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Database: UniProt
Entry: A0A094JLY5_9PEZI
LinkDB: A0A094JLY5_9PEZI
Original site: A0A094JLY5_9PEZI 
ID   A0A094JLY5_9PEZI        Unreviewed;       620 AA.
AC   A0A094JLY5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623, ECO:0000259|PROSITE:PS00624};
GN   ORFNames=V501_05356 {ECO:0000313|EMBL:KFZ10038.1};
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:KFZ10038.1, ECO:0000313|Proteomes:UP000029315};
RN   [1] {ECO:0000313|EMBL:KFZ10038.1, 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|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:KFZ10038.1}.
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DR   EMBL; JPKD01001710; KFZ10038.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094JLY5; -.
DR   STRING; 1420914.A0A094JLY5; -.
DR   HOGENOM; CLU_002865_6_0_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:SF210; GLUCOSE-METHANOL-CHOLINE OXIDOREDUCTASE N-TERMINAL DOMAIN-CONTAINING PROTEIN-RELATED; 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.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029315};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..620
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal
FT                   domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001900391"
FT   DOMAIN          128..151
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          299..313
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   ACT_SITE        556
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   ACT_SITE        599
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   BINDING         130
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         267
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   620 AA;  66045 MW;  E1BA4044BF0DAFE0 CRC64;
     MTRLNRAAFT HLLAVLLQIL PVTAVPPTAV PPPAVPPTAV HACTSGLKSY DFIIVGGGTA
     GLAVATRLSQ RLPSSCVLVI EAGQDGRTEP GIIIPGKKGS TIGTKYDWNL TTVVQPDANG
     RVIGMTRGKV LGGSSALNLM TWDRGSIKDY DAWEELGNPG WNWKSIQAAM LKVENFVPSP
     EYVGDGVGKG GLIQTLMNRI LPTHQLTFIP TLNGLGVKEN LASLGGHLLG VMRQPTNIRL
     KDYTRSYSTS YLDAAGKNLV LLLNTRVSKV NFAGTTASGV TLEDGTVISA AKEVILSAGS
     FQSPGLLELS GIGSRTVLAA AGVTKVISDL PGVGENLQDH TRIQSSYKLL PNFLSFDRLR
     INATYAALQL ALYNSNLVSA YDYTGSGYAY LNWSQVSTST NADLLALARK SADLSNPIDA
     KKLSFLSDPK LTPLMSQLEI IFSDGYTGVK GYPAADAPLF GSEFFSLLAV SVHPFGRGSV
     HVKSTNINTP PTIDPKYLHT PYDLHSMVVA AKFMRTIATT APMSSIWTTE YEPGSAVATD
     ADWEAYARAN TLSIYHPVGT CAMLPRKDGG VVDSKLKVYG VNHLRVVDAS IIPIIPGAHI
     QTAVYGVAEM AADIIVAAWK
//
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