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 27-MAR-2024, entry version 120.
DE RecName: Full=Pyruvate decarboxylase;
DE EC=4.1.1.1 {ECO:0000269|PubMed:15625313};
GN Name=PDC1; Synonyms=PDC; OrderedLocusNames=CAGL0M07920g;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
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 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138;
RX PubMed=15229592; DOI=10.1038/nature02579;
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.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., 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 Evidence={ECO:0000269|PubMed:15625313};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + pyruvate = acetaldehyde + CO2; Xref=Rhea:RHEA:45484,
CC ChEBI:CHEBI:15343, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526; Evidence={ECO:0000250|UniProtKB:P06169};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P06169};
CC Note=Binds 1 Mg(2+) per subunit. {ECO:0000250|UniProtKB:P06169};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250|UniProtKB:P06169};
CC Note=Binds 1 thiamine pyrophosphate per subunit.
CC {ECO:0000250|UniProtKB:P06169};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR EMBL; AF545432; AAN77243.1; -; Genomic_DNA.
DR EMBL; CR380959; CAG62667.1; -; Genomic_DNA.
DR RefSeq; XP_449691.1; XM_449691.1.
DR AlphaFoldDB; Q6FJA3; -.
DR SMR; Q6FJA3; -.
DR STRING; 284593.Q6FJA3; -.
DR EnsemblFungi; CAGL0M07920g-T; CAGL0M07920g-T-p1; CAGL0M07920g.
DR GeneID; 2891742; -.
DR KEGG; cgr:CAGL0M07920g; -.
DR CGD; CAL0137069; PDC.
DR VEuPathDB; FungiDB:B1J91_M07920g; -.
DR VEuPathDB; FungiDB:CAGL0M07920g; -.
DR eggNOG; KOG1184; Eukaryota.
DR HOGENOM; CLU_013748_0_2_1; -.
DR InParanoid; Q6FJA3; -.
DR OMA; GPEQRYN; -.
DR BRENDA; 4.1.1.1; 1113.
DR Proteomes; UP000002428; Chromosome M.
DR GO; GO:0009986; C:cell surface; IDA:CGD.
DR GO; GO:0005829; C:cytosol; IDA:CGD.
DR GO; GO:0062040; C:fungal biofilm matrix; 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 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; IPR000399; TPP-bd_CS.
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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 1: Evidence at protein level;
KW Decarboxylase; Lyase; Magnesium; Metal-binding; Reference proteome;
KW Thiamine pyrophosphate.
FT CHAIN 1..564
FT /note="Pyruvate decarboxylase"
FT /id="PRO_0000090762"
FT BINDING 28
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 115
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 390
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 413..415
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 444
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 445..446
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 471..476
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 471
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 473
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 477
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT CONFLICT 559
FT /note="I -> T (in Ref. 1; AAN77243)"
FT /evidence="ECO:0000305"
FT CONFLICT 564
FT /note="Missing (in Ref. 1; AAN77243)"
FT /evidence="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
//
