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P06169

- PDC1_YEAST

UniProt

P06169 - PDC1_YEAST

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Protein

Pyruvate decarboxylase isozyme 1

Gene

PDC1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.10 Publications

Catalytic activityi

A 2-oxo acid = an aldehyde + CO2.1 Publication
3-(indol-3-yl)pyruvate = 2-(indol-3-yl)acetaldehyde + CO2.1 Publication
Phenylpyruvate = phenylacetaldehyde + CO2.1 Publication
Pyruvate = Acetaldehyde + CO2.1 Publication
A 2-oxo acid + an aldehyde = A 2-hydroxy ketone + CO2.1 Publication
An aldehyde + an aldehyde = A 2-hydroxy ketone.1 Publication

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Allosterically activated by substrate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei28 – 281Substrate
Binding sitei115 – 1151Substrate
Binding sitei157 – 1571Substrate; allosteric site
Metal bindingi444 – 4441Magnesium
Metal bindingi471 – 4711Magnesium
Metal bindingi473 – 4731Magnesium; via carbonyl oxygen
Binding sitei477 – 4771Substrate

GO - Molecular functioni

  1. branched-chain-2-oxoacid decarboxylase activity Source: SGD
  2. magnesium ion binding Source: InterPro
  3. pyruvate decarboxylase activity Source: SGD
  4. thiamine pyrophosphate binding Source: InterPro

GO - Biological processi

  1. aromatic amino acid family catabolic process to alcohol via Ehrlich pathway Source: SGD
  2. branched-chain amino acid catabolic process Source: UniProtKB-KW
  3. glucose catabolic process to ethanol Source: SGD
  4. L-phenylalanine catabolic process Source: SGD
  5. pyruvate metabolic process Source: SGD
  6. tryptophan catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Branched-chain amino acid catabolism, Phenylalanine catabolism, Tryptophan catabolism

Keywords - Ligandi

Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER3O-117.
YEAST:MONOMER3O-117.
BRENDAi4.1.1.1. 984.
SABIO-RKP06169.
UniPathwayiUPA00206.
UPA00866.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate decarboxylase isozyme 1 (EC:4.1.1.-, EC:4.1.1.1)
Gene namesi
Name:PDC1
Ordered Locus Names:YLR044C
ORF Names:L2104
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XII

Organism-specific databases

SGDiS000004034. PDC1.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytosol Source: SGD
  2. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Biotechnological usei

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).1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi291 – 2911D → N in PDC1-8; reduces catalytic activity to 10% but retains autoregulatory activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 563562Pyruvate decarboxylase isozyme 1PRO_0000090770Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei223 – 2231Phosphoserine3 Publications
Modified residuei266 – 2661Phosphothreonine1 Publication
Modified residuei336 – 3361Phosphothreonine1 Publication
Modified residuei353 – 3531Phosphothreonine2 Publications
Modified residuei522 – 5221Phosphothreonine1 Publication
Modified residuei526 – 5261Phosphoserine1 Publication

Post-translational modificationi

Cleavage of N-terminal methionine and N-terminal acetylation by NAT1/ARD1.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP06169.
PaxDbiP06169.
PeptideAtlasiP06169.

2D gel databases

COMPLUYEAST-2DPAGEP06169.
SWISS-2DPAGEP06169.

Expressioni

Inductioni

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.

Gene expression databases

GenevestigatoriP06169.

Interactioni

Subunit structurei

Homotetramer.3 Publications

Protein-protein interaction databases

BioGridi31319. 122 interactions.
DIPiDIP-6773N.
IntActiP06169. 79 interactions.
MINTiMINT-667063.

Structurei

Secondary structure

1
563
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53Combined sources
Helixi6 – 1611Combined sources
Beta strandi21 – 244Combined sources
Helixi28 – 303Combined sources
Helixi31 – 355Combined sources
Helixi36 – 394Combined sources
Helixi51 – 6515Combined sources
Beta strandi68 – 736Combined sources
Helixi76 – 9116Combined sources
Beta strandi95 – 1017Combined sources
Helixi104 – 1085Combined sources
Beta strandi109 – 1113Combined sources
Beta strandi114 – 1163Combined sources
Beta strandi118 – 1203Combined sources
Helixi124 – 1307Combined sources
Beta strandi134 – 1385Combined sources
Turni142 – 1443Combined sources
Helixi145 – 15915Combined sources
Beta strandi163 – 1686Combined sources
Helixi171 – 1733Combined sources
Beta strandi174 – 1774Combined sources
Helixi178 – 1825Combined sources
Helixi194 – 21017Combined sources
Beta strandi212 – 2187Combined sources
Helixi220 – 2245Combined sources
Helixi228 – 23811Combined sources
Beta strandi242 – 2443Combined sources
Turni246 – 2505Combined sources
Beta strandi259 – 2624Combined sources
Helixi265 – 2673Combined sources
Helixi270 – 2778Combined sources
Beta strandi280 – 2867Combined sources
Turni291 – 2977Combined sources
Beta strandi306 – 3094Combined sources
Beta strandi311 – 3166Combined sources
Beta strandi319 – 3224Combined sources
Helixi326 – 34015Combined sources
Turni341 – 3433Combined sources
Helixi367 – 3748Combined sources
Turni375 – 3773Combined sources
Beta strandi383 – 3864Combined sources
Helixi390 – 3945Combined sources
Helixi395 – 3973Combined sources
Beta strandi405 – 4073Combined sources
Turni410 – 4123Combined sources
Helixi417 – 43216Combined sources
Beta strandi438 – 4436Combined sources
Helixi444 – 4507Combined sources
Helixi451 – 4533Combined sources
Helixi454 – 4596Combined sources
Beta strandi465 – 4739Combined sources
Helixi475 – 4806Combined sources
Helixi486 – 4883Combined sources
Helixi495 – 4973Combined sources
Helixi498 – 5014Combined sources
Beta strandi505 – 5128Combined sources
Helixi515 – 5228Combined sources
Turni525 – 5284Combined sources
Beta strandi531 – 5399Combined sources
Helixi547 – 56115Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP06169.
SMRiP06169. Positions 2-563.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06169.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni390 – 47687Thiamine pyrophosphate bindingAdd
BLAST

Sequence similaritiesi

Belongs to the TPP enzyme family.Curated

Phylogenomic databases

eggNOGiCOG3961.
GeneTreeiENSGT00550000075465.
InParanoidiP06169.
KOiK01568.
OMAiLADACCS.
OrthoDBiEOG779P6S.

Family and domain databases

Gene3Di3.40.50.1220. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR029035. 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]
PANTHERiPTHR18968:SF4. PTHR18968:SF4. 1 hit.
PfamiPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
PIRSFiPIRSF036565. Pyruvt_ip_decrb. 1 hit.
SUPFAMiSSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.
PROSITEiPS00187. TPP_ENZYMES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P06169-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSEITLGKYL FERLKQVNVN TVFGLPGDFN LSLLDKIYEV EGMRWAGNAN
60 70 80 90 100
ELNAAYAADG YARIKGMSCI ITTFGVGELS ALNGIAGSYA EHVGVLHVVG
110 120 130 140 150
VPSISAQAKQ LLLHHTLGNG DFTVFHRMSA NISETTAMIT DIATAPAEID
160 170 180 190 200
RCIRTTYVTQ RPVYLGLPAN LVDLNVPAKL LQTPIDMSLK PNDAESEKEV
210 220 230 240 250
IDTILALVKD AKNPVILADA CCSRHDVKAE TKKLIDLTQF PAFVTPMGKG
260 270 280 290 300
SIDEQHPRYG GVYVGTLSKP EVKEAVESAD LILSVGALLS DFNTGSFSYS
310 320 330 340 350
YKTKNIVEFH SDHMKIRNAT FPGVQMKFVL QKLLTTIADA AKGYKPVAVP
360 370 380 390 400
ARTPANAAVP ASTPLKQEWM WNQLGNFLQE GDVVIAETGT SAFGINQTTF
410 420 430 440 450
PNNTYGISQV LWGSIGFTTG ATLGAAFAAE EIDPKKRVIL FIGDGSLQLT
460 470 480 490 500
VQEISTMIRW GLKPYLFVLN NDGYTIEKLI HGPKAQYNEI QGWDHLSLLP
510 520 530 540 550
TFGAKDYETH RVATTGEWDK LTQDKSFNDN SKIRMIEIML PVFDAPQNLV
560
EQAKLTAATN AKQ
Length:563
Mass (Da):61,495
Last modified:January 23, 2007 - v7
Checksum:i799F85C3AC3FCAB6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551A → R in CAA54522. (PubMed:3537965)Curated
Sequence conflicti106 – 1061A → S in CAA28380. (PubMed:3537965)Curated
Sequence conflicti106 – 1061A → S in CAA54522. (PubMed:3537965)Curated
Sequence conflicti106 – 1061A → S in CAA54518. (PubMed:3537965)Curated
Sequence conflicti106 – 1061A → S in CAA54521. (PubMed:3537965)Curated
Sequence conflicti115 – 1151Missing in CAA28380. (PubMed:3537965)Curated
Sequence conflicti143 – 1431A → C in CAA54522. (PubMed:3537965)Curated
Sequence conflicti143 – 1431A → C in CAA54518. (PubMed:3537965)Curated
Sequence conflicti143 – 1431A → C in CAA54521. (PubMed:3537965)Curated
Sequence conflicti145 – 1462AP → PQ in CAA28380. (PubMed:3537965)Curated
Sequence conflicti206 – 2061A → V in CAA28380. (PubMed:3537965)Curated
Sequence conflicti208 – 2081V → A in CAA54522. (PubMed:3537965)Curated
Sequence conflicti253 – 2531D → S in CAA28380. (PubMed:3537965)Curated
Sequence conflicti253 – 2531D → S in CAA54522. (PubMed:3537965)Curated
Sequence conflicti253 – 2531D → S in CAA54518. (PubMed:3537965)Curated
Sequence conflicti253 – 2531D → S in CAA54521. (PubMed:3537965)Curated
Sequence conflicti336 – 3361T → N in CAA28380. (PubMed:3537965)Curated
Sequence conflicti336 – 3361T → N in CAA54522. (PubMed:3537965)Curated
Sequence conflicti336 – 3361T → N in CAA54518. (PubMed:3537965)Curated
Sequence conflicti336 – 3361T → N in CAA54521. (PubMed:3537965)Curated
Sequence conflicti538 – 5381I → V in CAA28380. (PubMed:3537965)Curated
Sequence conflicti538 – 5381I → V in CAA54522. (PubMed:3537965)Curated
Sequence conflicti538 – 5381I → V in CAA54518. (PubMed:3537965)Curated
Sequence conflicti538 – 5381I → V in CAA54521. (PubMed:3537965)Curated
Sequence conflicti545 – 56319APQNL…TNAKQ → CSTKLG in CAA28380. (PubMed:3537965)CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS64871. DCBYP.
RefSeqiNP_013145.1. NM_001181931.1.

Genome annotation databases

EnsemblFungiiYLR044C; YLR044C; YLR044C.
GeneIDi850733.
KEGGisce:YLR044C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
PIRi S64871. DCBYP.
RefSeqi NP_013145.1. NM_001181931.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali P06169.
SMRi P06169. Positions 2-563.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31319. 122 interactions.
DIPi DIP-6773N.
IntActi P06169. 79 interactions.
MINTi MINT-667063.

2D gel databases

COMPLUYEAST-2DPAGE P06169.
SWISS-2DPAGE P06169.

Proteomic databases

MaxQBi P06169.
PaxDbi P06169.
PeptideAtlasi P06169.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YLR044C ; YLR044C ; YLR044C .
GeneIDi 850733.
KEGGi sce:YLR044C.

Organism-specific databases

SGDi S000004034. PDC1.

Phylogenomic databases

eggNOGi COG3961.
GeneTreei ENSGT00550000075465.
InParanoidi P06169.
KOi K01568.
OMAi LADACCS.
OrthoDBi EOG779P6S.

Enzyme and pathway databases

UniPathwayi UPA00206 .
UPA00866 .
BioCyci MetaCyc:MONOMER3O-117.
YEAST:MONOMER3O-117.
BRENDAi 4.1.1.1. 984.
SABIO-RK P06169.

Miscellaneous databases

EvolutionaryTracei P06169.
NextBioi 966831.

Gene expression databases

Genevestigatori P06169.

Family and domain databases

Gene3Di 3.40.50.1220. 1 hit.
3.40.50.970. 2 hits.
InterProi IPR029035. 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 ]
PANTHERi PTHR18968:SF4. PTHR18968:SF4. 1 hit.
Pfami PF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF036565. Pyruvt_ip_decrb. 1 hit.
SUPFAMi SSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.
PROSITEi PS00187. TPP_ENZYMES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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 204508 / S288c.
  5. 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. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  25. 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.

Entry informationi

Entry nameiPDC1_YEAST
AccessioniPrimary (citable) accession number: P06169
Secondary accession number(s): D6VY46
, O00042, Q07991, Q12682, Q12686, Q12687
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 169 of the entry and version 7 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 8966 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

External Data

Dasty 3