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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//