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UniProtKB - P06169 (PDC1_YEAST)

Entry version 210 (08 May 2019)
Sequence version 7 (23 Jan 2007)
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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:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 derived from threonine (2-oxobutanoate), norvaline (2-oxopentanoate), valine (3-methyl-2-oxobutanoate, also alpha-keto-isovalerate), isoleucine ((3S)-3-methyl-2-oxopentanoate, also alpha-keto-beta-methylvalerate), phenylalanine (phenylpyruvate), and tryptophan (3-(indol-3-yl)pyruvate), whereas transaminated 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.11 Publications

Miscellaneous

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Allosterically activated by substrate.

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=2.8 mM for pyruvate1 Publication
  2. KM=1.0 mM for 2-oxobutanoate1 Publication
  3. KM=1.5 mM for 2-oxopentanoate1 Publication
  1. Vmax=1.5 µmol/min/mg enzyme for pyruvate1 Publication
  2. Vmax=0.5 µmol/min/mg enzyme for 2-oxobutanoate1 Publication
  3. Vmax=0.4 µmol/min/mg enzyme for 2-oxopentanoate1 Publication
  4. Vmax=38 µmol/min/mg enzyme for 3-methyl-2-oxobutanoate1 Publication
  5. Vmax=15 µmol/min/mg enzyme for 4-methyl-2-oxopentanoate1 Publication
  6. Vmax=9 µmol/min/mg enzyme for 3-methyl-2-oxopentanoate1 Publication
  7. Vmax=41 µmol/min/mg enzyme for 4-methylthio-2-oxobutanoate1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: ethanol fermentation

This protein is involved in the pathway ethanol fermentation, which is part of Fermentation.
View all proteins of this organism that are known to be involved in the pathway ethanol fermentation and in Fermentation.

Pathwayi: Ehrlich pathway

This protein is involved in the pathway Ehrlich pathway, which is part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the pathway Ehrlich pathway and in Amino-acid degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei28Substrate1
Binding sitei115Substrate1
Binding sitei157Substrate; allosteric site1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi444Magnesium1
Metal bindingi471Magnesium1
Metal bindingi473Magnesium; via carbonyl oxygen1
Binding sitei477Substrate1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAllosteric enzyme, Decarboxylase, Lyase
Biological processBranched-chain amino acid catabolism, Phenylalanine catabolism, Tryptophan catabolism
LigandMagnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:MONOMER3O-117
YEAST:MONOMER3O-117

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		4.1.1.1 984

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P06169

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi
UPA00206

UPA00866

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Pyruvate decarboxylase isozyme 1 (EC:4.1.1.-2 Publications, EC:4.1.1.431 Publication, EC:4.1.1.722 Publications, EC:4.1.1.741 Publication)
Alternative name(s):
Thiamine pyrophosphate-dependent 2-oxo-acid decarboxylase
Short name:
2ODC
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PDC1
Ordered Locus Names:YLR044C
ORF Names:L2104
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome XII

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		FungiDB:YLR044C

Saccharomyces Genome Database

More...SGDi		S000004034 PDC1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>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)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi291D → N in PDC1-8; reduces catalytic activity to 10% but retains autoregulatory activity. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved2 Publications
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000907702 – 563Pyruvate decarboxylase isozyme 1Add BLAST562

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserine2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki212Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei223PhosphoserineCombined sources1
Cross-linki233Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei266PhosphothreonineCombined sources1
Cross-linki269Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki332Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei336PhosphothreonineCombined sources1
Modified residuei353PhosphothreonineCombined sources1
Cross-linki484Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki505Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki520Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei522PhosphothreonineCombined sources1
Modified residuei526PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P06169

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P06169

PRoteomics IDEntifications database

More...PRIDEi		P06169

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P06169

2D gel databases

2-DE database at Universidad Complutense de Madrid

More...COMPLUYEAST-2DPAGEi		P06169

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...SWISS-2DPAGEi		P06169

PTM databases

CarbonylDB database of protein carbonylation sites

More...CarbonylDBi		P06169

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P06169

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>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.

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer.3 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		31319, 183 interactors

Database of interacting proteins

More...DIPi		DIP-6773N

Protein interaction database and analysis system

More...IntActi		P06169, 134 interactors

Molecular INTeraction database

More...MINTi		P06169

STRING: functional protein association networks

More...STRINGi		4932.YLR044C

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1563
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB 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[»]

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P06169

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P06169

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni390 – 476Thiamine pyrophosphate bindingAdd BLAST87

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the TPP enzyme family.Curated

Phylogenomic databases

Ensembl GeneTree

More...GeneTreei		ENSGT00940000176336

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P06169

KEGG Orthology (KO)

More...KOi		K01568

Identification of Orthologs from Complete Genome Data

More...OMAi		EWIGNCN

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
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

Pfam protein domain database

More...Pfami		View protein in Pfam
PF02775 TPP_enzyme_C, 1 hit
PF00205 TPP_enzyme_M, 1 hit
PF02776 TPP_enzyme_N, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF036565 Pyruvt_ip_decrb, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52467 SSF52467, 1 hit
SSF52518 SSF52518, 2 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00187 TPP_ENZYMES, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i799F85C3AC3FCAB6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti55A → R in CAA54522 (PubMed:3537965).Curated1
Sequence conflicti106A → S in CAA28380 (PubMed:3537965).Curated1
Sequence conflicti106A → S in CAA54522 (PubMed:3537965).Curated1
Sequence conflicti106A → S in CAA54518 (PubMed:3537965).Curated1
Sequence conflicti106A → S in CAA54521 (PubMed:3537965).Curated1
Sequence conflicti115Missing in CAA28380 (PubMed:3537965).Curated1
Sequence conflicti143A → C in CAA54522 (PubMed:3537965).Curated1
Sequence conflicti143A → C in CAA54518 (PubMed:3537965).Curated1
Sequence conflicti143A → C in CAA54521 (PubMed:3537965).Curated1
Sequence conflicti145 – 146AP → PQ in CAA28380 (PubMed:3537965).Curated2
Sequence conflicti206A → V in CAA28380 (PubMed:3537965).Curated1
Sequence conflicti208V → A in CAA54522 (PubMed:3537965).Curated1
Sequence conflicti253D → S in CAA28380 (PubMed:3537965).Curated1
Sequence conflicti253D → S in CAA54522 (PubMed:3537965).Curated1
Sequence conflicti253D → S in CAA54518 (PubMed:3537965).Curated1
Sequence conflicti253D → S in CAA54521 (PubMed:3537965).Curated1
Sequence conflicti336T → N in CAA28380 (PubMed:3537965).Curated1
Sequence conflicti336T → N in CAA54522 (PubMed:3537965).Curated1
Sequence conflicti336T → N in CAA54518 (PubMed:3537965).Curated1
Sequence conflicti336T → N in CAA54521 (PubMed:3537965).Curated1
Sequence conflicti538I → V in CAA28380 (PubMed:3537965).Curated1
Sequence conflicti538I → V in CAA54522 (PubMed:3537965).Curated1
Sequence conflicti538I → V in CAA54518 (PubMed:3537965).Curated1
Sequence conflicti538I → V in CAA54521 (PubMed:3537965).Curated1
Sequence conflicti545 – 563APQNL…TNAKQ → CSTKLG in CAA28380 (PubMed:3537965).CuratedAdd BLAST19

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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

Protein sequence database of the Protein Information Resource

More...PIRi		S64871 DCBYP

NCBI Reference Sequences

More...RefSeqi		NP_013145.1, NM_001181931.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YLR044C_mRNA; YLR044C_mRNA; YLR044C

Database of genes from NCBI RefSeq genomes

More...GeneIDi		850733

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YLR044C

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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
PIRiS64871 DCBYP
RefSeqiNP_013145.1, NM_001181931.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
SMRiP06169
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31319, 183 interactors
DIPiDIP-6773N
IntActiP06169, 134 interactors
MINTiP06169
STRINGi4932.YLR044C

PTM databases

CarbonylDBiP06169
iPTMnetiP06169

2D gel databases

COMPLUYEAST-2DPAGEiP06169
SWISS-2DPAGEiP06169

Proteomic databases

MaxQBiP06169
PaxDbiP06169
PRIDEiP06169
TopDownProteomicsiP06169

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR044C_mRNA; YLR044C_mRNA; YLR044C
GeneIDi850733
KEGGisce:YLR044C

Organism-specific databases

EuPathDBiFungiDB:YLR044C
SGDiS000004034 PDC1

Phylogenomic databases

GeneTreeiENSGT00940000176336
InParanoidiP06169
KOiK01568
OMAiEWIGNCN

Enzyme and pathway databases

UniPathwayi
UPA00206

UPA00866

BioCyciMetaCyc:MONOMER3O-117
YEAST:MONOMER3O-117
BRENDAi4.1.1.1 984
SABIO-RKiP06169

Miscellaneous databases

EvolutionaryTraceiP06169

Protein Ontology

More...PROi		PR:P06169

Family and domain databases

InterProiView protein in InterPro
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
PfamiView protein in Pfam
PF02775 TPP_enzyme_C, 1 hit
PF00205 TPP_enzyme_M, 1 hit
PF02776 TPP_enzyme_N, 1 hit
PIRSFiPIRSF036565 Pyruvt_ip_decrb, 1 hit
SUPFAMiSSF52467 SSF52467, 1 hit
SSF52518 SSF52518, 2 hits
PROSITEiView protein in PROSITE
PS00187 TPP_ENZYMES, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPDC1_YEAST
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P06169
Secondary accession number(s): D6VY46
, O00042, Q07991, Q12682, Q12686, Q12687
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: May 8, 2019
This is version 210 of the entry and version 7 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

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