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Database: UniProt
Entry: A0A094DA05_9PEZI
LinkDB: A0A094DA05_9PEZI
Original site: A0A094DA05_9PEZI 
ID   A0A094DA05_9PEZI        Unreviewed;       713 AA.
AC   A0A094DA05;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   22-FEB-2023, entry version 26.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN   ORFNames=V497_03169 {ECO:0000313|EMBL:KFY61043.1};
OS   Pseudogymnoascus sp. VKM F-4516 (FW-969).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420910 {ECO:0000313|EMBL:KFY61043.1, ECO:0000313|Proteomes:UP000029268};
RN   [1] {ECO:0000313|EMBL:KFY61043.1, ECO:0000313|Proteomes:UP000029268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4516 (FW-969) {ECO:0000313|Proteomes:UP000029268};
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:KFY61043.1}.
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DR   EMBL; JPJZ01000766; KFY61043.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094DA05; -.
DR   STRING; 1420910.A0A094DA05; -.
DR   HOGENOM; CLU_002865_4_1_1; -.
DR   OrthoDB; 3382025at2759; -.
DR   Proteomes; UP000029268; 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:SF100; DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G00630)-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   Pfam; PF13450; NAD_binding_8; 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:UP000029268}.
FT   DOMAIN          421..435
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         210..213
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   713 AA;  76254 MW;  DFC6DEF8BE3EC7C2 CRC64;
     MNWHLARRTT TKSDPALDDE DQLEYRSMWC GARGGFASST DGTLEILPIA TKVSFIGNRT
     YEIRGAVELP TEAKHLCRVA YLLASAVVAV RATSYEYIVV GSGAGGGVLA ARLALAGRSV
     LLIEAGDDQG TNDNYTIPAF NAKSTEDSSM AWDFFVRHYE DDSRQAKDFK LTYTTPDGND
     YTGLYPPTGA AIKGVLYPRT ATLGGCTAHN AMVAIYPHQD DFQYVASLTG DASWTPDKMR
     KYFAKLEKNE YLQSLLSPGH GRSGWLGIDL TPVTLALQDL KLLSMLQGGI TALSGLAGTV
     INLATFLAGD ANADSPHRDS TQAIYQVPLA SRNGARNGVR DFLVSVNNAV NADGSKKYKL
     EIRTHCLATK VNFDTSNPPK ATGVSFLDGQ SLYRADPRSG KAQAGTPGSA TASREVIISG
     GAYNSPQLLK LSGIGPAAEL KKFGIPVVKD LPGVGANLQD HYEVAVQGTT PTDFAVLKGC
     TFAASKSDPC LEKWHQGKLA LTRGTYVSNG FVAAMFIKSS QSPDGNYDEL AFGGPLNFRG
     YYPGYSIDAT AAKNVWTWAL LKAHPRNTAG SVKLASADPR DPPKILFNYF DTGSGDYAAD
     LETITESIRI ARWAIGNQSV PVTEVLPGSS IKTTEEIQDY IKNTAWGHHA SCTCPIGADG
     DPMAVLDSSF RVRGVSGLRV VDASVYPRIP GTFTLLSTYI VGEKAADIIL GGL
//
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