UniProt Accession

 TKT1_ECOLI; P27302; Q2M9Q8; Q6BF59 

Genbank Protein ID

 X68025; U28377; U00096; AP009048; M32363 

Genbank Nucleotide ID

 CAA48166.1; AAA69102.1; AAT48155.1; BAE76998.1 

Protein Name

 Transketolase 1 

Protein Synonyms/Alias

 TK 1 

Gene Name

 tktA 

Gene Synonyms/Alias

 tkt; b2935; JW5478 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
21	LSMDAVQKAKSGHPG	acetylation	[1]
46	VLWRDFLKHNPQNPS	acetylation	[1, 2]
225	GHDAASIKRAVEEAR	acetylation	[1]
237	EARAVTDKPSLLMCK	acetylation	[1, 3]
244	KPSLLMCKTIIGFGS	acetylation	[1]
254	IGFGSPNKAGTHDSH	acetylation	[1]
297	IYAQWDAKEAGQAKE	acetylation	[1]
303	AKEAGQAKESAWNEK	acetylation	[3]
310	KESAWNEKFAAYAKA	acetylation	[1]
316	EKFAAYAKAYPQEAA	acetylation	[1, 3]
316	EKFAAYAKAYPQEAA	pupylation	[4]
330	AEFTRRMKGEMPSDF	acetylation	[1]
340	MPSDFDAKAKEFIAK	acetylation	[1]
342	SDFDAKAKEFIAKLQ	acetylation	[1]
347	KAKEFIAKLQANPAK	acetylation	[1, 3, 5]
347	KAKEFIAKLQANPAK	pupylation	[4]
354	KLQANPAKIASRKAS	acetylation	[1, 3]
452	VRMAALMKQRQVMVY	acetylation	[3]
591	PSTDAFDKQDAAYRE	acetylation	[1]
603	YRESVLPKAVTARVA	acetylation	[1, 3]

Reference

 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618]
 [2] 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 CF, Grishin NV, Zhao Y.
 Mol Cell Proteomics. 2009 Feb;8(2):215-25. [PMID: 18723842]
 [3] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111]
 [4] Reconstitution of the Mycobacterium tuberculosis pupylation pathway in Escherichia coli.
 Cerda-Maira FA, McAllister F, Bode NJ, Burns KE, Gygi SP, Darwin KH.
 EMBO Rep. 2011 Jul 8;12(8):863-70. [PMID: 21738222]
 [5] The diversity of lysine-acetylated proteins in Escherichia coli.
 Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG.
 J Microbiol Biotechnol. 2008 Sep;18(9):1529-36. [PMID: 18852508] 

Functional Description

 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. 

Sequence Annotation

 NP_BIND 114 116 Thiamine pyrophosphate.
 ACT_SITE 411 411 Proton donor (Probable).
 METAL 155 155 Magnesium.
 METAL 185 185 Magnesium.
 METAL 187 187 Magnesium; via carbonyl oxygen.
 BINDING 26 26 Substrate.
 BINDING 66 66 Thiamine pyrophosphate.
 BINDING 156 156 Thiamine pyrophosphate; via amide
 BINDING 185 185 Thiamine pyrophosphate.
 BINDING 261 261 Substrate.
 BINDING 261 261 Thiamine pyrophosphate.
 BINDING 358 358 Substrate.
 BINDING 385 385 Substrate.
 BINDING 437 437 Thiamine pyrophosphate.
 BINDING 461 461 Substrate.
 BINDING 469 469 Substrate.
 BINDING 473 473 Substrate.
 BINDING 520 520 Substrate.
 MOD_RES 46 46 N6-acetyllysine.  

Keyword

 3D-structure; Acetylation; Calcium; Complete proteome; Magnesium; Metal-binding; Reference proteome; Thiamine pyrophosphate; Transferase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 663 AA 

Protein Sequence

Gene Ontology

 GO:0030145; F:manganese ion binding; IDA:EcoCyc.
 GO:0030976; F:thiamine pyrophosphate binding; IDA:EcoCyc.
 GO:0004802; F:transketolase activity; IDA:EcoCyc.
 GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IMP:EcoCyc. 

Interpro

 IPR009014; Transketo_C/Pyr-ferredox_oxred.
 IPR015941; Transketolase-like_C.
 IPR005475; Transketolase-like_Pyr-bd.
 IPR005478; Transketolase_bac-like.
 IPR020826; Transketolase_BS.
 IPR005476; Transketolase_C.
 IPR005474; Transketolase_N. 

Pfam

 PF02779; Transket_pyr
 PF02780; Transketolase_C
 PF00456; Transketolase_N 

SMART

 SM00861; Transket_pyr 

PROSITE

 PS00801; TRANSKETOLASE_1
 PS00802; TRANSKETOLASE_2 

PRINTS