UniProtKB - P27302 (TKT1_ECOLI)

>sp|P27302|TKT1_ECOLI Transketolase 1 OS=Escherichia coli (strain K12) OX=83333 GN=tktA PE=1 SV=5
MSSRKELANAIRALSMDAVQKAKSGHPGAPMGMADIAEVLWRDFLKHNPQNPSWADRDRF
VLSNGHGSMLIYSLLHLTGYDLPMEELKNFRQLHSKTPGHPEVGYTAGVETTTGPLGQGI
ANAVGMAIAEKTLAAQFNRPGHDIVDHYTYAFMGDGCMMEGISHEVCSLAGTLKLGKLIA
FYDDNGISIDGHVEGWFTDDTAMRFEAYGWHVIRDIDGHDAASIKRAVEEARAVTDKPSL
LMCKTIIGFGSPNKAGTHDSHGAPLGDAEIALTREQLGWKYAPFEIPSEIYAQWDAKEAG
QAKESAWNEKFAAYAKAYPQEAAEFTRRMKGEMPSDFDAKAKEFIAKLQANPAKIASRKA
SQNAIEAFGPLLPEFLGGSADLAPSNLTLWSGSKAINEDAAGNYIHYGVREFGMTAIANG
ISLHGGFLPYTSTFLMFVEYARNAVRMAALMKQRQVMVYTHDSIGLGEDGPTHQPVEQVA
SLRVTPNMSTWRPCDQVESAVAWKYGVERQDGPTALILSRQNLAQQERTEEQLANIARGG
YVLKDCAGQPELIFIATGSEVELAVAAYEKLTAEGVKARVVSMPSTDAFDKQDAAYRESV
LPKAVTARVAVEAGIADYWYKYVGLNGAIVGMTTFGESAPAELLFEEFGFTVDNVVAKAK
ELL

Entry version 180 (02 Jun 2021)
Sequence version 5 (11 Oct 2004)
Previous versions | rss

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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

D-glyceraldehyde 3-phosphate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
D-sedoheptulose 7-phosphate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
=
aldehydo-D-ribose 5-phosphate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
D-xylulose 5-phosphate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
2 Publications
Manual assertion based on experiment inⁱ
- Ref.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.
- Ref.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.
EC:
2.2.1.1
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
- Search reactions for this EC number in Rhea.
2 Publications
Manual assertion based on experiment inⁱ
- Ref.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.
- Ref.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.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
D-glyceraldehyde 3-phosphate
zoom
+
D-sedoheptulose 7-phosphate
zoom
=
aldehydo-D-ribose 5-phosphate
zoom
+
D-xylulose 5-phosphate
zoom

Cofactorⁱ

Protein has several cofactor binding sites:

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	26	Substrate1 Publication	1
Siteⁱ	26	Important for catalytic activity	1
Binding siteⁱ	66	Thiamine pyrophosphateCombined sources2 Publications	1
Metal bindingⁱ	155	Magnesium2 Publications	1
Binding siteⁱ	156	Thiamine pyrophosphate; via amide nitrogenCombined sources1 Publication	1
Metal bindingⁱ	185	Magnesium2 Publications	1
Binding siteⁱ	185	Thiamine pyrophosphateCombined sources2 Publications	1
Metal bindingⁱ	187	Magnesium; via carbonyl oxygen2 Publications	1
Binding siteⁱ	261	Substrate1 Publication	1
Binding siteⁱ	261	Thiamine pyrophosphateCombined sources2 Publications	1
Siteⁱ	261	Important for catalytic activity	1
Binding siteⁱ	358	Substrate1 Publication	1
Binding siteⁱ	385	Substrate1 Publication	1
Active siteⁱ	411	Proton donorCurated	1
Binding siteⁱ	437	Thiamine pyrophosphate2 Publications	1
Binding siteⁱ	461	Substrate1 Publication	1
Binding siteⁱ	469	Substrate1 Publication	1
Binding siteⁱ	473	Substrate1 Publication	1
Binding siteⁱ	520	Substrate1 Publication	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	114 – 116	Thiamine pyrophosphateCombined sources2 Publications		3

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Transferase
Ligand	Calcium, Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BioCycⁱ	EcoCyc:TRANSKETOI-MONOMER MetaCyc:TRANSKETOI-MONOMER
BRENDAⁱ	2.2.1.1, 2026
SABIO-RKⁱ	P27302

Protein family/group databases

MoonProtⁱ	P27302

MoonProtⁱ

P27302

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
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Pathology & Biotechⁱ

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB01987, Cocarboxylase

DrugBankⁱ

DB01987, Cocarboxylase

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000191856	1 – 663	Transketolase 1Add BLAST		663

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Modified residueⁱ	46	N6-acetyllysine1 Publication		1

Keywords - PTMⁱ

Acetylation

Proteomic databases

jPOSTⁱ	P27302
PaxDbⁱ	P27302
PRIDEⁱ	P27302

PTM databases

iPTMnetⁱ	P27302

iPTMnetⁱ

P27302

Interactionⁱ

Subunit structureⁱ

Homodimer.

3 Publications

Protein-protein interaction databases

BioGRIDⁱ	4260954, 9 interactors
Database of interacting proteins More...DIPⁱ	DIP-10998N
IntActⁱ	P27302, 1 interactor
STRINGⁱ	511145.b2935

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	4 – 22	Combined sources	19
Helixⁱ	28 – 43	Combined sources	16
Beta strandⁱ	59 – 64	Combined sources	6
Helixⁱ	65 – 67	Combined sources	3
Helixⁱ	68 – 78	Combined sources	11
Helixⁱ	84 – 87	Combined sources	4
Turnⁱ	88 – 91	Combined sources	4
Turnⁱ	103 – 105	Combined sources	3
Helixⁱ	118 – 137	Combined sources	20
Beta strandⁱ	149 – 153	Combined sources	5
Helixⁱ	155 – 159	Combined sources	5
Helixⁱ	161 – 172	Combined sources	12
Beta strandⁱ	178 – 184	Combined sources	7
Beta strandⁱ	186 – 188	Combined sources	3
Helixⁱ	193 – 195	Combined sources	3
Helixⁱ	201 – 207	Combined sources	7
Beta strandⁱ	211 – 217	Combined sources	7
Helixⁱ	221 – 233	Combined sources	13
Beta strandⁱ	239 – 244	Combined sources	6
Turnⁱ	247 – 250	Combined sources	4
Turnⁱ	252 – 256	Combined sources	5
Helixⁱ	258 – 260	Combined sources	3
Beta strandⁱ	261 – 263	Combined sources	3
Helixⁱ	267 – 277	Combined sources	11
Helixⁱ	288 – 294	Combined sources	7
Helixⁱ	297 – 317	Combined sources	21
Helixⁱ	319 – 330	Combined sources	12
Helixⁱ	337 – 350	Combined sources	14
Helixⁱ	357 – 368	Combined sources	12
Turnⁱ	369 – 371	Combined sources	3
Beta strandⁱ	375 – 381	Combined sources	7
Helixⁱ	383 – 386	Combined sources	4
Turnⁱ	396 – 398	Combined sources	3
Beta strandⁱ	403 – 406	Combined sources	4
Helixⁱ	411 – 424	Combined sources	14
Beta strandⁱ	428 – 434	Combined sources	7
Helixⁱ	435 – 439	Combined sources	5
Helixⁱ	442 – 450	Combined sources	9
Beta strandⁱ	456 – 460	Combined sources	5
Helixⁱ	464 – 466	Combined sources	3
Turnⁱ	471 – 473	Combined sources	3
Helixⁱ	478 – 483	Combined sources	6
Beta strandⁱ	489 – 491	Combined sources	3
Helixⁱ	496 – 508	Combined sources	13
Beta strandⁱ	510 – 512	Combined sources	3
Beta strandⁱ	514 – 518	Combined sources	5
Beta strandⁱ	520 – 523	Combined sources	4
Helixⁱ	530 – 535	Combined sources	6
Helixⁱ	536 – 538	Combined sources	3
Beta strandⁱ	541 – 544	Combined sources	4
Beta strandⁱ	547 – 549	Combined sources	3
Beta strandⁱ	551 – 556	Combined sources	6
Helixⁱ	558 – 560	Combined sources	3
Helixⁱ	561 – 574	Combined sources	14
Beta strandⁱ	578 – 582	Combined sources	5
Helixⁱ	586 – 590	Combined sources	5
Helixⁱ	594 – 600	Combined sources	7
Beta strandⁱ	608 – 615	Combined sources	8
Helixⁱ	616 – 619	Combined sources	4
Helixⁱ	620 – 623	Combined sources	4
Beta strandⁱ	626 – 632	Combined sources	7
Helixⁱ	641 – 647	Combined sources	7
Helixⁱ	652 – 663	Combined sources	12

Show more details

3D structure databases

SMRⁱ	P27302
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P27302

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the transketolase family.Curated

Phylogenomic databases

eggNOGⁱ	COG0021, Bacteria
HOGENOMⁱ	CLU_009227_0_0_6
InParanoidⁱ	P27302
PhylomeDBⁱ	P27302

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd02012, TPP_TK, 1 hit
Gene3Dⁱ	3.40.50.920, 1 hit
InterProⁱ	View 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
PANTHERⁱ	PTHR43522, PTHR43522, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF02779, Transket_pyr, 1 hit PF02780, Transketolase_C, 1 hit PF00456, Transketolase_N, 1 hit
SMARTⁱ	View protein in SMART SM00861, Transket_pyr, 1 hit
SUPFAMⁱ	SSF52518, SSF52518, 2 hits SSF52922, SSF52922, 1 hit
TIGRFAMsⁱ	TIGR00232, tktlase_bact, 1 hit
PROSITEⁱ	View protein in PROSITE PS00801, TRANSKETOLASE_1, 1 hit PS00802, TRANSKETOLASE_2, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P27302-1 [UniParc]FASTA Add 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

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	103 – 107	VGYTA → SGVTPL in CAA48166 (PubMed:8241274).Curated	5
Sequence conflictⁱ	584	P → S in CAA48166 (PubMed:8241274).Curated	1
Sequence conflictⁱ	584	P → S in AAA69102 (PubMed:9278503).Curated	1

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.
PIRⁱ	F65078, XJECTK
NCBI Reference Sequences More...RefSeqⁱ	WP_000098614.1, NZ_STEB01000001.1 YP_026188.1, NC_000913.3

Genome annotation databases

EnsemblBacteriaⁱ	AAT48155; AAT48155; b2935 BAE76998; BAE76998; BAE76998
GeneIDⁱ	61755008 947420
KEGGⁱ	ecj:JW5478 eco:b2935
PATRICⁱ	fig\|1411691.4.peg.3798

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P27302	Transketolase		Escherichia coli H591		673	UniRef100_P27302
Transketolase		Escherichia coli H386		673
Transketolase		Escherichia coli H420		673
Transketolase		Escherichia coli H736		673
Transketolase		Escherichia coli D9		673
+98

Protein	Similar proteins		Species	Score	Length	Source
P27302	Transketolase		Escherichia coli H591		673	UniRef90_P27302
Transketolase		Escherichia coli H386		673
Transketolase		Escherichia coli H420		673
Transketolase		Escherichia coli H736		673
Transketolase		Escherichia coli D9		673
+3224

Protein	Similar proteins		Species	Score	Length	Source
P27302	Transketolase		BUCAP		665	UniRef50_P27302
Transketolase 2		PASMU		668
Transketolase 2		XANFL		687
Transketolase 1		VIBVY		664
Transketolase 1		VIBVU		664
+24364

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.
PIRⁱ	F65078, XJECTK
RefSeqⁱ	WP_000098614.1, NZ_STEB01000001.1 YP_026188.1, NC_000913.3

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1QGD	X-ray	1.90	A/B	2-663	[»]
	2R5N	X-ray	1.60	A/B	1-663	[»]
	2R8O	X-ray	1.47	A/B	1-663	[»]
	2R8P	X-ray	1.65	A/B	1-663	[»]
	5HHT	X-ray	1.50	A/B	1-663	[»]
	6RJC	X-ray	1.05	A/B	1-663	[»]
	6TJ8	X-ray	0.92	A/B	1-663	[»]
	6TJ9	X-ray	0.95	A/B	1-663	[»]
SMRⁱ	P27302
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	4260954, 9 interactors
DIPⁱ	DIP-10998N
IntActⁱ	P27302, 1 interactor
STRINGⁱ	511145.b2935

Chemistry databases

DrugBankⁱ	DB01987, Cocarboxylase

DrugBankⁱ

DB01987, Cocarboxylase

Protein family/group databases

MoonProtⁱ	P27302

MoonProtⁱ

P27302

PTM databases

iPTMnetⁱ	P27302

iPTMnetⁱ

P27302

Proteomic databases

jPOSTⁱ	P27302
PaxDbⁱ	P27302
PRIDEⁱ	P27302

Genome annotation databases

EnsemblBacteriaⁱ	AAT48155; AAT48155; b2935 BAE76998; BAE76998; BAE76998
GeneIDⁱ	61755008 947420
KEGGⁱ	ecj:JW5478 eco:b2935
PATRICⁱ	fig\|1411691.4.peg.3798

Organism-specific databases

EchoBASEⁱ	EB1397

EchoBASEⁱ

EB1397

Phylogenomic databases

eggNOGⁱ	COG0021, Bacteria
HOGENOMⁱ	CLU_009227_0_0_6
InParanoidⁱ	P27302
PhylomeDBⁱ	P27302

Enzyme and pathway databases

BioCycⁱ	EcoCyc:TRANSKETOI-MONOMER MetaCyc:TRANSKETOI-MONOMER
BRENDAⁱ	2.2.1.1, 2026
SABIO-RKⁱ	P27302

Miscellaneous databases

EvolutionaryTraceⁱ	P27302
Protein Ontology More...PROⁱ	PR:P27302

Family and domain databases

CDDⁱ	cd02012, TPP_TK, 1 hit
Gene3Dⁱ	3.40.50.920, 1 hit
InterProⁱ	View 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
PANTHERⁱ	PTHR43522, PTHR43522, 1 hit
Pfamⁱ	View protein in Pfam PF02779, Transket_pyr, 1 hit PF02780, Transketolase_C, 1 hit PF00456, Transketolase_N, 1 hit
SMARTⁱ	View protein in SMART SM00861, Transket_pyr, 1 hit
SUPFAMⁱ	SSF52518, SSF52518, 2 hits SSF52922, SSF52922, 1 hit
TIGRFAMsⁱ	TIGR00232, tktlase_bact, 1 hit
PROSITEⁱ	View protein in PROSITE PS00801, TRANSKETOLASE_1, 1 hit PS00802, TRANSKETOLASE_2, 1 hit
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	TKT1_ECOLI
Accessionⁱ	P27302Primary (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:	June 2, 2021
	This is version 180 of the entry and version 5 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

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UniProtKB - P27302 (TKT1_ECOLI)

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Transketolase 1

tktA

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Cytosol

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ