(data stored in ACNUC8465 zone)

SWISSPROT: PDC1_CANGA

ID   PDC1_CANGA              Reviewed;         564 AA.
AC   Q6FJA3; Q8J134;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   08-MAY-2019, entry version 101.
DE   RecName: Full=Pyruvate decarboxylase;
DE            EC=4.1.1.1;
GN   Name=PDC1; Synonyms=PDC; OrderedLocusNames=CAGL0M07920g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=JCM 3699 / NBRC 0005;
RX   PubMed=15625313; DOI=10.1093/jb/mvh141;
RA   Wang Q., He P., Lu D., Shen A., Jiang N.;
RT   "Purification, characterization, cloning and expression of pyruvate
RT   decarboxylase from Torulopsis glabrata IFO005.";
RL   J. Biochem. 136:447-455(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2-oxocarboxylate + H(+) = an aldehyde + CO2;
CC         Xref=Rhea:RHEA:11628, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:35179; EC=4.1.1.1;
CC   -!- COFACTOR:
CC       Name=a metal cation; Xref=ChEBI:CHEBI:25213;
CC       Note=Binds 1 metal ion per subunit.;
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC       Note=Binds 1 thiamine pyrophosphate per subunit.;
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
DR   EMBL; AF545432; AAN77243.1; -; Genomic_DNA.
DR   EMBL; CR380959; CAG62667.1; -; Genomic_DNA.
DR   RefSeq; XP_449691.1; XM_449691.1.
DR   SMR; Q6FJA3; -.
DR   STRING; 5478.XP_449691.1; -.
DR   PRIDE; Q6FJA3; -.
DR   EnsemblFungi; CAG62667; CAG62667; CAGL0M07920g.
DR   GeneID; 2891742; -.
DR   KEGG; cgr:CAGL0M07920g; -.
DR   CGD; CAL0137069; PDC.
DR   EuPathDB; FungiDB:CAGL0M07920g; -.
DR   eggNOG; KOG1184; Eukaryota.
DR   eggNOG; COG3961; LUCA.
DR   HOGENOM; HOG000061334; -.
DR   InParanoid; Q6FJA3; -.
DR   KO; K01568; -.
DR   OMA; EWIGNCN; -.
DR   BRENDA; 4.1.1.1; 1113.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0005829; C:cytosol; IDA:CGD.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004737; F:pyruvate decarboxylase activity; IDA:CGD.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006090; P:pyruvate metabolic process; IDA:CGD.
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;
DR   PRODOM; Q6FJA3.
DR   SWISS-2DPAGE; Q6FJA3.
KW   Complete proteome; Decarboxylase; Lyase; Magnesium; Metal-binding;
KW   Reference proteome; Thiamine pyrophosphate.
FT   CHAIN         1    564       Pyruvate decarboxylase.
FT                                /FTId=PRO_0000090762.
FT   REGION      390    476       Thiamine pyrophosphate binding.
FT   METAL       444    444       Magnesium. {ECO:0000250}.
FT   METAL       473    473       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   BINDING      28     28       Substrate. {ECO:0000250}.
FT   BINDING     115    115       Substrate. {ECO:0000250}.
FT   BINDING     477    477       Substrate. {ECO:0000250}.
FT   CONFLICT    559    559       I -> T (in Ref. 1; AAN77243).
FT                                {ECO:0000305}.
FT   CONFLICT    564    564       Missing (in Ref. 1; AAN77243).
FT                                {ECO:0000305}.
SQ   SEQUENCE   564 AA;  61906 MW;  A0F08DE36A96D2AA CRC64;
     MSEITLGRYL FERLNQVDVK TIFGLPGDFN LSLLDKIYEV EGMRWAGNAN ELNAAYAADG
     YARIKGMSCI ITTFGVGELS ALNGIAGSYA EHVGVLHVVG VPSISSQAKQ LLLHHTLGNG
     DFTVFHRMSA NISETTAMVT DIATAPAEID RCIRTTYITQ RPVYLGLPAN LVDLKVPAKL
     LETPIDLSLK PNDPEAETEV VDTVLELIKA AKNPVILADA CASRHDVKAE TKKLIDATQF
     PSFVTPMGKG SIDEQHPRFG GVYVGTLSRP EVKEAVESAD LILSVGALLS DFNTGSFSYS
     YKTKNIVEFH SDYIKIRNAT FPGVQMKFAL QKLLNAVPEA IKGYKPVPVP ARVPENKSCD
     PATPLKQEWM WNQVSKFLQE GDVVITETGT SAFGINQTPF PNNAYGISQV LWGSIGFTTG
     ACLGAAFAAE EIDPKKRVIL FIGDGSLQLT VQEISTMIRW GLKPYLFVLN NDGYTIERLI
     HGEKAGYNDI QNWDHLALLP TFGAKDYENH RVATTGEWDK LTQDKEFNKN SKIRMIEVML
     PVMDAPTSLI EQAKLTASIN AKQE
//

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