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Protein

Transketolase 1

Gene

tktA

Organism
Escherichia coli (strain K12)
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. 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei26 – 261Substrate1 Publication
Sitei26 – 261Important for catalytic activity
Binding sitei66 – 661Thiamine pyrophosphateCombined sources2 Publications
Metal bindingi155 – 1551Magnesium2 Publications
Binding sitei156 – 1561Thiamine pyrophosphate; via amide nitrogenCombined sources1 Publication
Metal bindingi185 – 1851Magnesium2 Publications
Binding sitei185 – 1851Thiamine pyrophosphateCombined sources2 Publications
Metal bindingi187 – 1871Magnesium; via carbonyl oxygen2 Publications
Binding sitei261 – 2611Substrate1 Publication
Binding sitei261 – 2611Thiamine pyrophosphateCombined sources2 Publications
Sitei261 – 2611Important for catalytic activity
Binding sitei358 – 3581Substrate1 Publication
Binding sitei385 – 3851Substrate1 Publication
Active sitei411 – 4111Proton donorCurated
Binding sitei437 – 4371Thiamine pyrophosphate2 Publications
Binding sitei461 – 4611Substrate1 Publication
Binding sitei469 – 4691Substrate1 Publication
Binding sitei473 – 4731Substrate1 Publication
Binding sitei520 – 5201Substrate1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi114 – 1163Thiamine pyrophosphateCombined sources2 Publications

GO - Molecular functioni

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

GO - Biological processi

  • pentose-phosphate shunt, non-oxidative branch Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

Calcium, Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciEcoCyc:TRANSKETOI-MONOMER.
ECOL316407:JW5478-MONOMER.
MetaCyc:TRANSKETOI-MONOMER.
BRENDAi2.2.1.1. 2026.
SABIO-RKP27302.

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11427. tktA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 663663Transketolase 1PRO_0000191856Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 461N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP27302.
PaxDbiP27302.
PRIDEiP27302.

Interactioni

Subunit structurei

Homodimer.3 Publications

Protein-protein interaction databases

BioGridi4260954. 9 interactions.
DIPiDIP-10998N.
IntActiP27302. 1 interaction.
MINTiMINT-1260939.
STRINGi511145.b2935.

Structurei

Secondary structure

1
663
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 2219Combined sources
Helixi28 – 4316Combined sources
Beta strandi59 – 646Combined sources
Helixi65 – 673Combined sources
Helixi68 – 7811Combined sources
Helixi84 – 874Combined sources
Turni88 – 914Combined sources
Turni103 – 1053Combined sources
Helixi118 – 13720Combined sources
Beta strandi149 – 1535Combined sources
Helixi155 – 1595Combined sources
Helixi161 – 17212Combined sources
Beta strandi178 – 1847Combined sources
Beta strandi186 – 1883Combined sources
Helixi193 – 1953Combined sources
Helixi201 – 2077Combined sources
Beta strandi211 – 2177Combined sources
Helixi221 – 23313Combined sources
Beta strandi239 – 2446Combined sources
Turni247 – 2504Combined sources
Turni252 – 2565Combined sources
Helixi258 – 2603Combined sources
Beta strandi261 – 2633Combined sources
Helixi267 – 27711Combined sources
Helixi288 – 2947Combined sources
Helixi297 – 31721Combined sources
Helixi319 – 33012Combined sources
Helixi337 – 35014Combined sources
Helixi357 – 36812Combined sources
Turni369 – 3713Combined sources
Beta strandi375 – 3817Combined sources
Helixi383 – 3864Combined sources
Turni396 – 3983Combined sources
Beta strandi403 – 4064Combined sources
Helixi411 – 42414Combined sources
Beta strandi428 – 4347Combined sources
Helixi435 – 4395Combined sources
Helixi442 – 4509Combined sources
Beta strandi456 – 4605Combined sources
Helixi464 – 4663Combined sources
Turni471 – 4733Combined sources
Helixi478 – 4836Combined sources
Beta strandi489 – 4913Combined sources
Helixi496 – 50813Combined sources
Beta strandi510 – 5123Combined sources
Beta strandi514 – 5174Combined sources
Beta strandi520 – 5234Combined sources
Helixi530 – 5356Combined sources
Helixi536 – 5383Combined sources
Beta strandi541 – 5444Combined sources
Beta strandi547 – 5493Combined sources
Beta strandi551 – 5566Combined sources
Helixi558 – 5603Combined sources
Helixi561 – 57414Combined sources
Beta strandi578 – 5825Combined sources
Helixi586 – 5905Combined sources
Helixi594 – 6007Combined sources
Beta strandi608 – 6158Combined sources
Helixi616 – 6194Combined sources
Helixi620 – 6234Combined sources
Beta strandi626 – 6327Combined sources
Helixi641 – 6477Combined sources
Helixi652 – 66211Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP27302.

Family & Domainsi

Sequence similaritiesi

Belongs to the transketolase family.Curated

Phylogenomic databases

eggNOGiENOG4105CV1. Bacteria.
COG0021. LUCA.
HOGENOMiHOG000225953.
InParanoidiP27302.
KOiK00615.
OMAiWEVLYVE.
OrthoDBiEOG6N3CRG.
PhylomeDBiP27302.

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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti103 – 1075VGYTA → SGVTPL in CAA48166 (PubMed:8241274).Curated
Sequence conflicti584 – 5841P → S in CAA48166 (PubMed:8241274).Curated
Sequence conflicti584 – 5841P → S in AAA69102 (PubMed:9278503).Curated

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.
PATRICi32121282. VBIEscCol129921_3029.

Cross-referencesi

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.

3D structure databases

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

Protein-protein interaction databases

BioGridi4260954. 9 interactions.
DIPiDIP-10998N.
IntActiP27302. 1 interaction.
MINTiMINT-1260939.
STRINGi511145.b2935.

Proteomic databases

EPDiP27302.
PaxDbiP27302.
PRIDEiP27302.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAT48155; AAT48155; b2935.
BAE76998; BAE76998; BAE76998.
GeneIDi947420.
KEGGiecj:JW5478.
eco:b2935.
PATRICi32121282. VBIEscCol129921_3029.

Organism-specific databases

EchoBASEiEB1397.
EcoGeneiEG11427. tktA.

Phylogenomic databases

eggNOGiENOG4105CV1. Bacteria.
COG0021. LUCA.
HOGENOMiHOG000225953.
InParanoidiP27302.
KOiK00615.
OMAiWEVLYVE.
OrthoDBiEOG6N3CRG.
PhylomeDBiP27302.

Enzyme and pathway databases

BioCyciEcoCyc:TRANSKETOI-MONOMER.
ECOL316407:JW5478-MONOMER.
MetaCyc:TRANSKETOI-MONOMER.
BRENDAi2.2.1.1. 2026.
SABIO-RKP27302.

Miscellaneous databases

EvolutionaryTraceiP27302.
PROiP27302.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the Escherichia coli K-12 transketolase (tkt) gene."
    Sprenger G.A.
    Biochim. Biophys. Acta 1216:307-310(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. Sprenger G.A.
    Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 632-633.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. Cited for: SEQUENCE REVISION TO 584.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Analysis and sequence of the speB gene encoding agmatine ureohydrolase, a putrescine biosynthetic enzyme in Escherichia coli."
    Szumanski M.B.W., Boyle S.M.
    J. Bacteriol. 172:538-547(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
  7. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
    Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
    Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-46, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
  8. "Transketolase A of Escherichia coli K12. Purification and properties of the enzyme from recombinant strains."
    Sprenger G.A., Schorken U., Sprenger G., Sahm H.
    Eur. J. Biochem. 230:525-532(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR.
  9. "Crystal structure of Escherichia coli transketolase."
    Isupov M.N., Rupprecht M.P., Wilson K.S., Dauter Z., Littlechild J.A.
    Submitted (APR-1999) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-663 IN COMPLEX WITH CALCIUM AND THIAMINE PYROPHOSPHATE.
  10. "Strain and near attack conformers in enzymic thiamin catalysis: X-ray crystallographic snapshots of bacterial transketolase in covalent complex with donor ketoses xylulose 5-phosphate and fructose 6-phosphate, and in noncovalent complex with acceptor aldose ribose 5-phosphate."
    Asztalos P., Parthier C., Golbik R., Kleinschmidt M., Hubner G., Weiss M.S., Friedemann R., Wille G., Tittmann K.
    Biochemistry 46:12037-12052(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) IN COMPLEXES WITH SUBSTRATES; CALCIUM AND THIAMINE PYROPHOSPHATE, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiTKT1_ECOLI
AccessioniPrimary (citable) accession number: P27302
Secondary accession number(s): Q2M9Q8, Q6BF59
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: October 11, 2004
Last modified: May 11, 2016
This is version 144 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.