CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007745
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Transketolase 
Protein Synonyms/Alias
 TK 
Gene Name
 tkt 
Gene Synonyms/Alias
 tktA; BSU17890 
Created Date
 July 27, 2013 
Organism
 Bacillus subtilis (strain 168) 
NCBI Taxa ID
 224308 
Lysine Modification
Position
Peptide
Type
References
268VHGAPLGKEESKLTKacetylation[1]
275KEESKLTKEAYAWTYacetylation[1]
339AIKGELPKDWDQEVPacetylation[1]
Reference
 [1] The acetylproteome of Gram-positive model bacterium Bacillus subtilis.
 Kim D, Yu BJ, Kim JA, Lee YJ, Choi SG, Kang S, Pan JG.
 Proteomics. 2013 May;13(10-11):1726-36. [PMID: 23468065
Functional Description
 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 115 117 Thiamine pyrophosphate (By similarity).
 ACT_SITE 411 411 Proton donor (By similarity).
 METAL 156 156 Magnesium (By similarity).
 METAL 186 186 Magnesium (By similarity).
 METAL 188 188 Magnesium; via carbonyl oxygen (By
 BINDING 27 27 Substrate (By similarity).
 BINDING 67 67 Thiamine pyrophosphate (By similarity).
 BINDING 157 157 Thiamine pyrophosphate; via amide
 BINDING 186 186 Thiamine pyrophosphate (By similarity).
 BINDING 262 262 Substrate (By similarity).
 BINDING 262 262 Thiamine pyrophosphate (By similarity).
 BINDING 357 357 Substrate (By similarity).
 BINDING 384 384 Substrate (By similarity).
 BINDING 437 437 Thiamine pyrophosphate (By similarity).
 BINDING 461 461 Substrate (By similarity).
 BINDING 469 469 Substrate (By similarity).
 BINDING 520 520 Substrate (By similarity).  
Keyword
 Calcium; Complete proteome; Magnesium; Metal-binding; Reference proteome; Thiamine pyrophosphate; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 667 AA 
Protein Sequence
MDTIEKKSVA TIRTLSIDAI EKANSGHPGM PMGAAPMAYT LWTKFMNVSP ANPGWFNRDR 60
FVLSAGHGSA LLYSMLHLSG FDLSIEDLKG FRQWGSKTPG HPEFGHTAGV DATTGPLGQG 120
IAMAVGMAIA ERHLAETYNR DSFNVVDHYT YSICGDGDLM EGISSEAASL AGHLQLGRLI 180
VLYDSNDISL DGDLDRSFSE NVKQRFEAMN WEVLYVEDGN NIEELTAAIE KARQNEKKPT 240
LIEVKTTIGF GSPNRAGTSG VHGAPLGKEE SKLTKEAYAW TYEEDFYVPS EVYEHFAVAV 300
KESGEKKEQE WNAQFAKYKE VYPELAEQLE LAIKGELPKD WDQEVPVYEK GSSLASRASS 360
GEVLNGLAKK IPFFVGGSAD LAGSNKTTIK NAGDFTAVDY SGKNFWFGVR EFAMGAALNG 420
MALHGGLRVF GGTFFVFSDY LRPAIRLAAL MGLPVTYVFT HDSIAVGEDG PTHEPVEQLA 480
SLRAMPNLSL IRPADGNETA AAWKLAVQST DHPTALVLTR QNLPTIDQTS EEALAGVEKG 540
AYVVSKSKNE TPDALLIASG SEVGLAIEAQ AELAKENIDV SVVSMPSMDR FEKQSDEYKN 600
EVLPADVKKR LAIEMGSSFG WGKYTGLEGD VLGIDRFGAS APGETIINEY GFSVPNVVNR 660
VKALINK 667 
Gene Ontology
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004802; F:transketolase activity; IEA:EC. 
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