CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003298
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Citrate synthase 
Protein Synonyms/Alias
  
Gene Name
 gltA 
Gene Synonyms/Alias
 gluT; icdB; b0720; JW0710 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
7*MADTKAKLTLNGDTacetylation[1]
38DIRTLGSKGVFTFDPacetylation[1, 2]
56STASCESKITFIDGDacetylation[2]
105QEQYDEFKTTVTRHTacetylation[1]
168AAFRLLSKMPTMAAMacetylation[1]
283LEEISSVKHIPEFVRacetylation[1, 2, 3, 4]
295FVRRAKDKNDSFRLMacetylation[1, 2]
310GFGHRVYKNYDPRATacetylation[1, 2]
328ETCHEVLKELGTKDDacetylation[1]
356NDPYFIEKKLYPNVDacetylation[2, 4]
405EMHSDGMKIARPRQLacetylation[1, 2]
418QLYTGYEKRDFKSDIacetylation[1]
422GYEKRDFKSDIKR**acetylation[1, 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]
 [4] 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
  
Sequence Annotation
 ACT_SITE 306 306 By similarity.
 ACT_SITE 363 363 By similarity.
 MOD_RES 283 283 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Allosteric enzyme; Complete proteome; Direct protein sequencing; Reference proteome; Transferase; Tricarboxylic acid cycle. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 427 AA 
Protein Sequence
MADTKAKLTL NGDTAVELDV LKGTLGQDVI DIRTLGSKGV FTFDPGFTST ASCESKITFI 60
DGDEGILLHR GFPIDQLATD SNYLEVCYIL LNGEKPTQEQ YDEFKTTVTR HTMIHEQITR 120
LFHAFRRDSH PMAVMCGITG ALAAFYHDSL DVNNPRHREI AAFRLLSKMP TMAAMCYKYS 180
IGQPFVYPRN DLSYAGNFLN MMFSTPCEPY EVNPILERAM DRILILHADH EQNASTSTVR 240
TAGSSGANPF ACIAAGIASL WGPAHGGANE AALKMLEEIS SVKHIPEFVR RAKDKNDSFR 300
LMGFGHRVYK NYDPRATVMR ETCHEVLKEL GTKDDLLEVA MELENIALND PYFIEKKLYP 360
NVDFYSGIIL KAMGIPSSMF TVIFAMARTV GWIAHWSEMH SDGMKIARPR QLYTGYEKRD 420
FKSDIKR 427 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0004108; F:citrate (Si)-synthase activity; IEA:EC.
 GO:0044262; P:cellular carbohydrate metabolic process; IEA:InterPro.
 GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway. 
Interpro
 IPR016142; Citrate_synth-like_lrg_a-sub.
 IPR016143; Citrate_synth-like_sm_a-sub.
 IPR002020; Citrate_synthase-like.
 IPR016141; Citrate_synthase-like_core.
 IPR019810; Citrate_synthase_AS.
 IPR024176; Citrate_synthase_bac-typ.
 IPR010953; Citrate_synthase_typ-II. 
Pfam
 PF00285; Citrate_synt 
SMART
  
PROSITE
 PS00480; CITRATE_SYNTHASE 
PRINTS
 PR00143; CITRTSNTHASE.