PDC1_KLULA
ID PDC1_KLULA Reviewed; 563 AA.
AC Q12629; Q6CN05;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Pyruvate decarboxylase;
DE EC=4.1.1.1;
GN Name=PDC1; OrderedLocusNames=KLLA0E16357g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 76492 / CBS 2359/152 / CLIB 210;
RX PubMed=8821934; DOI=10.1046/j.1365-2958.1996.346875.x;
RA Bianchi M.M., Tizzani L., Destruelle M., Frontall L., Wesolowski-Louvel M.;
RT "The 'petite-negative' yeast Kluyveromyces lactis has a single gene
RT expressing pyruvate decarboxylase activity.";
RL Mol. Microbiol. 19:27-36(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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 -!- 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; X85968; CAA59953.1; -; Genomic_DNA.
DR EMBL; CR382125; CAG99771.1; -; Genomic_DNA.
DR PIR; S70684; S70684.
DR RefSeq; XP_454684.1; XM_454684.1.
DR PDB; 2VJY; X-ray; 2.30 A; A/B/C/D=1-563.
DR PDB; 2VK4; X-ray; 1.95 A; A/B/C/D=1-563.
DR PDB; 6EFG; X-ray; 2.04 A; A/B/D/E=1-563.
DR PDB; 6EFH; X-ray; 2.99 A; A/B=1-563.
DR PDBsum; 2VJY; -.
DR PDBsum; 2VK4; -.
DR PDBsum; 6EFG; -.
DR PDBsum; 6EFH; -.
DR AlphaFoldDB; Q12629; -.
DR SMR; Q12629; -.
DR STRING; 28985.XP_454684.1; -.
DR MoonProt; Q12629; -.
DR EnsemblFungi; CAG99771; CAG99771; KLLA0_E16303g.
DR GeneID; 2894295; -.
DR KEGG; kla:KLLA0_E16303g; -.
DR eggNOG; KOG1184; Eukaryota.
DR HOGENOM; CLU_013748_0_2_1; -.
DR InParanoid; Q12629; -.
DR OMA; EQRYNDI; -.
DR BRENDA; 4.1.1.1; 2825.
DR EvolutionaryTrace; Q12629; -.
DR Proteomes; UP000000598; Chromosome E.
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 GO; GO:0000949; P:aromatic amino acid family catabolic process to alcohol via Ehrlich pathway; IEA:EnsemblFungi.
DR GO; GO:0006067; P:ethanol metabolic process; IEA:EnsemblFungi.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:EnsemblFungi.
DR GO; GO:0006569; P:tryptophan catabolic process; IEA:EnsemblFungi.
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 PANTHER; PTHR43452; PTHR43452; 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; SSF52467; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Decarboxylase; Lyase; Magnesium; Metal-binding;
KW Reference proteome; Thiamine pyrophosphate.
FT CHAIN 1..563
FT /note="Pyruvate decarboxylase"
FT /id="PRO_0000090765"
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 129
FT /note="S -> C (in Ref. 1; CAA59953)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="D -> H (in Ref. 1; CAA59953)"
FT /evidence="ECO:0000305"
FT CONFLICT 318..319
FT /note="SA -> RP (in Ref. 1; CAA59953)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="A -> D (in Ref. 1; CAA59953)"
FT /evidence="ECO:0000305"
FT CONFLICT 559
FT /note="T -> S (in Ref. 1; CAA59953)"
FT /evidence="ECO:0000305"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:2VK4"
FT HELIX 6..16
FT /evidence="ECO:0007829|PDB:2VK4"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:2VK4"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:2VK4"
FT HELIX 31..35
FT /evidence="ECO:0007829|PDB:2VK4"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:2VK4"
FT HELIX 51..65
FT /evidence="ECO:0007829|PDB:2VK4"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:2VK4"
FT HELIX 76..80
FT /evidence="ECO:0007829|PDB:2VK4"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:2VK4"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:2VK4"
FT HELIX 104..108
FT /evidence="ECO:0007829|PDB:2VJY"
FT HELIX 109..114
FT /evidence="ECO:0007829|PDB:2VK4"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:6EFG"
FT HELIX 124..130
FT /evidence="ECO:0007829|PDB:2VK4"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:2VK4"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:2VK4"
FT HELIX 145..159
FT /evidence="ECO:0007829|PDB:2VK4"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:2VK4"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:2VK4"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:2VK4"
FT HELIX 178..182
FT /evidence="ECO:0007829|PDB:2VK4"
FT HELIX 194..210
FT /evidence="ECO:0007829|PDB:2VK4"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:2VK4"
FT TURN 220..226
FT /evidence="ECO:0007829|PDB:2VK4"
FT HELIX 228..238
FT /evidence="ECO:0007829|PDB:2VK4"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:2VK4"
FT TURN 246..250
FT /evidence="ECO:0007829|PDB:2VK4"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:2VK4"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:2VK4"
FT HELIX 270..277
FT /evidence="ECO:0007829|PDB:2VK4"
FT STRAND 280..286
FT /evidence="ECO:0007829|PDB:2VK4"
FT TURN 291..297
FT /evidence="ECO:0007829|PDB:2VJY"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:2VK4"
FT STRAND 311..316
FT /evidence="ECO:0007829|PDB:2VK4"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:2VK4"
FT HELIX 326..340
FT /evidence="ECO:0007829|PDB:2VK4"
FT TURN 341..343
FT /evidence="ECO:0007829|PDB:2VK4"
FT HELIX 367..377
FT /evidence="ECO:0007829|PDB:2VK4"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:2VK4"
FT HELIX 390..394
FT /evidence="ECO:0007829|PDB:2VK4"
FT HELIX 395..397
FT /evidence="ECO:0007829|PDB:2VK4"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:2VK4"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:2VK4"
FT HELIX 417..432
FT /evidence="ECO:0007829|PDB:2VK4"
FT STRAND 438..443
FT /evidence="ECO:0007829|PDB:2VK4"
FT HELIX 444..450
FT /evidence="ECO:0007829|PDB:2VK4"
FT HELIX 453..459
FT /evidence="ECO:0007829|PDB:2VK4"
FT STRAND 465..473
FT /evidence="ECO:0007829|PDB:2VK4"
FT HELIX 475..480
FT /evidence="ECO:0007829|PDB:2VK4"
FT HELIX 486..488
FT /evidence="ECO:0007829|PDB:2VK4"
FT HELIX 495..497
FT /evidence="ECO:0007829|PDB:2VK4"
FT HELIX 498..501
FT /evidence="ECO:0007829|PDB:2VK4"
FT STRAND 505..512
FT /evidence="ECO:0007829|PDB:2VK4"
FT HELIX 515..522
FT /evidence="ECO:0007829|PDB:2VK4"
FT HELIX 525..528
FT /evidence="ECO:0007829|PDB:2VK4"
FT STRAND 532..539
FT /evidence="ECO:0007829|PDB:2VK4"
FT HELIX 547..558
FT /evidence="ECO:0007829|PDB:2VK4"
SQ SEQUENCE 563 AA; 61658 MW; B6A4691DC081626C CRC64;
MSEITLGRYL FERLKQVEVQ TIFGLPGDFN LSLLDNIYEV PGMRWAGNAN ELNAAYAADG
YARLKGMSCI ITTFGVGELS ALNGIAGSYA EHVGVLHVVG VPSVSSQAKQ LLLHHTLGNG
DFTVFHRMSS NISETTAMIT DINTAPAEID RCIRTTYVSQ RPVYLGLPAN LVDLTVPASL
LDTPIDLSLK PNDPEAEEEV IENVLQLIKE AKNPVILADA CCSRHDAKAE TKKLIDLTQF
PAFVTPMGKG SIDEKHPRFG GVYVGTLSSP AVKEAVESAD LVLSVGALLS DFNTGSFSYS
YKTKNIVEFH SDYTKIRSAT FPGVQMKFAL QKLLTKVADA AKGYKPVPVP SEPEHNEAVA
DSTPLKQEWV WTQVGEFLRE GDVVITETGT SAFGINQTHF PNNTYGISQV LWGSIGFTTG
ATLGAAFAAE EIDPKKRVIL FIGDGSLQLT VQEISTMIRW GLKPYLFVLN NDGYTIERLI
HGETAQYNCI QNWQHLELLP TFGAKDYEAV RVSTTGEWNK LTTDEKFQDN TRIRLIEVML
PTMDAPSNLV KQAQLTAATN AKN
