ID   A0A094JMB6_9PEZI        Unreviewed;       630 AA.
AC   A0A094JMB6;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   22-FEB-2023, entry version 28.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN   ORFNames=V501_05311 {ECO:0000313|EMBL:KFZ10173.1};
OS   Pseudogymnoascus sp. VKM F-4519 (FW-2642).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420914 {ECO:0000313|EMBL:KFZ10173.1, ECO:0000313|Proteomes:UP000029315};
RN   [1] {ECO:0000313|EMBL:KFZ10173.1, ECO:0000313|Proteomes:UP000029315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4519 (FW-2642) {ECO:0000313|Proteomes:UP000029315};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) 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}.
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:KFZ10173.1}.
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DR   EMBL; JPKD01001698; KFZ10173.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094JMB6; -.
DR   STRING; 1420914.A0A094JMB6; -.
DR   HOGENOM; CLU_002865_5_1_1; -.
DR   Proteomes; UP000029315; 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; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR11552:SF78; GMC_OXRDTASE_N 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000029315}.
FT   DOMAIN          284..298
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         238
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         550..551
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   630 AA;  68541 MW;  DE354C8C241D35D8 CRC64;
     MTISNNVADH ITEVDILIAG GGTAACVLAG RLAKLDPSLS ILLVEGGKNN HNDLTVNCPA
     LFLKHLAPDS KTAIFYKGNK SDALAGREPI VPTGGILGGG SSINFMMYTR AQSVDFDSFK
     TEGWTQQDLL PLLKKLETFH SDDPIIDRNL HGYDGPIHVS SGTHRATRAE REFLEVASTQ
     GWPEIVDLQD LQQNNGFSSW QRYVSPDGKR QDSAHRYIHD LLEHGDYPNL HVLTETLVSR
     VIFDAKRAVG LEVEPNMVHR PLTGLSKHPR TRITARKTVV IAAGALGTPQ ILERSGVGEE
     NHLKSLGIPV VADLPGVGAN YQDHHLTLLP YKTSLAPDET IDALLSGRLD LEAAVKEKNP
     ILGWNSVDIS SKLRPRDDEV AALGPEFQAA WDRDFKDSPS RPLMLMGIVS AFLGDPSSVP
     AGQYSTVGCY TGYPYSRGSI HISGESVYDP PSFETGFLSD KDDLDLKAQV WAYKRQREIC
     RRLSTYRGEL QIGHPKFSTG SAAALVSFED GAQPENRSME DRCKMPNIEY SAEDDKAIAQ
     YVRENLNTTW HSLGTCAMRP LQGGGVVDKD LNVYGVEGLK LCDLSIIPEN VGANTNNTAL
     LVGEKAAAIL AAELGLTDGE GAKGNRTTQL
//