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Database: UniProt
Entry: G3AEG2_SPAPN
LinkDB: G3AEG2_SPAPN
Original site: G3AEG2_SPAPN 
ID   G3AEG2_SPAPN            Unreviewed;       566 AA.
AC   G3AEG2;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   28-MAR-2018, entry version 27.
DE   SubName: Full=Pyruvate decarboxylase {ECO:0000313|EMBL:EGW35750.1};
DE            EC=4.1.1.1 {ECO:0000313|EMBL:EGW35750.1};
GN   Name=PDC2 {ECO:0000313|EMBL:EGW35750.1};
GN   ORFNames=SPAPADRAFT_58954 {ECO:0000313|EMBL:EGW35750.1};
OS   Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX   NCBI_TaxID=619300 {ECO:0000313|Proteomes:UP000000709};
RN   [1] {ECO:0000313|EMBL:EGW35750.1, ECO:0000313|Proteomes:UP000000709}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-27907 / 11-Y1 {ECO:0000313|Proteomes:UP000000709};
RX   PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA   Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A.,
RA   LaButti K.M., Sun H., Clum A., Pangilinan J.L., Lindquist E.A.,
RA   Lucas S., Lapidus A., Jin M., Gunawan C., Balan V., Dale B.E.,
RA   Jeffries T.W., Zinkel R., Barry K.W., Grigoriev I.V., Gasch A.P.;
RT   "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT   production.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; GL996499; EGW35750.1; -; Genomic_DNA.
DR   RefSeq; XP_007373162.1; XM_007373100.1.
DR   EnsemblFungi; EGW35750; EGW35750; SPAPADRAFT_58954.
DR   GeneID; 18872694; -.
DR   KEGG; spaa:SPAPADRAFT_58954; -.
DR   InParanoid; G3AEG2; -.
DR   KO; K01568; -.
DR   OMA; THFRSNE; -.
DR   OrthoDB; EOG092C29BL; -.
DR   Proteomes; UP000000709; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004737; F:pyruvate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR000399; TPP-bd_CS.
DR   InterPro; IPR012110; TPP_enzyme.
DR   InterPro; IPR011766; TPP_enzyme-bd_C.
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; SSF52467; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000000709};
KW   Lyase {ECO:0000313|EMBL:EGW35750.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR036565-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR036565-2};
KW   Pyruvate {ECO:0000313|EMBL:EGW35750.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000709};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN        5    177       TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}.
FT   DOMAIN      201    332       TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}.
FT   DOMAIN      402    482       TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
FT   METAL       445    445       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR036565-2}.
FT   METAL       473    473       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR036565-2}.
FT   METAL       475    475       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR036565-2}.
FT   BINDING      28     28       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR036565-1}.
FT   BINDING     115    115       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR036565-1}.
FT   BINDING     157    157       Substrate; allosteric site.
FT                                {ECO:0000256|PIRSR:PIRSR036565-1}.
FT   BINDING     479    479       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR036565-1}.
SQ   SEQUENCE   566 AA;  61830 MW;  7B90464C494BC00B CRC64;
     MSEVTLGRYL FERLHQLEVN TIFGLPGDFN LSLLDKIYEV ENMKWAGNAN ELNAAYAADG
     YSRIKRLACL VTTFGVGELS ALNGVGGAYA EHVGLLHVVG VPSIASQAKQ LLLHHTLGNG
     DFTVFHRMSN NISQTTAFIS DIHSAPSEID RCIRDAYVYQ RPVYVGLPAN LVDLKVPASL
     LDTPIDLTLK PNDPEAQDEV IETVKQLISQ AANPIILVDA CASRHDCKLE VEQLVDATQF
     PVFTTPMGKS GVNEAHPRFG GVYVGTLSHP EVKAAVESAD LVLSVGALLS DFNTGSFSYS
     YKTKNIVEFH SDYTKIRQAT FPGVQMKEAL QSLLKTVKQA VNPSYVALPV PSVKLIASPA
     PPATPLTQEY LWTKVSSWFR DGDIIVTETG TSAFGIVQSR FPSNTVGISQ VLWGSIGFTV
     GACVGAAMAA QELDPNRRVI LFVGDGSLQL TVQEISTLCK WECNNTYLFV LNNDGYTIER
     LIHGETASYN DIQPWNNLQL LPLFNAKEYE TLRISTVGEL NKLFNDKAFA TPDKLRMVEV
     MLPRMDAPAN LVAQAKISEA TNAAQD
//
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