CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001840
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cystathionine gamma-synthase 
Protein Synonyms/Alias
 CGS; O-succinylhomoserine (thiol)-lyase 
Gene Name
 metB 
Gene Synonyms/Alias
 b3939; JW3910 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
113RLFDSLAKRGCYRVLacetylation[1]
137LRAALAEKPKLVLVEacetylation[1]
139AALAEKPKLVLVESPacetylation[1]
158LRVVDIAKICHLAREacetylation[1]
264RNAQAIVKYLQTQPLacetylation[1]
274QTQPLVKKLYHPSLPacetylation[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] 
Functional Description
 Catalyzes the formation of L-cystathionine from O- succinyl-L-homoserine (OSHS) and L-cysteine, via a gamma- replacement reaction. In the absence of thiol, catalyzes gamma- elimination to form 2-oxobutanoate, succinate and ammonia. 
Sequence Annotation
 MOD_RES 198 198 N6-(pyridoxal phosphate)lysine.  
Keyword
 3D-structure; Amino-acid biosynthesis; Complete proteome; Cytoplasm; Direct protein sequencing; Methionine biosynthesis; Pyridoxal phosphate; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 386 AA 
Protein Sequence
MTRKQATIAV RSGLNDDEQY GCVVPPIHLS STYNFTGFNE PRAHDYSRRG NPTRDVVQRA 60
LAELEGGAGA VLTNTGMSAI HLVTTVFLKP GDLLVAPHDC YGGSYRLFDS LAKRGCYRVL 120
FVDQGDEQAL RAALAEKPKL VLVESPSNPL LRVVDIAKIC HLAREVGAVS VVDNTFLSPA 180
LQNPLALGAD LVLHSCTKYL NGHSDVVAGV VIAKDPDVVT ELAWWANNIG VTGGAFDSYL 240
LLRGLRTLVP RMELAQRNAQ AIVKYLQTQP LVKKLYHPSL PENQGHEIAA RQQKGFGAML 300
SFELDGDEQT LRRFLGGLSL FTLAESLGGV ESLISHAATM THAGMAPEAR AAAGISETLL 360
RISTGIEDGE DLIADLENGF RAANKG 386 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0003962; F:cystathionine gamma-synthase activity; IDA:EcoCyc.
 GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc.
 GO:0009086; P:methionine biosynthetic process; IMP:EcoCyc. 
Interpro
 IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
 IPR011821; O_succ_thio_ly.
 IPR015424; PyrdxlP-dep_Trfase.
 IPR015421; PyrdxlP-dep_Trfase_major_sub1.
 IPR015422; PyrdxlP-dep_Trfase_major_sub2. 
Pfam
 PF01053; Cys_Met_Meta_PP 
SMART
  
PROSITE
 PS00868; CYS_MET_METAB_PP 
PRINTS