UniProt Accession

 PDC1_YEAST; P06169; D6VY46; O00042; Q07991; Q12682; Q12686; Q12687 

Genbank Protein ID

 X04675; X77316; X94607; Z73216; Z73217; X77312; X77315; BK006945 

Genbank Nucleotide ID

 CAA28380.1; CAA54522.1; CAA64291.1; CAA97573.1; CAA97575.1; CAA54518.1; CAA54521.1; DAA09362.1 

Protein Name

 Pyruvate decarboxylase isozyme 1 

Protein Synonyms/Alias

  

Gene Name

 PDC1 

Gene Synonyms/Alias

 YLR044C; L2104 

Created Date

 July 27, 2013 

Organism

 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 

NCBI Taxa ID

 559292 

Lysine Modification

Position	Peptide	Type	References
8	MSEITLGKYLFERLK	acetylation	[1]
190	TPIDMSLKPNDAESE	acetylation	[1]
190	TPIDMSLKPNDAESE	ubiquitination	[2]
198	PNDAESEKEVIDTIL	ubiquitination	[2]
209	DTILALVKDAKNPVI	acetylation	[1]
212	LALVKDAKNPVILAD	ubiquitination	[2, 3]
228	CCSRHDVKAETKKLI	acetylation	[1]
233	DVKAETKKLIDLTQF	acetylation	[1]
233	DVKAETKKLIDLTQF	ubiquitination	[2, 3]
249	AFVTPMGKGSIDEQH	ubiquitination	[2, 4]
269	VYVGTLSKPEVKEAV	acetylation	[1]
269	VYVGTLSKPEVKEAV	ubiquitination	[2, 3]
304	FSYSYKTKNIVEFHS	acetylation	[1]
304	FSYSYKTKNIVEFHS	ubiquitination	[2]
315	EFHSDHMKIRNATFP	acetylation	[1]
315	EFHSDHMKIRNATFP	ubiquitination	[2]
327	TFPGVQMKFVLQKLL	acetylation	[1]
332	QMKFVLQKLLTTIAD	acetylation	[1]
332	QMKFVLQKLLTTIAD	ubiquitination	[2, 3]
342	TTIADAAKGYKPVAV	acetylation	[1]
342	TTIADAAKGYKPVAV	ubiquitination	[2]
345	ADAAKGYKPVAVPAR	acetylation	[1, 5]
345	ADAAKGYKPVAVPAR	ubiquitination	[2]
463	TMIRWGLKPYLFVLN	ubiquitination	[2]
484	EKLIHGPKAQYNEIQ	ubiquitination	[2, 3]
505	LLPTFGAKDYETHRV	ubiquitination	[2, 3]
520	ATTGEWDKLTQDKSF	acetylation	[1]
520	ATTGEWDKLTQDKSF	ubiquitination	[2, 3]
525	WDKLTQDKSFNDNSK	acetylation	[1]
525	WDKLTQDKSFNDNSK	ubiquitination	[2]
532	KSFNDNSKIRMIEIM	acetylation	[1]
532	KSFNDNSKIRMIEIM	ubiquitination	[2]
554	QNLVEQAKLTAATNA	ubiquitination	[3]
562	LTAATNAKQ******	ubiquitination	[2]

Reference

 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [3] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047]
 [4] Identification, analysis, and prediction of protein ubiquitination sites.
 Radivojac P, Vacic V, Haynes C, Cocklin RR, Mohan A, Heyen JW, Goebl MG, Iakoucheva LM.
 Proteins. 2010 Feb 1;78(2):365-80. [PMID: 19722269]
 [5] Preparative peptide isoelectric focusing as a tool for improving the identification of lysine-acetylated peptides from complex mixtures.
 Xie H, Bandhakavi S, Roe MR, Griffin TJ.
 J Proteome Res. 2007 May;6(5):2019-26. [PMID: 17397211] 

Functional Description

 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. 

Sequence Annotation

 REGION 390 476 Thiamine pyrophosphate binding.
 METAL 444 444 Magnesium.
 METAL 471 471 Magnesium.
 METAL 473 473 Magnesium; via carbonyl oxygen.
 BINDING 28 28 Substrate.
 BINDING 115 115 Substrate.
 BINDING 157 157 Substrate; allosteric site.
 BINDING 477 477 Substrate.
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 223 223 Phosphoserine.
 MOD_RES 266 266 Phosphothreonine.
 MOD_RES 336 336 Phosphothreonine.
 MOD_RES 353 353 Phosphothreonine.
 MOD_RES 522 522 Phosphothreonine.
 MOD_RES 526 526 Phosphoserine.  

Keyword

 3D-structure; Acetylation; Allosteric enzyme; Branched-chain amino acid catabolism; Complete proteome; Cytoplasm; Decarboxylase; Direct protein sequencing; Lyase; Magnesium; Metal-binding; Nucleus; Phenylalanine catabolism; Phosphoprotein; Reference proteome; Thiamine pyrophosphate; Tryptophan catabolism. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 563 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; IDA:SGD.
 GO:0005634; C:nucleus; IDA:SGD.
 GO:0000287; F:magnesium ion binding; IEA:InterPro.
 GO:0004737; F:pyruvate decarboxylase activity; IDA:SGD.
 GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
 GO:0000949; P:aromatic amino acid family catabolic process to alcohol via Ehrlich pathway; IGI:SGD.
 GO:0009083; P:branched-chain amino acid catabolic process; IEA:UniProtKB-KW.
 GO:0019655; P:glucose catabolic process to ethanol; IDA:SGD.
 GO:0006559; P:L-phenylalanine catabolic process; IGI:SGD.
 GO:0006090; P:pyruvate metabolic process; IDA:SGD.
 GO:0006569; P:tryptophan catabolic process; IGI:SGD. 

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. 

Pfam

 PF02775; TPP_enzyme_C
 PF00205; TPP_enzyme_M
 PF02776; TPP_enzyme_N 

SMART

  

PROSITE

 PS00187; TPP_ENZYMES 

PRINTS