CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004119
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 S-adenosylmethionine synthase isoform type-1 
Protein Synonyms/Alias
 AdoMet synthase 1; Methionine adenosyltransferase 1; MAT 1; Methionine adenosyltransferase I/III; MAT-I/III 
Gene Name
 Mat1a 
Gene Synonyms/Alias
 Ams1 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
89RVVRDTIKHIGYDDSacetylation[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. 
Sequence Annotation
 NP_BIND 132 137 ATP (Potential).
 METAL 32 32 Magnesium (By similarity).
 METAL 58 58 Potassium (By similarity).
 METAL 284 284 Potassium (By similarity).
 METAL 292 292 Magnesium (By similarity).
 BINDING 30 30 Substrate (By similarity).
 BINDING 160 160 ATP (Potential).
 BINDING 180 180 Substrate (By similarity).
 BINDING 248 248 Substrate (By similarity).
 BINDING 250 250 Substrate; via carbonyl oxygen (By
 BINDING 259 259 Substrate (By similarity).
 MOD_RES 121 121 S-nitrosocysteine.
 DISULFID 35 61  
Keyword
 3D-structure; ATP-binding; Cobalt; Complete proteome; Disulfide bond; Magnesium; Metal-binding; Nucleotide-binding; One-carbon metabolism; Potassium; Reference proteome; S-nitrosylation; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 397 AA 
Protein Sequence
MNGPVDGLCD HSLSEEGAFM FTSESVGEGH PDKICDQISD AVLDAHLKQD PNAKVACETV 60
CKTGMVLLCG EITSMAMIDY QRVVRDTIKH IGYDDSAKGF DFKTCNVLVA LEQQSPDIAQ 120
CVHLDRNEED VGAGDQGLMF GYATDETEEC MPLTIVLAHK LNTRMADLRR SGVLPWLRPD 180
SKTQVTVQYV QDNGAVIPVR VHTIVISVQH NEDITLEAMR EALKEQVIKA VVPAKYLDED 240
TIYHLQPSGR FVIGGPQGDA GVTGRKIIVD TYGGWGAHGG GAFSGKDYTK VDRSAAYAAR 300
WVAKSLVKAG LCRRVLVQVS YAIGVAEPLS ISIFTYGTSK KTERDELLEV VNKNFDLRPG 360
VIVRDLDLKK PIYQKTACYG HFGRSEFPWE VPKKLVF 397 
Gene Ontology
 GO:0005829; C:cytosol; IDA:RGD.
 GO:0016363; C:nuclear matrix; IDA:RGD.
 GO:0043531; F:ADP binding; IDA:RGD.
 GO:0016597; F:amino acid binding; IDA:RGD.
 GO:0005524; F:ATP binding; IDA:RGD.
 GO:0000287; F:magnesium ion binding; IDA:RGD.
 GO:0004478; F:methionine adenosyltransferase activity; IDA:RGD.
 GO:0042803; F:protein homodimerization activity; IDA:RGD.
 GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
 GO:0051289; P:protein homotetramerization; IDA:RGD.
 GO:0006556; P:S-adenosylmethionine biosynthetic process; IDA:RGD. 
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