CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003050
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 S-adenosylmethionine synthase 
Protein Synonyms/Alias
 AdoMet synthase; MAT; Methionine adenosyltransferase 
Gene Name
 metK 
Gene Synonyms/Alias
 metX; b2942; JW2909 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
3*****MAKHLFTSESacetylation[1, 2]
37AILEQDPKARVACETacetylation[3]
166PWLRPDAKSQVTFQYacetylation[3]
209AVMEEIIKPILPAEWacetylation[3]
246DCGLTGRKIIVDTYGacetylation[3]
266GGGAFSGKDPSKVDRacetylation[3]
270FSGKDPSKVDRSAAYacetylation[3]
284YAARYVAKNIVAAGLacetylation[3]
370REHFPWEKTDKAQLLacetylation[3]
373FPWEKTDKAQLLRDAacetylation[3]
Reference
 [1] 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]
 [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] 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 S-adenosylmethionine from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. Is essential for growth. 
Sequence Annotation
 NP_BIND 260 267 ATP (Potential).
 REGION 239 248 Pyrophosphate binding.
 METAL 17 17 Magnesium.
 METAL 43 43 Potassium.
 METAL 264 264 Potassium.
 METAL 272 272 Magnesium.
 BINDING 119 119 Methionine.
 BINDING 239 239 Methionine.
 MOD_RES 3 3 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; ATP-binding; Cobalt; Complete proteome; Cytoplasm; Magnesium; Metal-binding; Nucleotide-binding; One-carbon metabolism; Potassium; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 384 AA 
Protein Sequence
MAKHLFTSES VSEGHPDKIA DQISDAVLDA ILEQDPKARV ACETYVKTGM VLVGGEITTS 60
AWVDIEEITR NTVREIGYVH SDMGFDANSC AVLSAIGKQS PDINQGVDRA DPLEQGAGDQ 120
GLMFGYATNE TDVLMPAPIT YAHRLVQRQA EVRKNGTLPW LRPDAKSQVT FQYDDGKIVG 180
IDAVVLSTQH SEEIDQKSLQ EAVMEEIIKP ILPAEWLTSA TKFFINPTGR FVIGGPMGDC 240
GLTGRKIIVD TYGGMARHGG GAFSGKDPSK VDRSAAYAAR YVAKNIVAAG LADRCEIQVS 300
YAIGVAEPTS IMVETFGTEK VPSEQLTLLV REFFDLRPYG LIQMLDLLHP IYKETAAYGH 360
FGREHFPWEK TDKAQLLRDA AGLK 384 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:HAMAP.
 GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
 GO:0004478; F:methionine adenosyltransferase activity; IDA:EcoCyc.
 GO:0030955; F:potassium ion binding; IDA:EcoCyc.
 GO:0006730; P:one-carbon metabolic process; IEA:HAMAP.
 GO:0006556; P:S-adenosylmethionine biosynthetic process; IMP:EcoCyc. 
Interpro
 IPR022631; ADOMET_SYNTHASE_CS.
 IPR022630; S-AdoMet_synt_C.
 IPR022629; S-AdoMet_synt_central.
 IPR022628; S-AdoMet_synt_N.
 IPR002133; S-AdoMet_synthetase.
 IPR022636; S-AdoMet_synthetase_sfam. 
Pfam
 PF02773; S-AdoMet_synt_C
 PF02772; S-AdoMet_synt_M
 PF00438; S-AdoMet_synt_N 
SMART
  
PROSITE
 PS00376; ADOMET_SYNTHASE_1
 PS00377; ADOMET_SYNTHASE_2 
PRINTS