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Database: UniProt
Entry: B8MDS4_TALSN
LinkDB: B8MDS4_TALSN
Original site: B8MDS4_TALSN 
ID   B8MDS4_TALSN            Unreviewed;       636 AA.
AC   B8MDS4;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Glucose oxidase, putative {ECO:0000313|EMBL:EED18303.1};
DE            EC=1.1.3.4 {ECO:0000313|EMBL:EED18303.1};
GN   ORFNames=TSTA_120510 {ECO:0000313|EMBL:EED18303.1};
OS   Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS   1006) (Penicillium stipitatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441959 {ECO:0000313|EMBL:EED18303.1, ECO:0000313|Proteomes:UP000001745};
RN   [1] {ECO:0000313|Proteomes:UP000001745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC   {ECO:0000313|Proteomes:UP000001745};
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
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}.
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DR   EMBL; EQ962655; EED18303.1; -; Genomic_DNA.
DR   RefSeq; XP_002482295.1; XM_002482250.1.
DR   AlphaFoldDB; B8MDS4; -.
DR   STRING; 441959.B8MDS4; -.
DR   GeneID; 8100035; -.
DR   VEuPathDB; FungiDB:TSTA_120510; -.
DR   eggNOG; KOG1238; Eukaryota.
DR   HOGENOM; CLU_002865_6_0_1; -.
DR   InParanoid; B8MDS4; -.
DR   OMA; QPWSPLM; -.
DR   OrthoDB; 858083at2759; -.
DR   PhylomeDB; B8MDS4; -.
DR   Proteomes; UP000001745; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0046562; F:glucose oxidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 4.10.450.10; Glucose Oxidase, domain 2; 1.
DR   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR027424; Glucose_Oxidase_domain_2.
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:SF201; GLUCOSE-METHANOL-CHOLINE OXIDOREDUCTASE N-TERMINAL 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; PS00623; GMC_OXRED_1; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003968};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:EED18303.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001745}.
FT   DOMAIN          150..173
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          343..357
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   ACT_SITE        569
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   ACT_SITE        612
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   BINDING         303
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         568..569
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         602
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   636 AA;  69555 MW;  94527F82E0C2129E CRC64;
     MKGNVCFLQV YKLSDIYRCS DKFFSTTIRS FTTLLAIPTL LFSAATVQAY LPAEQIDVQS
     SLLSEPSKVA GKTYDYIIAG GGLTGLTVAA KLTENPKIKV LVIEKGFYES NDGAIIEDPN
     AYGQIFGTTV DQNYLTVPLI NNRTNNIKAG KGLGGSTLIN GDSWTRPDKI QIDSWEKVFG
     MEGWNWDNMF EYMKKAEAAR PPTDAQLAAG HYFDATCHGT NGTVRSGARD NGKPWSPLMK
     ALMNTVSALG VPVQQDFLCG HPRGVSMIMN NVDENQVRAD AARAWLLPNY QRSNLEILTG
     QMVGKVLFKQ TASGPKAVGV NFGTNKVVNF DVFAKHEVLL AAGSAISPLI LEYSGIGLKS
     VLDQANITQL LDLPVGINMQ DQTTTTVSSR ASVAGAGQGQ AVFFANFTET FGDYAPQARE
     LLNTKLDQWA EETVARGGFH NVTALKVQYE NYRNWLLDED VAFAELFMDT EGKINFDLWD
     LIPFTRGSVH ILSSDPYLWQ FANDPKFFLN EFDLLGQAAA SKLAHDLSSQ GAMKEYFAGE
     TLPGYNLAEN ATLSQWSAYV LQNFRPNWHA VSSCSMMSRE LGGVVDATAK VYGTQGLRVI
     DGSIPPTQVS SHVMTIFYGM ALKVADAILD DYAKSA
//
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