ID   METK_THEVO              Reviewed;         400 AA.
AC   Q97CT6;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=TV0015;
GN   ORFNames=TVG0012665;
OS   Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS   15438 / GSS1).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX   PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA   Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA   Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA   Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT   "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT   Thermoplasma volcanium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(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; BA000011; BAB59157.1; -; Genomic_DNA.
DR   RefSeq; WP_010916272.1; NC_002689.2.
DR   AlphaFoldDB; Q97CT6; -.
DR   SMR; Q97CT6; -.
DR   STRING; 273116.14324229; -.
DR   EnsemblBacteria; BAB59157; BAB59157; BAB59157.
DR   GeneID; 1441500; -.
DR   KEGG; tvo:TVG0012665; -.
DR   eggNOG; arCOG01678; Archaea.
DR   HOGENOM; CLU_057642_0_0_2; -.
DR   OMA; IGHPDSI; -.
DR   OrthoDB; 21658at2157; -.
DR   PhylomeDB; Q97CT6; -.
DR   UniPathway; UPA00315; UER00080.
DR   Proteomes; UP000001017; 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; -; 1.
DR   Gene3D; 3.30.300.340; -; 1.
DR   HAMAP; MF_00136; S_AdoMet_synth2; 1.
DR   InterPro; IPR042543; AdoMet_synthase_2.
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..400
FT                   /note="S-adenosylmethionine synthase"
FT                   /id="PRO_0000150044"
FT   BINDING         136..141
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00136"
SQ   SEQUENCE   400 AA;  44200 MW;  6C48B8ECCDA1D188 CRC64;
     MERNISVEEL NQIPTPKKEV EIVERKGIGH PDSVADGIAE AVSRSLSKYY LEHYGRILHH
     NTDQVEVVGG QSAPKYGGGL VLEPTYILLS GRATTKVGND RVPYKSITIK AAKDYLRNNF
     SHLDVDADVM IDSRIGQGSV DLVEVYDTSK LEANDTSFGV GFAPLSETEN IVLKTERYLN
     GSLKKKLPMV GYDIKVMGFR QKDTINLTVA AAFVDKYIKD ADEYFNLKDQ LKDLVLDNAV
     EETDKEVKVY INTADIRENS KSVGYLTVTG MSMENGDDGS VGRGNRVNGL ITPYRAMSME
     AAAGKNPVTH VGKLYNVLAN KIANDIVQEE GNDIAEVLVR IVSQIGRPID DPHVASVQVI
     YEGNVDHSKH KNNIRNLVND RLAHVSDLTM QFVEGKITVF