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Database: UniProt
Entry: Q6FL20_CANGA
LinkDB: Q6FL20_CANGA
Original site: Q6FL20_CANGA 
ID   Q6FL20_CANGA            Unreviewed;       638 AA.
AC   Q6FL20;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 100.
DE   SubName: Full=Candida glabrata strain CBS138 chromosome L complete sequence {ECO:0000313|EMBL:CAG62044.1};
GN   Name=THI3 {ECO:0000313|CGD:CAL0135988};
GN   OrderedLocusNames=CAGL0L06842g {ECO:0000313|CGD:CAL0135988,
GN   ECO:0000313|EMBL:CAG62044.1};
OS   Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX   NCBI_TaxID=284593 {ECO:0000313|EMBL:CAG62044.1, ECO:0000313|Proteomes:UP000002428};
RN   [1] {ECO:0000313|EMBL:CAG62044.1, ECO:0000313|Proteomes:UP000002428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC   {ECO:0000313|Proteomes:UP000002428};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR036565-2};
CC       Note=Binds 1 Mg(2+) per subunit. {ECO:0000256|PIRSR:PIRSR036565-2};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; CR380958; CAG62044.1; -; Genomic_DNA.
DR   RefSeq; XP_449074.1; XM_449074.1.
DR   AlphaFoldDB; Q6FL20; -.
DR   STRING; 284593.Q6FL20; -.
DR   EnsemblFungi; CAGL0L06842g-T; CAGL0L06842g-T-p1; CAGL0L06842g.
DR   GeneID; 2890819; -.
DR   KEGG; cgr:CAGL0L06842g; -.
DR   CGD; CAL0135988; THI3.
DR   VEuPathDB; FungiDB:CAGL0L06842g; -.
DR   eggNOG; KOG1184; Eukaryota.
DR   HOGENOM; CLU_013748_0_2_1; -.
DR   InParanoid; Q6FL20; -.
DR   OMA; MNNQGYS; -.
DR   Proteomes; UP000002428; Chromosome L.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:EnsemblFungi.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0090180; P:positive regulation of thiamine biosynthetic process; IEA:EnsemblFungi.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR   GO; GO:0070623; P:regulation of thiamine biosynthetic process; IMP:CGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:CGD.
DR   CDD; cd02005; TPP_PDC_IPDC; 1.
DR   CDD; cd07038; TPP_PYR_PDC_IPDC_like; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR012110; PDC/IPDC-like.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   InterPro; IPR047214; TPP_PDC_IPDC.
DR   InterPro; IPR047213; TPP_PYR_PDC_IPDC-like.
DR   PANTHER; PTHR43452; PYRUVATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43452:SF30; PYRUVATE DECARBOXYLASE ISOZYME 1-RELATED; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   PIRSF; PIRSF036565; Pyruvt_ip_decrb; 1.
DR   SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR036565-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR036565-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002428};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW   ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          15..117
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          212..342
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          416..551
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   REGION          589..610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        593..609
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         471
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   BINDING         498
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   BINDING         500
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ   SEQUENCE   638 AA;  71895 MW;  191A0B315D72082E CRC64;
     MNYTEEYGLP SQISISEYLF HRLNQLKIWT IFGLPGDFNM PLLDKLYSIP TMRWAGNTNE
     LNAAYAADGY SRLKHLGCLI TTFGVGELSA INGVAGSYAE HVGILHIVGM PPTSAQTKQL
     LLHHTLGNGD YSVFYRIAND IACHTAIIND TDLCADEVDN CIRAAWGYQK PVYLGVPVNQ
     VDIPVDSSRL NNPIDLSILK KTKETDAQVI DLLLKQMYSA SKPIIVVDAC VRRHDALKET
     HALCELTNFP VFVTPMGKGT IDESYKNFGG VYSGSLSSPE VREVTDFADF VLFIGAILPE
     FSTSTFHFGF KKKNCCILFP TSVKIKKATF PDMLLKGTLQ SLVDTIEPSK ITYKHQAKVD
     IIAPKMEPSD SNLLRQEWVW NEISHWFKEN DIIITETGSS AFGINQTRFP TNTIGINQAL
     WGSVGFALCS CLGALFAVEE KTVVKHNLEI KLRNYNRNIF TENRTILFVG DGAFQLTVQE
     LSTIIRWKLK PYIFIMNNNG YSVDRFLHHR SDASYYDVQP WNYLYLLELF GCTSFETRKI
     VTVSDFKELL ADESFAKPDK IRMIEIMLPQ SDVPKTLIAR WQAEKELSNK RAGDFSENSS
     ENSSPTIDPH WVKKQYLGPV TPTSSLSTEL HSRSQMYL
//
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