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Protein

Transketolase 2

Gene

tktB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible transfer of a two-carbon ketol group from sedoheptulose-7-phosphate to glyceraldehyde-3-phosphate, producing xylulose-5-phosphate and ribose-5-phosphate. 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).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 sitei25 – 251SubstrateBy similarity
Sitei25 – 251Important for catalytic activityBy similarity
Binding sitei65 – 651Thiamine pyrophosphateBy similarity
Metal bindingi154 – 1541MagnesiumBy similarity
Binding sitei155 – 1551Thiamine pyrophosphate; via amide nitrogenBy similarity
Metal bindingi184 – 1841MagnesiumBy similarity
Binding sitei184 – 1841Thiamine pyrophosphateBy similarity
Metal bindingi186 – 1861Magnesium; via carbonyl oxygenBy similarity
Binding sitei260 – 2601SubstrateBy similarity
Binding sitei260 – 2601Thiamine pyrophosphateBy similarity
Sitei260 – 2601Important for catalytic activityBy similarity
Binding sitei357 – 3571SubstrateBy similarity
Binding sitei384 – 3841SubstrateBy similarity
Active sitei410 – 4101Proton donorBy similarity
Binding sitei436 – 4361Thiamine pyrophosphateBy similarity
Binding sitei460 – 4601SubstrateBy similarity
Binding sitei468 – 4681SubstrateBy similarity
Binding sitei519 – 5191SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi113 – 1153Thiamine pyrophosphateBy similarity

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

Calcium, Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciEcoCyc:TRANSKETOII-MONOMER.
ECOL316407:JW2449-MONOMER.
MetaCyc:TRANSKETOII-MONOMER.
BRENDAi2.2.1.1. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Transketolase 2 (EC:2.2.1.1)
Short name:
TK 2
Gene namesi
Name:tktB
Ordered Locus Names:b2465, JW2449
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12100. tktB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 667667Transketolase 2PRO_0000191857Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei342 – 3421N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP33570.
PaxDbiP33570.
PRIDEiP33570.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi4262216. 8 interactions.
DIPiDIP-10999N.
IntActiP33570. 6 interactions.
STRINGi511145.b2465.

Structurei

3D structure databases

ProteinModelPortaliP33570.
SMRiP33570. Positions 2-662.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the transketolase family.Curated

Phylogenomic databases

eggNOGiENOG4105CV1. Bacteria.
COG0021. LUCA.
HOGENOMiHOG000225953.
InParanoidiP33570.
KOiK00615.
OMAiGSYKEDV.
PhylomeDBiP33570.

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.
IPR005478. Transketolase_bac-like.
IPR020826. Transketolase_BS.
IPR033248. Transketolase_C.
IPR033247. Transketolase_fam.
IPR005474. Transketolase_N.
[Graphical view]
PANTHERiPTHR11624. PTHR11624. 2 hits.
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.
TIGRFAMsiTIGR00232. tktlase_bact. 1 hit.
PROSITEiPS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P33570-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRKDLANAI RALSMDAVQK ANSGHPGAPM GMADIAEVLW NDFLKHNPTD
60 70 80 90 100
PTWYDRDRFI LSNGHASMLL YSLLHLTGYD LPLEELKNFR QLHSKTPGHP
110 120 130 140 150
EIGYTPGVET TTGPLGQGLA NAVGLAIAER TLAAQFNQPD HEIVDHFTYV
160 170 180 190 200
FMGDGCLMEG ISHEVCSLAG TLGLGKLIGF YDHNGISIDG ETEGWFTDDT
210 220 230 240 250
AKRFEAYHWH VIHEIDGHDP QAVKEAILEA QSVKDKPSLI ICRTVIGFGS
260 270 280 290 300
PNKAGKEEAH GAPLGEEEVA LARQKLGWHH PPFEIPKEIY HAWDAREKGE
310 320 330 340 350
KAQQSWNEKF AAYKKAHPQL AEEFTRRMSG GLPKDWEKTT QKYINELQAN
360 370 380 390 400
PAKIATRKAS QNTLNAYGPM LPELLGGSAD LAPSNLTIWK GSVSLKEDPA
410 420 430 440 450
GNYIHYGVRE FGMTAIANGI AHHGGFVPYT ATFLMFVEYA RNAARMAALM
460 470 480 490 500
KARQIMVYTH DSIGLGEDGP THQAVEQLAS LRLTPNFSTW RPCDQVEAAV
510 520 530 540 550
GWKLAVERHN GPTALILSRQ NLAQVERTPD QVKEIARGGY VLKDSGGKPD
560 570 580 590 600
IILIATGSEM EITLQAAEKL AGEGRNVRVV SLPSTDIFDA QDEEYRESVL
610 620 630 640 650
PSNVAARVAV EAGIADYWYK YVGLKGAIVG MTGYGESAPA DKLFPFFGFT
660
AENIVAKAHK VLGVKGA
Length:667
Mass (Da):73,043
Last modified:February 1, 1994 - v1
Checksum:i451D748B13ED51E5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D12473 Genomic DNA. Translation: BAA02039.1.
U00096 Genomic DNA. Translation: AAC75518.1.
AP009048 Genomic DNA. Translation: BAA16340.1.
PIRiA48660.
RefSeqiNP_416960.1. NC_000913.3.
WP_000087280.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75518; AAC75518; b2465.
BAA16340; BAA16340; BAA16340.
GeneIDi945865.
KEGGiecj:JW2449.
eco:b2465.
PATRICi32120313. VBIEscCol129921_2559.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D12473 Genomic DNA. Translation: BAA02039.1.
U00096 Genomic DNA. Translation: AAC75518.1.
AP009048 Genomic DNA. Translation: BAA16340.1.
PIRiA48660.
RefSeqiNP_416960.1. NC_000913.3.
WP_000087280.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP33570.
SMRiP33570. Positions 2-662.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262216. 8 interactions.
DIPiDIP-10999N.
IntActiP33570. 6 interactions.
STRINGi511145.b2465.

Proteomic databases

EPDiP33570.
PaxDbiP33570.
PRIDEiP33570.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75518; AAC75518; b2465.
BAA16340; BAA16340; BAA16340.
GeneIDi945865.
KEGGiecj:JW2449.
eco:b2465.
PATRICi32120313. VBIEscCol129921_2559.

Organism-specific databases

EchoBASEiEB2024.
EcoGeneiEG12100. tktB.

Phylogenomic databases

eggNOGiENOG4105CV1. Bacteria.
COG0021. LUCA.
HOGENOMiHOG000225953.
InParanoidiP33570.
KOiK00615.
OMAiGSYKEDV.
PhylomeDBiP33570.

Enzyme and pathway databases

BioCyciEcoCyc:TRANSKETOII-MONOMER.
ECOL316407:JW2449-MONOMER.
MetaCyc:TRANSKETOII-MONOMER.
BRENDAi2.2.1.1. 2026.

Miscellaneous databases

PROiP33570.

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.
IPR005478. Transketolase_bac-like.
IPR020826. Transketolase_BS.
IPR033248. Transketolase_C.
IPR033247. Transketolase_fam.
IPR005474. Transketolase_N.
[Graphical view]
PANTHERiPTHR11624. PTHR11624. 2 hits.
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.
TIGRFAMsiTIGR00232. tktlase_bact. 1 hit.
PROSITEiPS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTKT2_ECOLI
AccessioniPrimary (citable) accession number: P33570
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: September 7, 2016
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. 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.