Mat1a
entrez
11720
canonical
uniprot
Q91X83
canonical
ensembl
ENSMUSG00000037798
resolver
ensp
ENSMUSP00000044288
resolver
ensp
ENSMUSP00000153488
resolver
ensp
ENSMUSP00000262669
resolver
enst
ENSMUST00000047286
resolver
enst
ENSMUST00000225720
resolver
genesymbol
Mat1a
resolver
uniprot_entry
METK1_MOUSE
resolver
amino_acid_sequence
MNGPVDGLCDHSLSEEGAFMFTSESVGEGHPDKICDQISDAVLDAHLKQDPNAKVACETVCKTGMVLLCGEITSVAMVDYQRVVRDTIKHIGYDDSAKGFDFKTCNVLVALEQQSPDIAQCVHLDRNEEDVGAGDQGLMFGYATDETEECMPLTIVLAHKLNTRIADLRRSGVLPWLRPDSKTQVTVQYMQDNGAVIPVRIHTIVISVQHNEDITLEAMQEALKEQVIKAVVPAKYLDEDTVYHLQPSGRFVIGGPQGDAGVTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARWVAKSLVKAGLCRRVLVQVSYAIGVAEPLSISIFTYGTSNKTERELLEVVNKNFDLRPGVIVRDLDLKKPIYQKTACYGHFGRSEFPWEVPKKLVF
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:8314764}.
uniprot
proteins
mass_dalton
43509
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:8314764}.
uniprot
proteins
post_translational_modification
PTM: S-nitrosylation of Cys-121 inactivates the enzyme. {ECO:0000250|UniProtKB:P13444}.; PTM: An intrachain disulfide bond can be formed. The protein structure shows that the relevant Cys residues are in a position that would permit formation of a disulfide bond. {ECO:0000250|UniProtKB:P13444}.
uniprot
proteins
protein_family
AdoMet synthase family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
8314764
uniprot
proteins
sequence_length
396
uniprot
proteins