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Protein

Transketolase 1

Gene

tktA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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. Thus, 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.2 Publications

Catalytic activityi

Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate.2 Publications

Cofactori

Protein has several cofactor binding sites:
  • Mg2+1 Publication, Ca2+1 Publication, Mn2+1 Publication, Co2+1 PublicationNote: Binds 1 Mg2+ ion per subunit. Can also utilize other divalent metal cations, such as Ca2+, Mn2+ and Co2+.1 Publication
  • thiamine diphosphate1 PublicationNote: Binds 1 thiamine pyrophosphate per subunit. During the reaction, the substrate forms a covalent intermediate with the cofactor.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei26Substrate1 Publication1
Sitei26Important for catalytic activity1
Binding sitei66Thiamine pyrophosphateCombined sources2 Publications1
Metal bindingi155Magnesium2 Publications1
Binding sitei156Thiamine pyrophosphate; via amide nitrogenCombined sources1 Publication1
Metal bindingi185Magnesium2 Publications1
Binding sitei185Thiamine pyrophosphateCombined sources2 Publications1
Metal bindingi187Magnesium; via carbonyl oxygen2 Publications1
Binding sitei261Substrate1 Publication1
Binding sitei261Thiamine pyrophosphateCombined sources2 Publications1
Sitei261Important for catalytic activity1
Binding sitei358Substrate1 Publication1
Binding sitei385Substrate1 Publication1
Active sitei411Proton donorCurated1
Binding sitei437Thiamine pyrophosphate2 Publications1
Binding sitei461Substrate1 Publication1
Binding sitei469Substrate1 Publication1
Binding sitei473Substrate1 Publication1
Binding sitei520Substrate1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi114 – 116Thiamine pyrophosphateCombined sources2 Publications3

GO - Molecular functioni

  • manganese ion binding Source: EcoCyc
  • thiamine pyrophosphate binding Source: EcoCyc
  • transketolase activity Source: EcoCyc

GO - Biological processi

  • cellular response to antibiotic Source: CAFA
  • cellular response to chloramphenicol Source: CAFA
  • cellular response to hydrogen peroxide Source: CAFA
  • cellular response to menadione Source: CAFA
  • cellular response to paraquat Source: CAFA
  • pentose-phosphate shunt, non-oxidative branch Source: EcoCyc
  • positive regulation of transcription, DNA-templated Source: CAFA

Keywordsi

Molecular functionTransferase
LigandCalcium, Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciEcoCyc:TRANSKETOI-MONOMER
MetaCyc:TRANSKETOI-MONOMER
BRENDAi2.2.1.1 2026
SABIO-RKiP27302

Protein family/group databases

MoonProtiP27302

Names & Taxonomyi

Protein namesi
Recommended name:
Transketolase 1 (EC:2.2.1.12 Publications)
Short name:
TK 1
Gene namesi
Name:tktA
Synonyms:tkt
Ordered Locus Names:b2935, JW5478
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11427 tktA

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • protein-containing complex Source: CAFA

Pathology & Biotechi

Chemistry databases

DrugBankiDB01987 Thiamin Diphosphate

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001918561 – 663Transketolase 1Add BLAST663

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei46N6-acetyllysine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP27302
PaxDbiP27302
PRIDEiP27302

PTM databases

iPTMnetiP27302

Interactioni

Subunit structurei

Homodimer.3 Publications

Protein-protein interaction databases

BioGridi4260954, 9 interactors
DIPiDIP-10998N
IntActiP27302, 1 interactor
STRINGi316385.ECDH10B_3110

Structurei

Secondary structure

1663
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 22Combined sources19
Helixi28 – 43Combined sources16
Beta strandi59 – 64Combined sources6
Helixi65 – 67Combined sources3
Helixi68 – 78Combined sources11
Helixi84 – 87Combined sources4
Turni88 – 91Combined sources4
Turni103 – 105Combined sources3
Helixi118 – 137Combined sources20
Beta strandi149 – 153Combined sources5
Helixi155 – 159Combined sources5
Helixi161 – 172Combined sources12
Beta strandi178 – 184Combined sources7
Beta strandi186 – 188Combined sources3
Helixi193 – 195Combined sources3
Helixi201 – 207Combined sources7
Beta strandi211 – 217Combined sources7
Helixi221 – 233Combined sources13
Beta strandi239 – 244Combined sources6
Turni247 – 250Combined sources4
Turni252 – 256Combined sources5
Helixi258 – 260Combined sources3
Beta strandi261 – 263Combined sources3
Helixi267 – 277Combined sources11
Helixi288 – 294Combined sources7
Helixi297 – 317Combined sources21
Helixi319 – 330Combined sources12
Helixi337 – 350Combined sources14
Helixi357 – 368Combined sources12
Turni369 – 371Combined sources3
Beta strandi375 – 381Combined sources7
Helixi383 – 386Combined sources4
Turni396 – 398Combined sources3
Beta strandi403 – 406Combined sources4
Helixi411 – 424Combined sources14
Beta strandi428 – 434Combined sources7
Helixi435 – 439Combined sources5
Helixi442 – 450Combined sources9
Beta strandi456 – 460Combined sources5
Helixi464 – 466Combined sources3
Turni471 – 473Combined sources3
Helixi478 – 483Combined sources6
Beta strandi489 – 491Combined sources3
Helixi496 – 508Combined sources13
Beta strandi510 – 512Combined sources3
Beta strandi514 – 517Combined sources4
Beta strandi520 – 523Combined sources4
Helixi530 – 535Combined sources6
Helixi536 – 538Combined sources3
Beta strandi541 – 544Combined sources4
Beta strandi547 – 549Combined sources3
Beta strandi551 – 556Combined sources6
Helixi558 – 560Combined sources3
Helixi561 – 574Combined sources14
Beta strandi578 – 582Combined sources5
Helixi586 – 590Combined sources5
Helixi594 – 600Combined sources7
Beta strandi608 – 615Combined sources8
Helixi616 – 619Combined sources4
Helixi620 – 623Combined sources4
Beta strandi626 – 632Combined sources7
Helixi641 – 647Combined sources7
Helixi652 – 662Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QGDX-ray1.90A/B2-663[»]
2R5NX-ray1.60A/B1-663[»]
2R8OX-ray1.47A/B1-663[»]
2R8PX-ray1.65A/B1-663[»]
5HHTX-ray1.50A/B1-663[»]
ProteinModelPortaliP27302
SMRiP27302
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27302

Family & Domainsi

Sequence similaritiesi

Belongs to the transketolase family.Curated

Phylogenomic databases

eggNOGiENOG4105CV1 Bacteria
COG0021 LUCA
HOGENOMiHOG000225953
InParanoidiP27302
KOiK00615
OMAiFADYMRG
PhylomeDBiP27302

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

P27302-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSRKELANA IRALSMDAVQ KAKSGHPGAP MGMADIAEVL WRDFLKHNPQ
60 70 80 90 100
NPSWADRDRF VLSNGHGSML IYSLLHLTGY DLPMEELKNF RQLHSKTPGH
110 120 130 140 150
PEVGYTAGVE TTTGPLGQGI ANAVGMAIAE KTLAAQFNRP GHDIVDHYTY
160 170 180 190 200
AFMGDGCMME GISHEVCSLA GTLKLGKLIA FYDDNGISID GHVEGWFTDD
210 220 230 240 250
TAMRFEAYGW HVIRDIDGHD AASIKRAVEE ARAVTDKPSL LMCKTIIGFG
260 270 280 290 300
SPNKAGTHDS HGAPLGDAEI ALTREQLGWK YAPFEIPSEI YAQWDAKEAG
310 320 330 340 350
QAKESAWNEK FAAYAKAYPQ EAAEFTRRMK GEMPSDFDAK AKEFIAKLQA
360 370 380 390 400
NPAKIASRKA SQNAIEAFGP LLPEFLGGSA DLAPSNLTLW SGSKAINEDA
410 420 430 440 450
AGNYIHYGVR EFGMTAIANG ISLHGGFLPY TSTFLMFVEY ARNAVRMAAL
460 470 480 490 500
MKQRQVMVYT HDSIGLGEDG PTHQPVEQVA SLRVTPNMST WRPCDQVESA
510 520 530 540 550
VAWKYGVERQ DGPTALILSR QNLAQQERTE EQLANIARGG YVLKDCAGQP
560 570 580 590 600
ELIFIATGSE VELAVAAYEK LTAEGVKARV VSMPSTDAFD KQDAAYRESV
610 620 630 640 650
LPKAVTARVA VEAGIADYWY KYVGLNGAIV GMTTFGESAP AELLFEEFGF
660
TVDNVVAKAK ELL
Length:663
Mass (Da):72,212
Last modified:October 11, 2004 - v5
Checksum:iFE6D624ADD11939A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti103 – 107VGYTA → SGVTPL in CAA48166 (PubMed:8241274).Curated5
Sequence conflicti584P → S in CAA48166 (PubMed:8241274).Curated1
Sequence conflicti584P → S in AAA69102 (PubMed:9278503).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68025 Genomic DNA Translation: CAA48166.1
U28377 Genomic DNA Translation: AAA69102.1
U00096 Genomic DNA Translation: AAT48155.1
AP009048 Genomic DNA Translation: BAE76998.1
M32363 Genomic DNA No translation available.
PIRiF65078 XJECTK
RefSeqiWP_000098614.1, NZ_LN832404.1
YP_026188.1, NC_000913.3

Genome annotation databases

EnsemblBacteriaiAAT48155; AAT48155; b2935
BAE76998; BAE76998; BAE76998
GeneIDi947420
KEGGiecj:JW5478
eco:b2935
PATRICifig|1411691.4.peg.3798

Similar proteinsi

Entry informationi

Entry nameiTKT1_ECOLI
AccessioniPrimary (citable) accession number: P27302
Secondary accession number(s): Q2M9Q8, Q6BF59
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: October 11, 2004
Last modified: April 25, 2018
This is version 160 of the entry and version 5 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health