CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003303
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cysteine synthase A 
Protein Synonyms/Alias
 CSase A; O-acetylserine (thiol)-lyase A; OAS-TL A; O-acetylserine sulfhydrylase A; S-carboxymethylcysteine synthase; Sulfate starvation-induced protein 5; SSI5 
Gene Name
 cysK 
Gene Synonyms/Alias
 cysZ; b2414; JW2407 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
3*****MSKIFEDNSLacetylation[1]
31GNGRILAKVESRNPSacetylation[1]
42RNPSFSVKCRIGANMacetylation[1]
55NMIWDAEKRGVLKPGacetylation[1]
60AEKRGVLKPGVELVEacetylation[1]
87VAAARGYKLTLTMPEacetylation[1]
105IERRKLLKALGANLVacetylation[1]
118LVLTEGAKGMKGAIQacetylation[1]
121TEGAKGMKGAIQKAEacetylation[1]
126GMKGAIQKAEEIVASacetylation[1, 2]
137IVASNPEKYLLLQQFacetylation[1, 3]
221ALAGEEIKPGPHKIQacetylation[1]
226EIKPGPHKIQGIGAGacetylation[1]
242IPANLDLKLVDKVIGacetylation[1]
246LDLKLVDKVIGITNEacetylation[1]
293EDESFTNKNIVVILPacetylation[1]
319FADLFTEKELQQ***acetylation[1]
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] 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
 REGION 177 181 Pyridoxal phosphate binding (By
 BINDING 8 8 Allosteric inhibitor (By similarity).
 BINDING 72 72 Pyridoxal phosphate (By similarity).
 BINDING 269 269 Allosteric inhibitor; via amide nitrogen
 BINDING 273 273 Pyridoxal phosphate (By similarity).
 MOD_RES 42 42 N6-(pyridoxal phosphate)lysine (By  
Keyword
 Allosteric enzyme; Amino-acid biosynthesis; Complete proteome; Cysteine biosynthesis; Direct protein sequencing; Lyase; Pyridoxal phosphate; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 323 AA 
Protein Sequence
MSKIFEDNSL TIGHTPLVRL NRIGNGRILA KVESRNPSFS VKCRIGANMI WDAEKRGVLK 60
PGVELVEPTS GNTGIALAYV AAARGYKLTL TMPETMSIER RKLLKALGAN LVLTEGAKGM 120
KGAIQKAEEI VASNPEKYLL LQQFSNPANP EIHEKTTGPE IWEDTDGQVD VFIAGVGTGG 180
TLTGVSRYIK GTKGKTDLIS VAVEPTDSPV IAQALAGEEI KPGPHKIQGI GAGFIPANLD 240
LKLVDKVIGI TNEEAISTAR RLMEEEGILA GISSGAAVAA ALKLQEDESF TNKNIVVILP 300
SSGERYLSTA LFADLFTEKE LQQ 323 
Gene Ontology
 GO:0009333; C:cysteine synthase complex; IDA:EcoCyc.
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0004124; F:cysteine synthase activity; IDA:EcoCyc.
 GO:0080146; F:L-cysteine desulfhydrase activity; IMP:EcoCyc.
 GO:0050272; F:S-carboxymethylcysteine synthase activity; IEA:EC.
 GO:0016740; F:transferase activity; IDA:EcoliWiki.
 GO:0006535; P:cysteine biosynthetic process from serine; IDA:EcoCyc. 
Interpro
 IPR001216; Cys_synth_BS.
 IPR005856; Cys_synthKM.
 IPR005859; CysK.
 IPR001926; Trp_syn_b_sub_like_PLP_eny_SF. 
Pfam
 PF00291; PALP 
SMART
  
PROSITE
 PS00901; CYS_SYNTHASE 
PRINTS