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
//