ID   METK_METTH              Reviewed;         401 AA.
AC   O27429;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=S-adenosylmethionine synthase;
DE            Short=AdoMet synthase;
DE            EC=2.5.1.6;
DE   AltName: Full=Methionine adenosyltransferase;
GN   Name=mat; OrderedLocusNames=MTH_1376;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
CC   -!- FUNCTION: Catalyzes the formation of S-adenosylmethionine from
CC       methionine and ATP. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis;
CC       S-adenosyl-L-methionine from L-methionine: step 1/1.
CC   -!- SIMILARITY: Belongs to the AdoMet synthase 2 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB85853.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000666; AAB85853.1; ALT_INIT; Genomic_DNA.
DR   PIR; A69050; A69050.
DR   RefSeq; WP_048061035.1; NC_000916.1.
DR   AlphaFoldDB; O27429; -.
DR   SMR; O27429; -.
DR   STRING; 187420.MTH_1376; -.
DR   EnsemblBacteria; AAB85853; AAB85853; MTH_1376.
DR   GeneID; 1471093; -.
DR   KEGG; mth:MTH_1376; -.
DR   PATRIC; fig|187420.15.peg.1341; -.
DR   HOGENOM; CLU_057642_0_0_2; -.
DR   OMA; IGHPDSI; -.
DR   UniPathway; UPA00315; UER00080.
DR   Proteomes; UP000005223; 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   Reference proteome; Transferase.
FT   CHAIN           1..401
FT                   /note="S-adenosylmethionine synthase"
FT                   /id="PRO_0000150032"
FT   BINDING         135..140
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   401 AA;  43757 MW;  1907300EC6115466 CRC64;
     MRNIIVEPLN QTPIEDQKVE IVERKGIGHP DSISDGIAES VSRALCNAYL DRFGAIMHHN
     TDEVQITAGE SAPQFGGGEV IKPMEILLTG RGIAEVDGEK IGLDRIAISA AKEYLRENIL
     NLDVETCAVV ECKIGHGSGD LRDVFARKGR APLSNDTSFG VGFAPFSETE RIVMEAENLL
     NSPEFKKKHP AVGEDIKVMG LRENDNITLT VACAMVDRYV SDLEEYLEVK NVVRDEVFKI
     ASKLTDRNLE VFVNTADRCE DDEPSVYITV TGTSAEMGDD GSVGRGNRAN GLITPNRPMS
     MEATSGKNPI NHVGKIYNLL SNQMAGDIVE SVEGVKQVHI MILSQIGKPI DHPKAATAQV
     ILEDGYTMDE VTGKVSGVMD AWLEDIPSIT EMLVKGQLRT F