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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei37 – 371SubstrateBy similarity
Sitei37 – 371Important for catalytic activityBy similarity
Binding sitei40 – 401Thiamine pyrophosphateBy similarity
Binding sitei77 – 771Thiamine pyrophosphateBy similarity
Metal bindingi155 – 1551MagnesiumBy similarity
Binding sitei156 – 1561Thiamine pyrophosphate; via amide nitrogenBy similarity
Metal bindingi185 – 1851MagnesiumBy similarity
Binding sitei185 – 1851Thiamine pyrophosphateBy similarity
Metal bindingi187 – 1871Magnesium; via carbonyl oxygenBy similarity
Binding sitei244 – 2441Thiamine pyrophosphateBy similarity
Binding sitei258 – 2581SubstrateBy similarity
Binding sitei258 – 2581Thiamine pyrophosphateBy similarity
Sitei258 – 2581Important for catalytic activityBy similarity
Binding sitei318 – 3181SubstrateBy similarity
Binding sitei345 – 3451SubstrateBy similarity
Active sitei366 – 3661Proton donorBy similarity
Binding sitei392 – 3921Thiamine pyrophosphateBy similarity
Binding sitei416 – 4161SubstrateBy similarity
Binding sitei424 – 4241SubstrateBy similarity
Binding sitei428 – 4281Thiamine pyrophosphateBy similarity
Binding sitei474 – 4741SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi123 – 1253Thiamine pyrophosphateBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 623623TransketolasePRO_0000191898Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei6 – 61N6-acetyllysineBy similarity
Modified residuei11 – 111N6-acetyllysineBy similarity
Modified residuei144 – 1441N6-acetyllysineBy similarity
Modified residuei204 – 2041N6-acetyllysineBy similarity
Modified residuei232 – 2321N6-acetyllysineBy similarity
Modified residuei241 – 2411N6-acetyllysineBy similarity
Modified residuei260 – 2601N6-acetyllysineBy similarity
Modified residuei275 – 2751PhosphotyrosineBy similarity
Modified residuei287 – 2871PhosphothreonineCombined sources
Modified residuei295 – 2951PhosphoserineBy similarity
Modified residuei345 – 3451PhosphoserineCombined sources
Modified residuei538 – 5381N6-acetyllysineBy similarity
Modified residuei603 – 6031N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP50137.
PRIDEiP50137.

2D gel databases

World-2DPAGE0004:P50137.

PTM databases

iPTMnetiP50137.
PhosphoSiteiP50137.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi249108. 1 interaction.
IntActiP50137. 2 interactions.
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 AAA18026.1 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 interaction.
IntActiP50137. 2 interactions.
MINTiMINT-4566297.
STRINGi10116.ENSRNOP00000021862.

PTM databases

iPTMnetiP50137.
PhosphoSiteiP50137.

2D gel databases

World-2DPAGE0004:P50137.

Proteomic databases

PaxDbiP50137.
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...

Publicationsi

« Hide 'large scale' publications
  1. Kim S., Kim B., Jeng J., Song B.J.
    Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.
  2. Lubec G., Afjehi-Sadat L., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 175-186; 284-302; 382-395; 472-493 AND 556-586, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus and Spinal cord.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-287 AND SER-345, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

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: June 8, 2016
This is version 117 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.