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Database: UniProt
Entry: A0A094EC32_9PEZI
LinkDB: A0A094EC32_9PEZI
Original site: A0A094EC32_9PEZI 
ID   A0A094EC32_9PEZI        Unreviewed;       692 AA.
AC   A0A094EC32;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   22-FEB-2023, entry version 25.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN   ORFNames=V499_05941 {ECO:0000313|EMBL:KFY73993.1};
OS   Pseudogymnoascus sp. VKM F-103.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420912 {ECO:0000313|EMBL:KFY73993.1, ECO:0000313|Proteomes:UP000029295};
RN   [1] {ECO:0000313|EMBL:KFY73993.1, ECO:0000313|Proteomes:UP000029295}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-103 {ECO:0000313|EMBL:KFY73993.1,
RC   ECO:0000313|Proteomes:UP000029295};
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:KFY73993.1}.
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DR   EMBL; JPKB01000987; KFY73993.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094EC32; -.
DR   HOGENOM; CLU_002865_4_1_1; -.
DR   Proteomes; UP000029295; 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   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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..692
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal
FT                   domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001901147"
FT   DOMAIN          393..407
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         339
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   692 AA;  74267 MW;  89C89016D8728F67 CRC64;
     MLSLLPLSVF LSFTSTVLAA YVIPQNVTLK KEAGTNCPSA LHNHPHEGHS KRQADSNTTW
     LENYEYVVVG SGPGGGPVAA NLAIAGFKVL LIDAGDDQGG ALQYQVPALQ LQATEYEPMR
     WDYFVNHYSD EARQQKDSKM VYQTTSGEQY VGLNPPSGST PLGILYPRAG TLGGCSAHNA
     LITIYPHDSD WTNIATITGD NSWSPDKMRK YFMKLERNRY LPSSIIGHGF DGWLGTALTD
     LSLVIEDPKL LSLIIAAGTA MGKGLLGLLV NTVGGLGQVL LRDINAPGQS SKAGLYQVPL
     AMADSKRNGP RNLVLDTANA VNKDGSRKYH LDIKLTTLVT KVRFSHDGPT PKAVGVDFLD
     GQSLYRADPR SGSATVTGSG SVNATREVIL AAGAFNTPQL LKLSGIGPAA ELESFDIPVV
     VDLPGVGTNL QDRYENTIIG DSPTDFFITK KCTFMETMPD PCLTRWTNGI GPIAKGTYGT
     NGIAIAIVQK SSVAEGEPDL LISGAPAKFK GYFPGYSSDS LHDAHHWAWI VLKAHSRNNA
     GAVTLRSTDP RDMPNINFNY FDTGVTANGA ADKDLQAVYE AMKFSRKIFK GLIPLDGGFN
     EVWPGPNVTT EADMKEFIKD EAWGHHASCT CPIGADGDPM AVLDSNFKVR GVEGLRVVDA
     SVFPKIPGFY ISLPIYIVSE KASDVIIQAA AA
//
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