ID   METK_METMI              Reviewed;         405 AA.
AC   P0CW62; Q9HHD2;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 31.
DE   RecName: Full=S-adenosylmethionine synthase {ECO:0000255|HAMAP-Rule:MF_00136};
DE            Short=AdoMet synthase {ECO:0000255|HAMAP-Rule:MF_00136};
DE            EC=2.5.1.6 {ECO:0000255|HAMAP-Rule:MF_00136};
DE   AltName: Full=Methionine adenosyltransferase {ECO:0000255|HAMAP-Rule:MF_00136};
GN   Name=mat {ECO:0000255|HAMAP-Rule:MF_00136};
OS   Methanococcus maripaludis (Methanococcus deltae).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=39152;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43000 / DSM 2067 / JCM 10722 / JJ;
RX   PubMed=10660563; DOI=10.1074/jbc.275.6.4055;
RA   Graham D.E., Bock C.L., Schalk-Hihi C., Lu Z.J., Markham G.D.;
RT   "Identification of a highly diverged class of S-adenosylmethionine
RT   synthetases in the archaea.";
RL   J. Biol. Chem. 275:4055-4059(2000).
CC   -!- FUNCTION: Catalyzes the formation of S-adenosylmethionine from
CC       methionine and ATP. {ECO:0000255|HAMAP-Rule:MF_00136}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-
CC         adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00136};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00136};
CC   -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis;
CC       S-adenosyl-L-methionine from L-methionine: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_00136}.
CC   -!- SIMILARITY: Belongs to the AdoMet synthase 2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00136}.
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DR   EMBL; AF295044; AAG02233.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0CW62; -.
DR   SMR; P0CW62; -.
DR   UniPathway; UPA00315; UER00080.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004478; F:methionine adenosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.300.280; -; 2.
DR   HAMAP; MF_00136; S_AdoMet_synth2; 1.
DR   InterPro; IPR027790; AdoMet_synthase_2_family.
DR   InterPro; IPR042544; AdoMet_synthase_3.
DR   InterPro; IPR002795; S-AdoMet_synthetase_arc.
DR   PANTHER; PTHR36697; PTHR36697; 1.
DR   Pfam; PF01941; AdoMet_Synthase; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Magnesium; Nucleotide-binding; One-carbon metabolism;
KW   Transferase.
FT   CHAIN           1..405
FT                   /note="S-adenosylmethionine synthase"
FT                   /id="PRO_0000150031"
FT   BINDING         141..146
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00136"
SQ   SEQUENCE   405 AA;  44281 MW;  640C792FFA18F55A CRC64;
     MANIVVKRLE RTPIDEIPVE IVERKGIGHP DSICDGIAES VSVALCKMYK EKMGVVLHHN
     TDQVELVGGY AYLELGGGCM VSPIYILLSG RATMEVLDKE TGKIIKLPVN TTAVNAARDY
     LKKALRNMDL EKDVVVDCRI GQGSVDLVEV FDRKRTEIPH ANDTSFGVGH APLSTTEKIV
     LETEKLLNSD ALKAEIPAVG EDIKVMGLRE GKKITLTIAM AAVDKYVNSC ADYVNVKELA
     KAKVEENAKK YLDGHELEVC INTADDDEDC IFLTVTGTSA EMGDDGSVGR GNRANGLITP
     FRPMSMEATS GKNPITHIGK IYNILSNIIA EDVAKIEGVR ECQIRILSQI GKPVTEPKIL
     DIEMIPENGF ELEELSPKAK EVAQKWLDNI SEVTERIVSG NVTTF