P06169 (PDC1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pyruvate decarboxylase isozyme 1
EC=4.1.1.-
EC=4.1.1.1

Gene names

Name:	PDC1
Ordered Locus Names:	YLR044C
ORF Names:	L2104

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	563 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Major of three pyruvate decarboxylases (PDC1, PDC5, PDC6) implicated in the nonoxidative conversion of pyruvate to acetaldehyde and carbon dioxide during alcoholic fermentation. Most of the produced acetaldehyde is subsequently reduced to ethanol, but some is required for cytosolic acetyl-CoA production for biosynthetic pathways. The enzyme is also one of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) able to decarboxylate more complex 2-oxo acids (alpha-ketoacids) than pyruvate, which seem mainly involved in amino acid catabolism. Here the enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids. In a third step, the resulting aldehydes are reduced to alcohols, collectively referred to as fusel oils or alcohols. Its preferred substrates are the transaminated amino acids valine, isoleucine, phenylalanine, and tryptophan, whereas leucine is no substrate. In a side-reaction the carbanionic intermediate (or active aldehyde) generated by decarboxylation or by activation of an aldehyde can react with an aldehyde via condensation (or carboligation) yielding a 2-hydroxy ketone, collectively called acyloins. Ref.9 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19 Ref.20 Ref.21
Catalytic activity	A 2-oxo acid = an aldehyde + CO2. Ref.9 3-(indol-3-yl)pyruvate = 2-(indol-3-yl)acetaldehyde + CO2. Ref.9 Phenylpyruvate = phenylacetaldehyde + CO2. Ref.9 Pyruvate = Acetaldehyde + CO2. Ref.9 A 2-oxo acid + an aldehyde = A 2-hydroxy ketone + CO2. Ref.9 An aldehyde + an aldehyde = A 2-hydroxy ketone. Ref.9
Cofactor	Binds 1 magnesium per subunit. Binds 1 thiamine pyrophosphate per subunit.
Enzyme regulation	Allosterically activated by substrate.
Pathway	Fermentation; ethanol fermentation. Amino-acid degradation; Ehrlich pathway.
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm. Nucleus Ref.24.
Induction	Protein expression is strongly induced by high concentrations of fermentable carbon sources and under anaerobic growth conditions and is repressed by ethanol. Protein expression level is also autoregulated through an unknown mechanism. Ref.16
Post-translational modification	Cleavage of N-terminal methionine and N-terminal acetylation by NAT1/ARD1.
Biotechnological use	Fusel oils and acyloins are important flavor and aroma compounds in yeast-fermented products contributing to the quality of beverages and food, e.g. fusel oils in whiskey, contrary to common believe, seem to alleviate hangover. In general they are desirable at low concentrations, whereas high concentrations may spoil the product. By adjusting growth conditions and substrate their production is sought to be influenced. Due to their broad substrate tolerance pyruvate decarboxylases are important biocatalysts for chemoenzymatic syntheses, both by fermentation and in vitro, e.g. in the production of ephedrine, vitamin E, or phenylethanol (rose flavor). Ref.22
Miscellaneous	Present with 8966 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the TPP enzyme family.

Ontologies

Keywords
Biological process	Branched-chain amino acid catabolism Phenylalanine catabolism Tryptophan catabolism
Cellular component	Cytoplasm Nucleus
Ligand	Magnesium Metal-binding Thiamine pyrophosphate
Molecular function	Decarboxylase Lyase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Allosteric enzyme Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	L-phenylalanine catabolic process Inferred from genetic interaction Ref.20. Source: SGD aromatic amino acid family catabolic process to alcohol via Ehrlich pathway Inferred from genetic interaction Ref.20. Source: SGD branched-chain amino acid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW glucose catabolic process to ethanol Inferred from direct assay PubMed 2404950. Source: SGD pyruvate metabolic process Inferred from direct assay PubMed 2404950. Source: SGD tryptophan catabolic process Inferred from genetic interaction Ref.20. Source: SGD
Cellular_component	cytosol Inferred from direct assay PubMed 2665820. Source: SGD nucleus Inferred from direct assay Ref.24PubMed 16850348. Source: SGD
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: InterPro pyruvate decarboxylase activity Inferred from direct assay PubMed 2404950. Source: SGD thiamine pyrophosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 563

562

Pyruvate decarboxylase isozyme 1

PRO_0000090770

Regions

Region

390 – 476

87

Thiamine pyrophosphate binding

Sites

Metal binding

444

1

Magnesium

Metal binding

471

1

Magnesium

Metal binding

473

1

Magnesium; via carbonyl oxygen

Binding site

28

1

Substrate

Binding site

115

1

Substrate

Binding site

157

1

Substrate; allosteric site

Binding site

477

1

Substrate

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.12 Ref.17

Modified residue

223

1

Phosphoserine Ref.26 Ref.28

Modified residue

266

1

Phosphothreonine Ref.28

Modified residue

320

1

Phosphothreonine Ref.28

Modified residue

353

1

Phosphothreonine Ref.26

Modified residue

362

1

Phosphoserine Ref.28

Modified residue

363

1

Phosphothreonine Ref.28

Modified residue

509

1

Phosphothreonine Ref.27

Modified residue

514

1

Phosphothreonine Ref.27

Modified residue

526

1

Phosphoserine Ref.28

Experimental info

Mutagenesis

291

1

D → N in PDC1-8; reduces catalytic activity to 10% but retains autoregulatory activity. Ref.10

Sequence conflict

55

1

A → R in CAA54522. Ref.1

Sequence conflict

106

1

A → S in CAA28380. Ref.1

Sequence conflict

106

1

A → S in CAA54522. Ref.1

Sequence conflict

106

1

A → S in CAA54518. Ref.1

Sequence conflict

106

1

A → S in CAA54521. Ref.1

Sequence conflict

115

1

Missing in CAA28380. Ref.1

Sequence conflict

143

1

A → C in CAA54522. Ref.1

Sequence conflict

143

1

A → C in CAA54518. Ref.1

Sequence conflict

143

1

A → C in CAA54521. Ref.1

Sequence conflict

145 – 146

2

AP → PQ in CAA28380. Ref.1

Sequence conflict

206

1

A → V in CAA28380. Ref.1

Sequence conflict

208

1

V → A in CAA54522. Ref.1

Sequence conflict

253

1

D → S in CAA28380. Ref.1

Sequence conflict

253

1

D → S in CAA54522. Ref.1

Sequence conflict

253

1

D → S in CAA54518. Ref.1

Sequence conflict

253

1

D → S in CAA54521. Ref.1

Sequence conflict

336

1

T → N in CAA28380. Ref.1

Sequence conflict

336

1

T → N in CAA54522. Ref.1

Sequence conflict

336

1

T → N in CAA54518. Ref.1

Sequence conflict

336

1

T → N in CAA54521. Ref.1

Sequence conflict

538

1

I → V in CAA28380. Ref.1

Sequence conflict

538

1

I → V in CAA54522. Ref.1

Sequence conflict

538

1

I → V in CAA54518. Ref.1

Sequence conflict

538

1

I → V in CAA54521. Ref.1

Sequence conflict

545 – 563

19

APQNL…TNAKQ → CSTKLG in CAA28380. Ref.1

Secondary structure

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563

Helix Strand Turn

Details...

Beta strand

3 – 5

3

Helix

6 – 16

11

Beta strand

21 – 24

4

Helix

28 – 30

3

Helix

31 – 35

5

Helix

36 – 39

4

Helix

51 – 65

15

Beta strand

68 – 73

6

Helix

76 – 91

16

Beta strand

95 – 101

7

Helix

104 – 108

5

Beta strand

109 – 111

3

Beta strand

114 – 116

3

Beta strand

118 – 120

3

Helix

124 – 130

7

Beta strand

134 – 138

5

Turn

142 – 144

3

Helix

145 – 159

15

Beta strand

163 – 168

6

Helix

171 – 173

3

Beta strand

174 – 177

4

Helix

178 – 182

5

Helix

194 – 210

17

Beta strand

212 – 218

7

Helix

220 – 224

5

Helix

228 – 238

11

Beta strand

242 – 244

3

Turn

246 – 250

5

Beta strand

259 – 262

4

Helix

265 – 267

3

Helix

270 – 277

8

Beta strand

280 – 286

7

Turn

291 – 297

7

Beta strand

306 – 309

4

Beta strand

311 – 316

6

Beta strand

319 – 322

4

Helix

326 – 340

15

Turn

341 – 343

3

Helix

367 – 374

8

Turn

375 – 377

3

Beta strand

383 – 386

4

Helix

390 – 394

5

Helix

395 – 397

3

Beta strand

405 – 407

3

Turn

410 – 412

3

Helix

417 – 432

16

Beta strand

438 – 443

6

Helix

444 – 450

7

Helix

451 – 453

3

Helix

454 – 459

6

Beta strand

465 – 473

9

Helix

475 – 480

6

Helix

486 – 488

3

Helix

495 – 497

3

Helix

498 – 501

4

Beta strand

505 – 512

8

Helix

515 – 522

8

Turn

525 – 528

4

Beta strand

531 – 539

9

Helix

547 – 561

15

Sequences

	Sequence		Length	Mass (Da)
	P06169 [UniParc]. Last modified January 23, 2007. Version 7. Checksum: 799F85C3AC3FCAB6	FASTA	563	61,495
	10 20 30 40 50 60 MSEITLGKYL FERLKQVNVN TVFGLPGDFN LSLLDKIYEV EGMRWAGNAN ELNAAYAADG 70 80 90 100 110 120 YARIKGMSCI ITTFGVGELS ALNGIAGSYA EHVGVLHVVG VPSISAQAKQ LLLHHTLGNG 130 140 150 160 170 180 DFTVFHRMSA NISETTAMIT DIATAPAEID RCIRTTYVTQ RPVYLGLPAN LVDLNVPAKL 190 200 210 220 230 240 LQTPIDMSLK PNDAESEKEV IDTILALVKD AKNPVILADA CCSRHDVKAE TKKLIDLTQF 250 260 270 280 290 300 PAFVTPMGKG SIDEQHPRYG GVYVGTLSKP EVKEAVESAD LILSVGALLS DFNTGSFSYS 310 320 330 340 350 360 YKTKNIVEFH SDHMKIRNAT FPGVQMKFVL QKLLTTIADA AKGYKPVAVP ARTPANAAVP 370 380 390 400 410 420 ASTPLKQEWM WNQLGNFLQE GDVVIAETGT SAFGINQTTF PNNTYGISQV LWGSIGFTTG 430 440 450 460 470 480 ATLGAAFAAE EIDPKKRVIL FIGDGSLQLT VQEISTMIRW GLKPYLFVLN NDGYTIEKLI 490 500 510 520 530 540 HGPKAQYNEI QGWDHLSLLP TFGAKDYETH RVATTGEWDK LTQDKSFNDN SKIRMIEIML 550 560 PVFDAPQNLV EQAKLTAATN AKQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of the primary structure and promoter function of a pyruvate decarboxylase gene (PDC1) from Saccharomyces cerevisiae." Kellermann E., Seeboth P.G., Hollenberg C.P. Nucleic Acids Res. 14:8963-8977(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Autoregulation may control the expression of yeast pyruvate decarboxylase structural genes PDC1 and PDC5." Hohmann S., Cederberg H. Eur. J. Biochem. 188:615-621(1990) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION.
[3]	Hohmann S. Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[4]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D. Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[5]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[6]	Eberhardt I., Cederberg H., Hohmann S. Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (MUTANTS PDC1-8 AND PDC1-803).
[7]	"Protein identifications for a Saccharomyces cerevisiae protein database." Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., Volpe T., Warner J.R., McLaughlin C.S. Electrophoresis 15:1466-1486(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 37-52. Strain: ATCC 204508 / S288c.
[8]	"Gene linkage of two-dimensional polyacrylamide gel electrophoresis resolved proteins from isogene families in Saccharomyces cerevisiae by microsequencing of in-gel trypsin generated peptides." Norbeck J., Blomberg A. Electrophoresis 16:149-156(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 47-57; 260-269; 344-355; 486-497 AND 507-512. Strain: ATCC 38531 / Y41.
[9]	"The influence of steric and electronic parameters on the substrate behavior of 2-oxo acids to yeast pyruvate decarboxylase." Lehmann H., Fischer G., Hubner G., Kohnert K.D., Schellenberger A. Eur. J. Biochem. 32:83-87(1973) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ENZYME ACTIVITY.
[10]	"Genetic analysis of the pyruvate decarboxylase reaction in yeast glycolysis." Schmitt H.D., Zimmermann F.K. J. Bacteriol. 151:1146-1152(1982) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF ASP-291.
[11]	"ERA, a novel cis-acting element required for autoregulation and ethanol repression of PDC1 transcription in Saccharomyces cerevisiae." Liesen T., Hollenberg C.P., Heinisch J.J. Mol. Microbiol. 21:621-632(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ETHANOL REPRESSION OF EXPRESSION.
[12]	"Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins." Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I., Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R., Payne W.E. Electrophoresis 18:1347-1360(1997) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT SER-2.
[13]	"A 13C nuclear magnetic resonance investigation of the metabolism of leucine to isoamyl alcohol in Saccharomyces cerevisiae." Dickinson J.R., Lanterman M.M., Danner D.J., Pearson B.M., Sanz P., Harrison S.J., Hewlins M.J. J. Biol. Chem. 272:26871-26878(1997) [PubMed] [Europe PMC] [Abstract] Cited for: ROLE IN AMINO ACID CATABOLISM.
[14]	"An investigation of the metabolism of valine to isobutyl alcohol in Saccharomyces cerevisiae." Dickinson J.R., Harrison S.J., Hewlins M.J. J. Biol. Chem. 273:25751-25756(1998) [PubMed] [Europe PMC] [Abstract] Cited for: ROLE IN VALINE CATABOLISM.
[15]	"Growth requirements of pyruvate-decarboxylase-negative Saccharomyces cerevisiae." Flikweert M.T., de Swaaf M., van Dijken J.P., Pronk J.T. FEMS Microbiol. Lett. 174:73-79(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CYTOSOLIC ACETYL-COA PRODUCTION.
[16]	"Autoregulation of yeast pyruvate decarboxylase gene expression requires the enzyme but not its catalytic activity." Eberhardt I., Cederberg H., Li H., Konig S., Jordan F., Hohmann S. Eur. J. Biochem. 262:191-201(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, AUTOREGULATION OF PDC1 AND PDC5 EXPRESSION.
[17]	"Identification and specificities of N-terminal acetyltransferases from Saccharomyces cerevisiae." Polevoda B., Norbeck J., Takakura H., Blomberg A., Sherman F. EMBO J. 18:6155-6168(1999) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT SER-2.
[18]	"An investigation of the metabolism of isoleucine to active Amyl alcohol in Saccharomyces cerevisiae." Dickinson J.R., Harrison S.J., Dickinson J.A., Hewlins M.J. J. Biol. Chem. 275:10937-10942(2000) [PubMed] [Europe PMC] [Abstract] Cited for: ROLE IN ISOLEUCINE CATABOLISM.
[19]	"Generation of odorous acyloins by yeast pyruvate decarboxylases and their occurrence in sherry and soy sauce." Neuser F., Zorn H., Berger R.G. J. Agric. Food Chem. 48:6191-6195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, GENERATION OF ACYLOINS.
[20]	"The catabolism of amino acids to long chain and complex alcohols in Saccharomyces cerevisiae." Dickinson J.R., Salgado L.E., Hewlins M.J. J. Biol. Chem. 278:8028-8034(2003) [PubMed] [Europe PMC] [Abstract] Cited for: ROLE IN PHENYLALANINE; TRYPTOPHAN AND LEUCINE CATABOLISM.
[21]	"Identification and characterization of phenylpyruvate decarboxylase genes in Saccharomyces cerevisiae." Vuralhan Z., Morais M.A., Tai S.L., Piper M.D., Pronk J.T. Appl. Environ. Microbiol. 69:4534-4541(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, AROMATIC AMINO ACIDS AS NITROGEN SOURCE.
[22]	"Application of alpha-keto acid decarboxylases in biotransformations." Iding H., Siegert P., Mesch K., Pohl M. Biochim. Biophys. Acta 1385:307-322(1998) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW, BIOTECHNOLOGICAL RELEVANCE.
[23]	"Thiamin metabolism and thiamin diphosphate-dependent enzymes in the yeast Saccharomyces cerevisiae: genetic regulation." Hohmann S., Meacock P.A. Biochim. Biophys. Acta 1385:201-219(1998) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[24]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[25]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[26]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223 AND THR-353, MASS SPECTROMETRY. Strain: ADR376.
[27]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-509 AND THR-514, MASS SPECTROMETRY.
[28]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223; THR-266; THR-320; SER-362; THR-363 AND SER-526, MASS SPECTROMETRY.
[29]	"Catalytic centers in the thiamin diphosphate dependent enzyme pyruvate decarboxylase at 2.4-A resolution." Dyda F., Furey W.F. Jr., Swaminathan S., Sax M., Farrenkopf B., Jordan F. Biochemistry 32:6165-6170(1993) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-556 IN COMPLEX WITH THIAMINE PYROPHOSPHATE.
[30]	"Crystal structure of the thiamin diphosphate-dependent enzyme pyruvate decarboxylase from the yeast Saccharomyces cerevisiae at 2.3-A resolution." Arjunan P., Umland T., Dyda F., Swaminathan S., Furey W.F. Jr., Sax M., Farrenkopf B., Gao Y., Zhang D., Jordan F. J. Mol. Biol. 256:590-600(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-556 IN COMPLEX WITH THIAMINE PYROPHOSPHATE.
[31]	"The structural basis of substrate activation in yeast pyruvate decarboxylase. A crystallographic and kinetic study." Lu G., Dobritzsch D., Baumann S., Schneider G., Koenig S. Eur. J. Biochem. 267:861-868(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-556 IN COMPLEX WITH THIAMINE PYROPHOSPHATE AND SUBSTRATE ANALOG, SUBSTRATE ACTIVATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X04675 Genomic DNA. Translation: CAA28380.1.
X77316 Genomic DNA. Translation: CAA54522.1.
X94607 Genomic DNA. Translation: CAA64291.1.
Z73216 Genomic DNA. Translation: CAA97573.1.
Z73217 Genomic DNA. Translation: CAA97575.1.
X77312 Genomic DNA. Translation: CAA54518.1.
X77315 Genomic DNA. Translation: CAA54521.1.
BK006945 Genomic DNA. Translation: DAA09362.1.

PIR

DCBYP. S64871.

RefSeq

NP_013145.1. NM_001181931.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PVD	X-ray	2.30	A/B	2-556	[»]
1PYD	X-ray	2.40	A/B	1-556	[»]
1QPB	X-ray	2.40	A/B	1-563	[»]
2VK1	X-ray	1.71	A/B/C/D	1-563	[»]
2VK8	X-ray	1.42	A/B/C/D	1-563	[»]
2W93	X-ray	1.60	A/B/C/D	1-563	[»]

ProteinModelPortal

P06169.

SMR

P06169. Positions 2-563.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6773N.

IntAct

P06169. 74 interactions.

MINT

MINT-667063.

2D gel databases

COMPLUYEAST-2DPAGE

P06169.

SWISS-2DPAGE

P06169.

Proteomic databases

PaxDb

P06169.

PeptideAtlas

P06169.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YLR044C; YLR044C; YLR044C.

GeneID

850733.

KEGG

sce:YLR044C.

Organism-specific databases

SGD

S000004034. PDC1.

Phylogenomic databases

eggNOG

COG3961.

GeneTree

ENSGT00550000075465.

KO

K01568.

OMA

NNTYGIS.

OrthoDB

EOG41NXVF.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-11722.

BRENDA

4.1.1.1. 984.

SABIO-RK

P06169.

UniPathway

UPA00206.
UPA00866.

Gene expression databases

Genevestigator

P06169.

GermOnline

YLR044C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR012000. Thiamin_PyroP_enz_cen_dom.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR000399. TPP-bd_CS.
IPR012110. TPP_enzyme.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]

PANTHER

PTHR18968:SF4. PTHR18968:SF4. 1 hit.

Pfam

PF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]

PIRSF

PIRSF036565. Pyruvt_ip_decrb. 1 hit.

PROSITE

PS00187. TPP_ENZYMES. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P06169.

NextBio

966831.

Entry information

Entry name

PDC1_YEAST

Accession

Primary (citable) accession number: P06169
Secondary accession number(s): D6VY46 , O00042, Q07991, Q12682, Q12686, Q12687

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 156 of the entry and version 7 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program