UniProt Accession

 TKT2_ECOLI; P33570 

Genbank Protein ID

 D12473; U00096; AP009048 

Genbank Nucleotide ID

 BAA02039.1; AAC75518.1; BAA16340.1 

Protein Name

 Transketolase 2 

Protein Synonyms/Alias

 TK 2 

Gene Name

 tktB 

Gene Synonyms/Alias

 b2465; JW2449 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
224	GHDPQAVKEAILEAQ	acetylation	[1]
236	EAQSVKDKPSLIICR	acetylation	[1, 2]
256	GSPNKAGKEEAHGAP	acetylation	[1]
275	EVALARQKLGWHHPP	acetylation	[1, 2]
287	HPPFEIPKEIYHAWD	acetylation	[1]
301	DAREKGEKAQQSWNE	acetylation	[1]
309	AQQSWNEKFAAYKKA	acetylation	[1]
314	NEKFAAYKKAHPQLA	acetylation	[1]
315	EKFAAYKKAHPQLAE	acetylation	[1]
334	RMSGGLPKDWEKTTQ	acetylation	[1]
338	GLPKDWEKTTQKYIN	acetylation	[1]
342	DWEKTTQKYINELQA	acetylation	[1, 2, 3]
353	ELQANPAKIATRKAS	acetylation	[1]
396	WKGSVSLKEDPAGNY	acetylation	[1]
533	ERTPDQVKEIARGGY	acetylation	[1, 2]
625	WYKYVGLKGAIVGMT	acetylation	[1, 2]
657	TAENIVAKAHKVLGV	acetylation	[1]
660	NIVAKAHKVLGVKGA	acetylation	[2]

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] 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]
 [3] 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] 

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 (By similarity). 

Sequence Annotation

 NP_BIND 113 115 Thiamine pyrophosphate (By similarity).
 ACT_SITE 410 410 Proton donor (By similarity).
 METAL 154 154 Magnesium (By similarity).
 METAL 184 184 Magnesium (By similarity).
 METAL 186 186 Magnesium; via carbonyl oxygen (By
 BINDING 25 25 Substrate (By similarity).
 BINDING 65 65 Thiamine pyrophosphate (By similarity).
 BINDING 155 155 Thiamine pyrophosphate; via amide
 BINDING 184 184 Thiamine pyrophosphate (By similarity).
 BINDING 260 260 Substrate (By similarity).
 BINDING 260 260 Thiamine pyrophosphate (By similarity).
 BINDING 357 357 Substrate (By similarity).
 BINDING 384 384 Substrate (By similarity).
 BINDING 436 436 Thiamine pyrophosphate (By similarity).
 BINDING 460 460 Substrate (By similarity).
 BINDING 468 468 Substrate (By similarity).
 BINDING 519 519 Substrate (By similarity).
 MOD_RES 342 342 N6-acetyllysine.  

Keyword

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

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 667 AA 

Protein Sequence

Gene Ontology

 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004802; F:transketolase activity; IMP:EcoliWiki.
 GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IGI: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