY HAIGTASMMP
     RELGGVVDPE LRVYGTANVR VVDASVLPIR FSGHPMATIY AVAERAADII KKAW
//