ID   METK_METS3              Reviewed;         401 AA.
AC   A5UMW7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 64.
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}; OrderedLocusNames=Msm_1340;
OS   Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=420247;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX   PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA   Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA   Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT   "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT   human gut.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
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; CP000678; ABQ87545.1; -; Genomic_DNA.
DR   RefSeq; WP_004032572.1; NC_009515.1.
DR   AlphaFoldDB; A5UMW7; -.
DR   SMR; A5UMW7; -.
DR   STRING; 420247.Msm_1340; -.
DR   EnsemblBacteria; ABQ87545; ABQ87545; Msm_1340.
DR   GeneID; 5217247; -.
DR   KEGG; msi:Msm_1340; -.
DR   PATRIC; fig|420247.28.peg.1335; -.
DR   eggNOG; arCOG01678; Archaea.
DR   HOGENOM; CLU_057642_0_0_2; -.
DR   OMA; IGHPDSI; -.
DR   UniPathway; UPA00315; UER00080.
DR   Proteomes; UP000001992; Chromosome.
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..401
FT                   /note="S-adenosylmethionine synthase"
FT                   /id="PRO_1000196739"
FT   BINDING         135..140
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00136"
SQ   SEQUENCE   401 AA;  43784 MW;  CFC996B960F95AF6 CRC64;
     MRNIIVKELN QTYIEDIDIE IVERKGIGHP DSISDGIGET VSEALCKMYM DELGGVLHHN
     TDEVQITAGE SNPVFGGGKI LKPIDILLTG RGVSEYDGIK FPLDRVAIEA AKNFLDDTII
     NLDVELDTVV ECKIGHGSGD LVDVFKREGA PSSNDTSFGV GYAPFSETET LVKATEELLN
     SKPFKAKHPA VGEDIKVMGL REGEKITLTI GCAMVSKFVA NREEYIAVRE ELKDIVSDLA
     TKYTNREVEV FVNTADNDDA TDESGYYLTV TGTSAEMGDD GSVGRGNRAN GLITPCRPMS
     MEASSGKNPI NHVGKIYNIL SNEIAKDVVE NVEGIKQMNV MILSQIGKPI DQPKAASTQV
     ILEDGVKLED VDKKVEQIVD RWLEDISIIT ENVVQGKTRT F