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Entry version 183 (13 Feb 2019)
Sequence version 4 (23 Jan 2007)
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Protein

Pyruvate decarboxylase isozyme 2

Gene

PDC5

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

Second most abundant 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-keto-acids) 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.10 Publications

Miscellaneous

Present with 471316 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=5.1 mM for pyruvate1 Publication
  2. KM=1.2 mM for 2-oxobutanoate1 Publication
  3. KM=1.5 mM for 2-oxopentanoate1 Publication
  4. KM=0.67 mM for phenylpyruvate1 Publication
  1. Vmax=1.3 µmol/min/mg enzyme for pyruvate1 Publication
  2. Vmax=0.4 µmol/min/mg enzyme for 2-oxobutanoate1 Publication
  3. Vmax=0.4 µmol/min/mg enzyme for 2-oxopentanoate1 Publication
  4. Vmax=68 µmol/min/mg enzyme for phenylpyruvate1 Publication
  5. Vmax=46 µmol/min/mg enzyme for 3-methyl-2-oxobutanoate1 Publication
  6. Vmax=19 µmol/min/mg enzyme for 4-methyl-2-oxopentanoate1 Publication
  7. Vmax=8 µmol/min/mg enzyme for 3-methyl-2-oxopentanoate1 Publication
  8. Vmax=54 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 sitei28SubstrateBy similarity1
Binding sitei115SubstrateBy similarity1
Binding sitei157Substrate; allosteric siteBy similarity1
<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 bindingi444MagnesiumBy similarity1
Metal bindingi471MagnesiumBy similarity1
Metal bindingi473Magnesium; via carbonyl oxygenBy similarity1
Binding sitei477SubstrateBy similarity1

<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

  • branched-chain-2-oxoacid decarboxylase activity Source: SGD
  • carboxy-lyase activity Source: GO_Central
  • indolepyruvate decarboxylase activity Source: UniProtKB-EC
  • magnesium ion binding Source: InterPro
  • phenylpyruvate decarboxylase activity Source: UniProtKB-EC
  • pyruvate decarboxylase activity Source: SGD
  • thiamine pyrophosphate binding Source: InterPro

GO - Biological processi

<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:YLR134W-MONOMER
YEAST:YLR134W-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
4.1.1.1 984

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P16467

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 2 (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:PDC5
Ordered Locus Names:YLR134W
ORF Names:L3133, L9606.7
<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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<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:YLR134W

Saccharomyces Genome Database

More...
SGDi
S000004124 PDC5

<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

<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 ‘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_00000907711 – 563Pyruvate decarboxylase isozyme 2Add BLAST563

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P16467

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

More...
PaxDbi
P16467

PRoteomics IDEntifications database

More...
PRIDEi
P16467

Consortium for Top Down Proteomics

More...
TopDownProteomicsi
P16467

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
P16467

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P16467

<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, under anaerobic growth conditions, and by thiamine limitation, but is repressed by the presence of PDC1 (independent of its catalytic activity) and thiamine.

<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.

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
31403, 52 interactors

Database of interacting proteins

More...
DIPi
DIP-4603N

Protein interaction database and analysis system

More...
IntActi
P16467, 12 interactors

Molecular INTeraction database

More...
MINTi
P16467

STRING: functional protein association networks

More...
STRINGi
4932.YLR134W

<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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P16467

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

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SMRi
P16467

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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 bindingBy similarityAdd 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

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000061334

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P16467

KEGG Orthology (KO)

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KOi
K01568

Identification of Orthologs from Complete Genome Data

More...
OMAi
THFRSNE

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.

P16467-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSEITLGKYL FERLSQVNCN TVFGLPGDFN LSLLDKLYEV KGMRWAGNAN
60 70 80 90 100
ELNAAYAADG YARIKGMSCI ITTFGVGELS ALNGIAGSYA EHVGVLHVVG
110 120 130 140 150
VPSISSQAKQ LLLHHTLGNG DFTVFHRMSA NISETTAMIT DIANAPAEID
160 170 180 190 200
RCIRTTYTTQ RPVYLGLPAN LVDLNVPAKL LETPIDLSLK PNDAEAEAEV
210 220 230 240 250
VRTVVELIKD AKNPVILADA CASRHDVKAE TKKLMDLTQF PVYVTPMGKG
260 270 280 290 300
AIDEQHPRYG GVYVGTLSRP EVKKAVESAD LILSIGALLS DFNTGSFSYS
310 320 330 340 350
YKTKNIVEFH SDHIKIRNAT FPGVQMKFAL QKLLDAIPEV VKDYKPVAVP
360 370 380 390 400
ARVPITKSTP ANTPMKQEWM WNHLGNFLRE GDIVIAETGT SAFGINQTTF
410 420 430 440 450
PTDVYAIVQV LWGSIGFTVG ALLGATMAAE ELDPKKRVIL FIGDGSLQLT
460 470 480 490 500
VQEISTMIRW GLKPYIFVLN NNGYTIEKLI HGPHAEYNEI QGWDHLALLP
510 520 530 540 550
TFGARNYETH RVATTGEWEK LTQDKDFQDN SKIRMIEVML PVFDAPQNLV
560
KQAQLTAATN AKQ
Length:563
Mass (Da):61,912
Last modified:January 23, 2007 - v4
<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:iDCA06A73E18DD819
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 conflicti35D → N in CAA33709 (PubMed:2185016).Curated1
Sequence conflicti143A → R in CAA33709 (PubMed:2185016).Curated1
Sequence conflicti207L → F in CAA33709 (PubMed:2185016).Curated1
Sequence conflicti222A → C in CAA33709 (PubMed:2185016).Curated1
Sequence conflicti341V → A in CAA33709 (PubMed:2185016).Curated1
Sequence conflicti373H → Q in CAA33709 (PubMed:2185016).Curated1

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
X15668 Genomic DNA Translation: CAA33709.1
X91258 Genomic DNA Translation: CAA62647.1
Z73306 Genomic DNA Translation: CAA97705.1
U53881 Genomic DNA Translation: AAB82395.1
BK006945 Genomic DNA Translation: DAA09445.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S59324

NCBI Reference Sequences

More...
RefSeqi
NP_013235.1, NM_001182021.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YLR134W_mRNA; YLR134W_mRNA; YLR134W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
850825

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YLR134W

<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
X15668 Genomic DNA Translation: CAA33709.1
X91258 Genomic DNA Translation: CAA62647.1
Z73306 Genomic DNA Translation: CAA97705.1
U53881 Genomic DNA Translation: AAB82395.1
BK006945 Genomic DNA Translation: DAA09445.1
PIRiS59324
RefSeqiNP_013235.1, NM_001182021.1

3D structure databases

ProteinModelPortaliP16467
SMRiP16467
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31403, 52 interactors
DIPiDIP-4603N
IntActiP16467, 12 interactors
MINTiP16467
STRINGi4932.YLR134W

PTM databases

CarbonylDBiP16467
iPTMnetiP16467

Proteomic databases

MaxQBiP16467
PaxDbiP16467
PRIDEiP16467
TopDownProteomicsiP16467

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR134W_mRNA; YLR134W_mRNA; YLR134W
GeneIDi850825
KEGGisce:YLR134W

Organism-specific databases

EuPathDBiFungiDB:YLR134W
SGDiS000004124 PDC5

Phylogenomic databases

GeneTreeiENSGT00940000176336
HOGENOMiHOG000061334
InParanoidiP16467
KOiK01568
OMAiTHFRSNE

Enzyme and pathway databases

UniPathwayi
UPA00206

UPA00866

BioCyciMetaCyc:YLR134W-MONOMER
YEAST:YLR134W-MONOMER
BRENDAi4.1.1.1 984
SABIO-RKiP16467

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P16467

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 nameiPDC5_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: P16467
Secondary accession number(s): D6VYC9
<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: August 1, 1990
Last sequence update: January 23, 2007
Last modified: February 13, 2019
This is version 183 of the entry and version 4 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

Complete proteome, Reference proteome

Documents

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