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Entry version 196 (05 Jun 2019)
Sequence version 4 (23 Jan 2007)
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Protein

Transketolase 1

Gene

TKL1

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

Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.1 Publication

Miscellaneous

Present with 40300 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:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei30Substrate1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei30Important for catalytic activity1
Binding sitei69Thiamine pyrophosphate3 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 bindingi157Magnesium1
Binding sitei158Thiamine pyrophosphate; via amide nitrogen3 Publications1
Metal bindingi187Magnesium1
Binding sitei187Thiamine pyrophosphate3 Publications1
Metal bindingi189Magnesium; via carbonyl oxygen1
Binding sitei263Substrate1
Binding sitei263Thiamine pyrophosphate3 Publications1
Sitei263Important for catalytic activity1
Binding sitei359Substrate1
Binding sitei386Substrate1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei418Proton donorCurated1
Binding sitei418Thiamine pyrophosphate3 Publications1
Binding sitei445Thiamine pyrophosphate3 Publications1
Binding sitei469Substrate1
Binding sitei477Substrate1
Binding sitei528Substrate1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi116 – 118Thiamine pyrophosphate3 Publications3

<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

  • metal ion binding Source: UniProtKB-KW
  • transketolase activity Source: SGD

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 functionTransferase
LigandCalcium, Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:YPR074C-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.2.1.1 984

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P23254

<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:
Transketolase 1 (EC:2.2.1.1)
Short name:
TK 1
<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:TKL1
Ordered Locus Names:YPR074C
ORF Names:YP9499.29C
<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 XVI

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YPR074C

Saccharomyces Genome Database

More...
SGDi
S000006278 TKL1

<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

<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

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>Mutagenesisi30H → A or Q: Strongly reduced catalytic activity. Decreases affinity for xylulose 5-phosphate about 15 times. 1 Publication1
Mutagenesisi30H → N: Loss of activity. 1 Publication1
Mutagenesisi69H → A: Reduces catalytic activity by about 98%. Decreased affinity for donor substrate. 1 Publication1
Mutagenesisi103H → A or N: Reduces activity by over 96% and decreases affinity for thiamine pyrophosphate and xylulose 5-phosphate. 2 Publications1
Mutagenesisi103H → F: Loss of activity. 2 Publications1
Mutagenesisi162E → A or Q: Most catalytic properties similar to wild-type. 1 Publication1
Mutagenesisi263H → A: Strongly reduced catalytic activity. 1 Publication1
Mutagenesisi359R → A: Slightly reduced affinity for xylulose 5-phosphate and strongly reduced affinity for ribose 5-phosphate. 1 Publication1
Mutagenesisi382D → A or R: Severe loss of activity. 1 Publication1
Mutagenesisi469H → A: Strongly reduced affinity for xylulose 5-phosphate and ribose 5-phosphate. 1 Publication1
Mutagenesisi477D → A: Strongly reduced catalytic activity. Strongly reduced affinity for xylulose 5-phosphate and ribose 5-phosphate. 1 Publication1
Mutagenesisi481H → A or Q: Reduces catalytic activity by about 95%. 1 Publication1
Mutagenesisi528R → A: Reduced affinity for xylulose 5-phosphate and strongly reduced affinity for ribose 5-phosphate. 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 methionineiRemoved1 Publication
<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_00001919042 – 680Transketolase 1Add BLAST679

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 residuei286PhosphoserineCombined sources1
Modified residuei335PhosphoserineCombined sources1
Modified residuei402PhosphoserineCombined sources1
Modified residuei492PhosphoserineCombined sources1
<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-linki647Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P23254

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

More...
PaxDbi
P23254

PRoteomics IDEntifications database

More...
PRIDEi
P23254

Consortium for Top Down Proteomics

More...
TopDownProteomicsi
P23254

2D gel databases

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

More...
SWISS-2DPAGEi
P23254

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P23254

<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

Homodimer.5 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
RSP5P399402EBI-19291,EBI-16219

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
36247, 211 interactors

Database of interacting proteins

More...
DIPi
DIP-6765N

Protein interaction database and analysis system

More...
IntActi
P23254, 13 interactors

Molecular INTeraction database

More...
MINTi
P23254

STRING: functional protein association networks

More...
STRINGi
4932.YPR074C

<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

1680
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
P23254

Database of comparative protein structure models

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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
P23254

<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

<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 transketolase family.Curated

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000176704

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000225953

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P23254

KEGG Orthology (KO)

More...
KOi
K00615

Identification of Orthologs from Complete Genome Data

More...
OMAi
FADYMRG

Family and domain databases

Conserved Domains Database

More...
CDDi
cd02012 TPP_TK, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.920, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR029061 THDP-binding
IPR009014 Transketo_C/PFOR_II
IPR005475 Transketolase-like_Pyr-bd
IPR005478 Transketolase_bac-like
IPR020826 Transketolase_BS
IPR033248 Transketolase_C
IPR033247 Transketolase_fam
IPR005474 Transketolase_N

The PANTHER Classification System

More...
PANTHERi
PTHR43522 PTHR43522, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02779 Transket_pyr, 1 hit
PF02780 Transketolase_C, 1 hit
PF00456 Transketolase_N, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00861 Transket_pyr, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52518 SSF52518, 2 hits
SSF52922 SSF52922, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00232 tktlase_bact, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00801 TRANSKETOLASE_1, 1 hit
PS00802 TRANSKETOLASE_2, 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>. The information is filed in different subsections. The current subsections and their content are listed below:<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.

P23254-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTQFTDIDKL AVSTIRILAV DTVSKANSGH PGAPLGMAPA AHVLWSQMRM
60 70 80 90 100
NPTNPDWINR DRFVLSNGHA VALLYSMLHL TGYDLSIEDL KQFRQLGSRT
110 120 130 140 150
PGHPEFELPG VEVTTGPLGQ GISNAVGMAM AQANLAATYN KPGFTLSDNY
160 170 180 190 200
TYVFLGDGCL QEGISSEASS LAGHLKLGNL IAIYDDNKIT IDGATSISFD
210 220 230 240 250
EDVAKRYEAY GWEVLYVENG NEDLAGIAKA IAQAKLSKDK PTLIKMTTTI
260 270 280 290 300
GYGSLHAGSH SVHGAPLKAD DVKQLKSKFG FNPDKSFVVP QEVYDHYQKT
310 320 330 340 350
ILKPGVEANN KWNKLFSEYQ KKFPELGAEL ARRLSGQLPA NWESKLPTYT
360 370 380 390 400
AKDSAVATRK LSETVLEDVY NQLPELIGGS ADLTPSNLTR WKEALDFQPP
410 420 430 440 450
SSGSGNYSGR YIRYGIREHA MGAIMNGISA FGANYKPYGG TFLNFVSYAA
460 470 480 490 500
GAVRLSALSG HPVIWVATHD SIGVGEDGPT HQPIETLAHF RSLPNIQVWR
510 520 530 540 550
PADGNEVSAA YKNSLESKHT PSIIALSRQN LPQLEGSSIE SASKGGYVLQ
560 570 580 590 600
DVANPDIILV ATGSEVSLSV EAAKTLAAKN IKARVVSLPD FFTFDKQPLE
610 620 630 640 650
YRLSVLPDNV PIMSVEVLAT TCWGKYAHQS FGIDRFGASG KAPEVFKFFG
660 670 680
FTPEGVAERA QKTIAFYKGD KLISPLKKAF
Length:680
Mass (Da):73,806
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:i40225EAA23A63835
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 conflicti37 – 38MA → RS in AAA35168 (PubMed:1737042).Curated2
Sequence conflicti45 – 77WSQMR…LLYSM → GESNAHEPNQPKTGSTEIDL SCLTVTRSLCCIY in AAA35168 (PubMed:1737042).CuratedAdd BLAST33
Sequence conflicti136 – 143AATYNKPG → DMPLTTSRA in AAA35168 (PubMed:1737042).Curated8
Sequence conflicti232 – 234AQA → RQR in AAA35168 (PubMed:1737042).Curated3
Sequence conflicti243 – 257LIKMT…GSLHA → FDQNDHNHWLRFLRS AA sequence (PubMed:1737042).CuratedAdd BLAST15
Sequence conflicti383L → LVLPIL AA sequence (PubMed:1737042).Curated1
Sequence conflicti396D → S in AAA35168 (PubMed:1737042).Curated1
Sequence conflicti528 – 538RQNLPQLEGSS → PDKTCHNWKVAL in AAA35168 (PubMed:1737042).CuratedAdd BLAST11
Sequence conflicti639 – 680SGKAP…LKKAF → PVRHQKSSSSSVSPQKVLLK ELKRPLHSIRVTS in AAA35168 (PubMed:1737042).CuratedAdd BLAST42

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
M63302 Genomic DNA Translation: AAA35168.1
X73224 Genomic DNA Translation: CAA51693.1
Z49219 Genomic DNA Translation: CAA89191.1
Z71255 Genomic DNA Translation: CAA94982.1
U51033 Genomic DNA Translation: AAB68125.1
BK006949 Genomic DNA Translation: DAA11494.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A49510 XJBYTK

NCBI Reference Sequences

More...
RefSeqi
NP_015399.1, NM_001184171.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YPR074C_mRNA; YPR074C_mRNA; YPR074C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
856188

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YPR074C

<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
M63302 Genomic DNA Translation: AAA35168.1
X73224 Genomic DNA Translation: CAA51693.1
Z49219 Genomic DNA Translation: CAA89191.1
Z71255 Genomic DNA Translation: CAA94982.1
U51033 Genomic DNA Translation: AAB68125.1
BK006949 Genomic DNA Translation: DAA11494.1
PIRiA49510 XJBYTK
RefSeqiNP_015399.1, NM_001184171.1

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
1AY0X-ray2.60A/B1-680[»]
1GPUX-ray1.86A/B1-680[»]
1NGSX-ray2.40A/B1-680[»]
1TKAX-ray2.70A/B3-680[»]
1TKBX-ray2.30A/B3-680[»]
1TKCX-ray2.70A/B3-680[»]
1TRKX-ray2.00A/B1-680[»]
SMRiP23254
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36247, 211 interactors
DIPiDIP-6765N
IntActiP23254, 13 interactors
MINTiP23254
STRINGi4932.YPR074C

PTM databases

iPTMnetiP23254

2D gel databases

SWISS-2DPAGEiP23254

Proteomic databases

MaxQBiP23254
PaxDbiP23254
PRIDEiP23254
TopDownProteomicsiP23254

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPR074C_mRNA; YPR074C_mRNA; YPR074C
GeneIDi856188
KEGGisce:YPR074C

Organism-specific databases

EuPathDBiFungiDB:YPR074C
SGDiS000006278 TKL1

Phylogenomic databases

GeneTreeiENSGT00940000176704
HOGENOMiHOG000225953
InParanoidiP23254
KOiK00615
OMAiFADYMRG

Enzyme and pathway databases

BioCyciYEAST:YPR074C-MONOMER
BRENDAi2.2.1.1 984
SABIO-RKiP23254

Miscellaneous databases

EvolutionaryTraceiP23254

Protein Ontology

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PROi
PR:P23254

Family and domain databases

CDDicd02012 TPP_TK, 1 hit
Gene3Di3.40.50.920, 1 hit
InterProiView protein in InterPro
IPR029061 THDP-binding
IPR009014 Transketo_C/PFOR_II
IPR005475 Transketolase-like_Pyr-bd
IPR005478 Transketolase_bac-like
IPR020826 Transketolase_BS
IPR033248 Transketolase_C
IPR033247 Transketolase_fam
IPR005474 Transketolase_N
PANTHERiPTHR43522 PTHR43522, 1 hit
PfamiView protein in Pfam
PF02779 Transket_pyr, 1 hit
PF02780 Transketolase_C, 1 hit
PF00456 Transketolase_N, 1 hit
SMARTiView protein in SMART
SM00861 Transket_pyr, 1 hit
SUPFAMiSSF52518 SSF52518, 2 hits
SSF52922 SSF52922, 1 hit
TIGRFAMsiTIGR00232 tktlase_bact, 1 hit
PROSITEiView protein in PROSITE
PS00801 TRANSKETOLASE_1, 1 hit
PS00802 TRANSKETOLASE_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<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 nameiTKT1_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: P23254
Secondary accession number(s): D6W478
<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: November 1, 1991
Last sequence update: January 23, 2007
Last modified: June 5, 2019
This is version 196 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

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 XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: 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
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