CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-039009
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 S-adenosylmethionine synthase 
Protein Synonyms/Alias
  
Gene Name
 LOC100363915 
Gene Synonyms/Alias
 rCG_56483 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
88KVVREAIKHIGYDDSacetylation[1]
163LAHKLNAKLAELRRNacetylation[1]
234IKAVVPAKYLDEDTIacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405
Functional Description
 Catalyzes the formation of S-adenosylmethionine from methionine and ATP (By similarity). 
Sequence Annotation
  
Keyword
 ATP-binding; Complete proteome; Magnesium; Metal-binding; Nucleotide-binding; One-carbon metabolism; Potassium; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 395 AA 
Protein Sequence
MNGQLNGFHE AFIEEGTFLF TSESVGEGHP DKICDQISDA VLDAHLQQDP DAKVACETVA 60
KTGMILLAGE ITSRAAIDYQ KVVREAIKHI GYDDSSKGFD YKTCNVLVAL EQQSPDIAQG 120
VHLDRNEEDI GAGDQGLMFG YATDETEECM PLTIVLAHKL NAKLAELRRN GTLPWLRPDS 180
KTQVTVQYMQ DRGAVIPIRV HTIVISVQHD EEVCLDEMRD ALKEKVIKAV VPAKYLDEDT 240
IYHLQPSGRF VIGGPQGDAG LTGRKIIVDT YGGWGAHGGG AFSGKDYTKV DRSAAYAARW 300
VAKSLVKGGL CRRVLVQVSY AIGVSHPLSI SIFHYGTSQK SERELLEIVK NNFDLRPGVI 360
VRDLDLKKPI YQRTAAYGHF GRDSFPWEVP KKLKY 395 
Gene Ontology
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004478; F:methionine adenosyltransferase activity; IEA:EC.
 GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
 GO:0006556; P:S-adenosylmethionine biosynthetic process; IEA:UniProtKB-UniPathway. 
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