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Protein

Transketolase

Gene

Tkt

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.By similarity

Catalytic activityi

Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate.

Cofactori

Protein has several cofactor binding sites:
  • Mg2+By similarity, Ca2+By similarity, Mn2+By similarity, Co2+By similarityNote: Binds 1 Mg2+ ion per subunit. Can also utilize other divalent metal cations, such as Ca2+, Mn2+ and Co2+.By similarity
  • thiamine diphosphateBy similarityNote: Binds 1 thiamine pyrophosphate per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei37SubstrateBy similarity1
Sitei37Important for catalytic activityBy similarity1
Binding sitei40Thiamine pyrophosphateBy similarity1
Binding sitei77Thiamine pyrophosphateBy similarity1
Metal bindingi155MagnesiumBy similarity1
Binding sitei156Thiamine pyrophosphate; via amide nitrogenBy similarity1
Metal bindingi185MagnesiumBy similarity1
Binding sitei185Thiamine pyrophosphateBy similarity1
Metal bindingi187Magnesium; via carbonyl oxygenBy similarity1
Binding sitei244Thiamine pyrophosphateBy similarity1
Binding sitei258SubstrateBy similarity1
Binding sitei258Thiamine pyrophosphateBy similarity1
Sitei258Important for catalytic activityBy similarity1
Binding sitei318SubstrateBy similarity1
Binding sitei345SubstrateBy similarity1
Active sitei366Proton donorBy similarity1
Binding sitei392Thiamine pyrophosphateBy similarity1
Binding sitei416SubstrateBy similarity1
Binding sitei424SubstrateBy similarity1
Binding sitei428Thiamine pyrophosphateBy similarity1
Binding sitei474SubstrateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi123 – 125Thiamine pyrophosphateBy similarity3

GO - Molecular functioni

  • carbohydrate binding Source: RGD
  • magnesium ion binding Source: RGD
  • monosaccharide binding Source: RGD
  • thiamine pyrophosphate binding Source: RGD
  • transketolase activity Source: RGD

GO - Biological processi

  • pentose-phosphate shunt Source: RGD
  • pentose-phosphate shunt, non-oxidative branch Source: RGD
  • ribose phosphate biosynthetic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

Calcium, Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

SABIO-RKP50137.

Names & Taxonomyi

Protein namesi
Recommended name:
Transketolase (EC:2.2.1.1)
Short name:
TK
Gene namesi
Name:Tkt
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621036. Tkt.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: RGD
  • intracellular membrane-bounded organelle Source: RGD
  • peroxisome Source: RGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001918981 – 623TransketolaseAdd BLAST623

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei6N6-acetyllysineBy similarity1
Modified residuei11N6-acetyllysineBy similarity1
Modified residuei104PhosphoserineBy similarity1
Modified residuei144N6-acetyllysineBy similarity1
Modified residuei204N6-acetyllysineBy similarity1
Modified residuei232N6-acetyllysineBy similarity1
Modified residuei241N6-acetyllysineBy similarity1
Modified residuei260N6-acetyllysineBy similarity1
Modified residuei275PhosphotyrosineBy similarity1
Modified residuei287PhosphothreonineCombined sources1
Modified residuei295PhosphoserineBy similarity1
Modified residuei345PhosphoserineCombined sources1
Modified residuei538N6-acetyllysineBy similarity1
Modified residuei603N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP50137.
PeptideAtlasiP50137.
PRIDEiP50137.

2D gel databases

World-2DPAGE0004:P50137.

PTM databases

iPTMnetiP50137.
PhosphoSitePlusiP50137.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi249108. 1 interactor.
IntActiP50137. 2 interactors.
MINTiMINT-4566297.
STRINGi10116.ENSRNOP00000021862.

Structurei

3D structure databases

ProteinModelPortaliP50137.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the transketolase family.Curated

Phylogenomic databases

eggNOGiKOG0523. Eukaryota.
COG0021. LUCA.
HOGENOMiHOG000243868.
HOVERGENiHBG004036.
InParanoidiP50137.
KOiK00615.
PhylomeDBiP50137.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR029061. THDP-binding.
IPR009014. Transketo_C/PFOR_II.
IPR005475. Transketolase-like_Pyr-bd.
IPR020826. Transketolase_BS.
IPR033248. Transketolase_C.
IPR033247. Transketolase_fam.
IPR005474. Transketolase_N.
[Graphical view]
PANTHERiPTHR11624. PTHR11624. 1 hit.
PfamiPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
PF00456. Transketolase_N. 1 hit.
[Graphical view]
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 2 hits.
SSF52922. SSF52922. 1 hit.
PROSITEiPS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P50137-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGYHKPDQQ KLQALKDTAN RLRISSIQAT TAAGSGHPTS CCSAAEIMAV
60 70 80 90 100
LFFHTMRYKA LDPRNPHNDR FVLSKGHAAP ILYAVWAEAG FLPEAELLNL
110 120 130 140 150
RKISSDLDGH PVPKQAFTDV ATGSLGQGLG AACGMAYTGK YFDKASYRVY
160 170 180 190 200
CMLGDGEVSE GSVWEAMAFA GIYKLDNLVA IFDINRLGQS DPAPLQHQVD
210 220 230 240 250
VYQKRCEAFG WHAIIVDGHS VEELCKAFGQ AKHQPTAIIA KTFKGRGITG
260 270 280 290 300
IEDKEAWHGK PLPKNMAEQI IQEIYSQVQS KKKILATPPQ EDAPSVDIAN
310 320 330 340 350
IRMPTPPNYK VGDKIATRKA YGLALAKLGH ASDRIIALDG DTKNSTFSEL
360 370 380 390 400
FKKEHPDRFI ECYIAEQNMV SIAVGCATRD RTVPFCSTFA AFFTRAFDQI
410 420 430 440 450
RMAAISESNI NLCGSHCGVS IGEDGPSQMA LEDLAMFRSV PMSTVFYPSD
460 470 480 490 500
GVATEKAVEL AANTKGICFI RTSRPENAII YSNNEDFQVG QAKVVLKSKD
510 520 530 540 550
DQVTVIGAGV TLHEALAAAE MLKKEKIGVR VLDPFTIKPL DKKLILDCAR
560 570 580 590 600
ATKGRILTVE DHYYEGGIGE AVSAVVVGEP GVTVTRLAVS QVPRSGKPAE
610 620
LLKMFGIDKD AIVQAVKGLV TKG
Length:623
Mass (Da):67,644
Last modified:October 1, 1996 - v1
Checksum:iA198AB56A73C23CE
GO

Sequence cautioni

The sequence AAA18026 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09256 mRNA. Translation: AAA18026.1. Different initiation.
RefSeqiNP_072114.1. NM_022592.1.
UniGeneiRn.5950.

Genome annotation databases

GeneIDi64524.
KEGGirno:64524.
UCSCiRGD:621036. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09256 mRNA. Translation: AAA18026.1. Different initiation.
RefSeqiNP_072114.1. NM_022592.1.
UniGeneiRn.5950.

3D structure databases

ProteinModelPortaliP50137.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249108. 1 interactor.
IntActiP50137. 2 interactors.
MINTiMINT-4566297.
STRINGi10116.ENSRNOP00000021862.

PTM databases

iPTMnetiP50137.
PhosphoSitePlusiP50137.

2D gel databases

World-2DPAGE0004:P50137.

Proteomic databases

PaxDbiP50137.
PeptideAtlasiP50137.
PRIDEiP50137.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi64524.
KEGGirno:64524.
UCSCiRGD:621036. rat.

Organism-specific databases

CTDi7086.
RGDi621036. Tkt.

Phylogenomic databases

eggNOGiKOG0523. Eukaryota.
COG0021. LUCA.
HOGENOMiHOG000243868.
HOVERGENiHBG004036.
InParanoidiP50137.
KOiK00615.
PhylomeDBiP50137.

Enzyme and pathway databases

SABIO-RKP50137.

Miscellaneous databases

PROiP50137.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR029061. THDP-binding.
IPR009014. Transketo_C/PFOR_II.
IPR005475. Transketolase-like_Pyr-bd.
IPR020826. Transketolase_BS.
IPR033248. Transketolase_C.
IPR033247. Transketolase_fam.
IPR005474. Transketolase_N.
[Graphical view]
PANTHERiPTHR11624. PTHR11624. 1 hit.
PfamiPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
PF00456. Transketolase_N. 1 hit.
[Graphical view]
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 2 hits.
SSF52922. SSF52922. 1 hit.
PROSITEiPS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTKT_RAT
AccessioniPrimary (citable) accession number: P50137
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.