Gene/Proteome Database (LMPD)

LMPD ID
LMP007369
Gene ID
850733
Species
Saccharomyces cerevisiae S288c (Yeast (S288c))
Gene Name
indolepyruvate decarboxylase 1
Gene Symbol
PDC1
Synonyms
-
Alternate Names
indolepyruvate decarboxylase 1
Chromosome
XII
EC Number
4.1.1.-

Proteins

indolepyruvate decarboxylase 1
Refseq ID NP_013145
Protein GI 6323073
UniProt ID P06169
mRNA ID NM_001181931
Length 563
RefSeq Status PROVISIONAL
MSEITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKGMSCIITTFGVGELSALNGIAGSYAEHVGVLHVVGVPSISAQAKQLLLHHTLGNGDFTVFHRMSANISETTAMITDIATAPAEIDRCIRTTYVTQRPVYLGLPANLVDLNVPAKLLQTPIDMSLKPNDAESEKEVIDTILALVKDAKNPVILADACCSRHDVKAETKKLIDLTQFPAFVTPMGKGSIDEQHPRYGGVYVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFSYSYKTKNIVEFHSDHMKIRNATFPGVQMKFVLQKLLTTIADAAKGYKPVAVPARTPANAAVPASTPLKQEWMWNQLGNFLQEGDVVIAETGTSAFGINQTTFPNNTYGISQVLWGSIGFTTGATLGAAFAAEEIDPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTIEKLIHGPKAQYNEIQGWDHLSLLPTFGAKDYETHRVATTGEWDKLTQDKSFNDNSKIRMIEIMLPVFDAPQNLVEQAKLTAATNAKQ

Gene Information

Entrez Gene ID
850733
Gene Name
indolepyruvate decarboxylase 1
Gene Symbol
PDC1
Species
Saccharomyces cerevisiae S288c

Gene Ontology (GO Annotations)

GO ID Source Type Description
GO:0005829 IDA:SGD C cytosol
GO:0005634 IDA:SGD C nucleus
GO:0047433 IMP:SGD F branched-chain-2-oxoacid decarboxylase activity
GO:0000287 IEA:InterPro F magnesium ion binding
GO:0004737 IDA:SGD F pyruvate decarboxylase activity
GO:0030976 IEA:InterPro F thiamine pyrophosphate binding
GO:0006559 IGI:SGD P L-phenylalanine catabolic process
GO:0000949 IGI:SGD P aromatic amino acid family catabolic process to alcohol via Ehrlich pathway
GO:0009083 IEA:UniProtKB-KW P branched-chain amino acid catabolic process
GO:0019655 IDA:SGD P glucose catabolic process to ethanol
GO:0006090 IDA:SGD P pyruvate metabolic process
GO:0006569 IGI:SGD P tryptophan catabolic process

Domain Information

InterPro Annotations

Accession Description
IPR029035 DHS-like NAD/FAD-binding domain
IPR000399 TPP-binding enzyme, conserved site
IPR029061 Thiamin diphosphate-binding fold
IPR012110 Thiamine pyrophosphate (TPP)-dependent enzyme
IPR011766 Thiamine pyrophosphate enzyme, C-terminal TPP-binding
IPR012001 Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain
IPR012000 Thiamine pyrophosphate enzyme, central domain

UniProt Annotations

Entry Information

Gene Name
indolepyruvate decarboxylase 1
Protein Entry
PDC1_YEAST
UniProt ID
P06169
Species
Yeast (S288c)

Comments

Comment Type Description
Biotechnology 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). {ECO:0000269|PubMed:9655924}.
Catalytic Activity 3-(indol-3-yl)pyruvate = 2-(indol-3- yl)acetaldehyde + CO(2). {ECO:0000269|PubMed:4687392}.
Catalytic Activity A 2-oxo acid + an aldehyde = A 2-hydroxy ketone + CO(2). {ECO:0000269|PubMed:4687392}.
Catalytic Activity A 2-oxo acid = an aldehyde + CO(2). {ECO:0000269|PubMed:4687392}.
Catalytic Activity An aldehyde + an aldehyde = A 2-hydroxy ketone. {ECO:0000269|PubMed:4687392}.
Catalytic Activity Phenylpyruvate = phenylacetaldehyde + CO(2). {ECO:0000269|PubMed:4687392}.
Catalytic Activity Pyruvate = Acetaldehyde + CO(2). {ECO:0000269|PubMed:4687392}.
Cofactor Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 1 Mg(2+) per subunit.;
Cofactor Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Note=Binds 1 thiamine pyrophosphate per subunit.;
Enzyme Regulation Allosterically activated by substrate.
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. {ECO:0000269|PubMed:10231381, ECO:0000269|PubMed:10234824, ECO:0000269|PubMed:10753893, ECO:0000269|PubMed:11141278, ECO:0000269|PubMed:12499363, ECO:0000269|PubMed:12902239, ECO:0000269|PubMed:4687392, ECO:0000269|PubMed:8866484, ECO:0000269|PubMed:9341119, ECO:0000269|PubMed:9748245}.
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.
Miscellaneous Present with 8966 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}.
Pathway Amino-acid degradation; Ehrlich pathway.
Pathway Fermentation; ethanol fermentation.
Ptm Cleavage of N-terminal methionine and N-terminal acetylation by NAT1/ARD1. {ECO:0000269|PubMed:10545125, ECO:0000269|PubMed:9298649}.
Similarity Belongs to the TPP enzyme family. {ECO:0000305}.
Subcellular Location Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Subunit Homotetramer. {ECO:0000269|PubMed:10651824, ECO:0000269|PubMed:8512926, ECO:0000269|PubMed:8604141}.

Identical and Related Proteins

Unique RefSeq proteins for LMP007369 (as displayed in Record Overview)

Protein GI Database Accession Length Protein Name
6323073 RefSeq NP_013145 563 indolepyruvate decarboxylase 1

Identical Sequences to LMP007369 proteins

Reference Database Accession Length Protein Name
GI:6323073 GenBank AGV92099.1 563 Sequence 14 from patent US 8530226
GI:6323073 GenBank EWG84318.1 563 Pdc1p [Saccharomyces cerevisiae R008]
GI:6323073 GenBank EWH17215.1 563 Pdc1p [Saccharomyces cerevisiae P283]
GI:6323073 GenBank AHZ90130.1 563 pyruvate decarboxylase [synthetic construct]
GI:6323073 GenBank AIB02120.1 563 Sequence 51 from patent US 8669094
GI:6323073 gnl McCuskerlabDuke 563 Pdc1p [Saccharomyces cerevisiae YJM993]

Related Sequences to LMP007369 proteins

Reference Database Accession Length Protein Name
GI:6323073 DBBJ GAA24929.1 563 K7_Pdc1p [Saccharomyces cerevisiae Kyokai no. 7]
GI:6323073 GenBank EGA85775.1 631 Pdc1p [Saccharomyces cerevisiae VL3]
GI:6323073 GenBank EIW09121.1 563 Pdc1p [Saccharomyces cerevisiae CEN.PK113-7D]
GI:6323073 PDB 1QPB 563 Chain A, Pyruvate Decarboyxlase From Yeast (Form B) Complexed With Pyruvamide
GI:6323073 PDB 1QPB 563 Chain B, Pyruvate Decarboyxlase From Yeast (Form B) Complexed With Pyruvamide
GI:6323073 PDB 2W93 563 Chain B, Crystal Structure Of The Saccharomyces Cerevisiae Pyruvate Decarboxylase Variant E477q In Complex With The Surrogate Pyruvamide