Mat1a
entrez
25331
canonical
uniprot
P13444
canonical
ensembl
ENSRNOG00000011351
resolver
ensp
ENSRNOP00000015190
resolver
enst
ENSRNOT00000015190
resolver
genesymbol
Mat1a
resolver
genesymbol_syn
Ams1
resolver
uniprot
F1LZ34
resolver
uniprot
Q5FVU2
resolver
uniprot_entry
F1LZ34_RAT
resolver
uniprot_entry
METK1_RAT
resolver
uniprot_sec
Q5FVU2
resolver
amino_acid_sequence
MNGPVDGLCDHSLSEEGAFMFTSESVGEGHPDKICDQISDAVLDAHLKQDPNAKVACETVCKTGMVLLCGEITSMAMIDYQRVVRDTIKHIGYDDSAKGFDFKTCNVLVALEQQSPDIAQCVHLDRNEEDVGAGDQGLMFGYATDETEECMPLTIVLAHKLNTRMADLRRSGVLPWLRPDSKTQVTVQYVQDNGAVIPVRVHTIVISVQHNEDITLEAMREALKEQVIKAVVPAKYLDEDTIYHLQPSGRFVIGGPQGDAGVTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARWVAKSLVKAGLCRRVLVQVSYAIGVAEPLSISIFTYGTSKKTERDELLEVVNKNFDLRPGVIVRDLDLKKPIYQKTACYGHFGRSEFPWEVPKKLVF
uniprot
proteins
ec_number
2.5.1.6
uniprot
proteins
function
FUNCTION: Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate. {ECO:0000269|PubMed:10873471, ECO:0000269|PubMed:1517209, ECO:0000269|PubMed:9755242}.
uniprot
proteins
mass_dalton
43698
uniprot
proteins
mutagenesis
MUTAGEN 180; /note="D->G: Loss of S-adenosylmethionine synthase activity, but does not abolish polyphosphatase activity."; /evidence="ECO:0000269|PubMed:10873471"; MUTAGEN 182; /note="K->G: Loss of S-adenosylmethionine synthase activity, but does not abolish polyphosphatase activity."; /evidence="ECO:0000269|PubMed:10873471"; MUTAGEN 251; /note="F->D,G: Loss of S-adenosylmethionine synthase activity, but does not abolish polyphosphatase activity."; /evidence="ECO:0000269|PubMed:10873471
uniprot
proteins
pathway_participation
PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. {ECO:0000269|PubMed:10873471, ECO:0000269|PubMed:1517209, ECO:0000269|PubMed:9755242}.
uniprot
proteins
post_translational_modification
PTM: S-nitrosylation of Cys-121 inactivates the enzyme. {ECO:0000269|PubMed:10358060, ECO:0000269|PubMed:9755242}.; PTM: An intrachain disulfide bond can be formed (PubMed:10601859). The protein structure shows that the relevant Cys residues are in a position that would permit formation of a disulfide bond (PubMed:10873471). {ECO:0000269|PubMed:10601859, ECO:0000269|PubMed:10873471}.
uniprot
proteins
protein_family
AdoMet synthase family
uniprot
proteins
pubmed
10358060
uniprot
proteins
pubmed
10601859
uniprot
proteins
pubmed
10873471
uniprot
proteins
pubmed
12888348
uniprot
proteins
pubmed
1517209
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1915866
uniprot
proteins
pubmed
2806235
uniprot
proteins
pubmed
9755242
uniprot
proteins
sequence_length
397
uniprot
proteins