Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P06169 (PDC1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 166. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length563 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Ref.12 Ref.17

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 processBranched-chain amino acid catabolism
Phenylalanine catabolism
Tryptophan catabolism
   Cellular componentCytoplasm
Nucleus
   LigandMagnesium
Metal-binding
Thiamine pyrophosphate
   Molecular functionDecarboxylase
Lyase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Allosteric enzyme
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processL-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_componentcytosol

Inferred from direct assay PubMed 2665820. Source: SGD

nucleus

Inferred from direct assay PubMed 16850348. Source: SGD

   Molecular_functionbranched-chain-2-oxoacid decarboxylase activity

Inferred from mutant phenotype PubMed 9546164. Source: SGD

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

pyruvate decarboxylase activity

Inferred from direct assay PubMed 23423327PubMed 2404950. Source: SGD

thiamine pyrophosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 563562Pyruvate decarboxylase isozyme 1
PRO_0000090770

Regions

Region390 – 47687Thiamine pyrophosphate binding

Sites

Metal binding4441Magnesium
Metal binding4711Magnesium
Metal binding4731Magnesium; via carbonyl oxygen
Binding site281Substrate
Binding site1151Substrate
Binding site1571Substrate; allosteric site
Binding site4771Substrate

Amino acid modifications

Modified residue21N-acetylserine Ref.12 Ref.17
Modified residue2231Phosphoserine Ref.26 Ref.27 Ref.28
Modified residue2661Phosphothreonine Ref.27
Modified residue3361Phosphothreonine Ref.28
Modified residue3531Phosphothreonine Ref.26 Ref.28
Modified residue5221Phosphothreonine Ref.28
Modified residue5261Phosphoserine Ref.27

Experimental info

Mutagenesis2911D → N in PDC1-8; reduces catalytic activity to 10% but retains autoregulatory activity. Ref.10
Sequence conflict551A → R in CAA54522. Ref.1
Sequence conflict1061A → S in CAA28380. Ref.1
Sequence conflict1061A → S in CAA54522. Ref.1
Sequence conflict1061A → S in CAA54518. Ref.1
Sequence conflict1061A → S in CAA54521. Ref.1
Sequence conflict1151Missing in CAA28380. Ref.1
Sequence conflict1431A → C in CAA54522. Ref.1
Sequence conflict1431A → C in CAA54518. Ref.1
Sequence conflict1431A → C in CAA54521. Ref.1
Sequence conflict145 – 1462AP → PQ in CAA28380. Ref.1
Sequence conflict2061A → V in CAA28380. Ref.1
Sequence conflict2081V → A in CAA54522. Ref.1
Sequence conflict2531D → S in CAA28380. Ref.1
Sequence conflict2531D → S in CAA54522. Ref.1
Sequence conflict2531D → S in CAA54518. Ref.1
Sequence conflict2531D → S in CAA54521. Ref.1
Sequence conflict3361T → N in CAA28380. Ref.1
Sequence conflict3361T → N in CAA54522. Ref.1
Sequence conflict3361T → N in CAA54518. Ref.1
Sequence conflict3361T → N in CAA54521. Ref.1
Sequence conflict5381I → V in CAA28380. Ref.1
Sequence conflict5381I → V in CAA54522. Ref.1
Sequence conflict5381I → V in CAA54518. Ref.1
Sequence conflict5381I → V in CAA54521. Ref.1
Sequence conflict545 – 56319APQNL…TNAKQ → CSTKLG in CAA28380. Ref.1

Secondary structure

........................................................................................................... 563
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06169 [UniParc].

Last modified January 23, 2007. Version 7.
Checksum: 799F85C3AC3FCAB6

FASTA56361,495
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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 204508 / S288c.
[5]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[27]"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 AND SER-526, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223; THR-336; THR-353 AND THR-522, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"Sites of ubiquitin attachment in Saccharomyces cerevisiae."
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"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.
[31]"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.
[32]"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.
PIRDCBYP. S64871.
RefSeqNP_013145.1. NM_001181931.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PVDX-ray2.30A/B2-556[»]
1PYDX-ray2.40A/B1-556[»]
1QPBX-ray2.40A/B1-563[»]
2VK1X-ray1.71A/B/C/D1-563[»]
2VK8X-ray1.42A/B/C/D1-563[»]
2W93X-ray1.60A/B/C/D1-563[»]
ProteinModelPortalP06169.
SMRP06169. Positions 2-563.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31319. 121 interactions.
DIPDIP-6773N.
IntActP06169. 79 interactions.
MINTMINT-667063.

2D gel databases

COMPLUYEAST-2DPAGEP06169.
SWISS-2DPAGEP06169.

Proteomic databases

MaxQBP06169.
PaxDbP06169.
PeptideAtlasP06169.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR044C; YLR044C; YLR044C.
GeneID850733.
KEGGsce:YLR044C.

Organism-specific databases

SGDS000004034. PDC1.

Phylogenomic databases

eggNOGCOG3961.
GeneTreeENSGT00550000075465.
KOK01568.
OMALADACCS.
OrthoDBEOG779P6S.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER3O-117.
YEAST:MONOMER3O-117.
BRENDA4.1.1.1. 984.
SABIO-RKP06169.
UniPathwayUPA00206.
UPA00866.

Gene expression databases

GenevestigatorP06169.

Family and domain databases

Gene3D3.40.50.1220. 1 hit.
3.40.50.970. 2 hits.
InterProIPR029035. DHS-like_NAD/FAD-binding_dom.
IPR029061. THDP-binding.
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]
PANTHERPTHR18968:SF4. PTHR18968:SF4. 1 hit.
PfamPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
PIRSFPIRSF036565. Pyruvt_ip_decrb. 1 hit.
SUPFAMSSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.
PROSITEPS00187. TPP_ENZYMES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP06169.
NextBio966831.

Entry information

Entry namePDC1_YEAST
AccessionPrimary (citable) accession number: P06169
Secondary accession number(s): D6VY46 expand/collapse secondary AC list , O00042, Q07991, Q12682, Q12686, Q12687
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 166 of the entry and version 7 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XII

Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways