ID   METK_CALMQ              Reviewed;         408 AA.
AC   A8MD44;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=Cmaq_0865;
OS   Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 /
OS   IC-167).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Caldivirga.
OX   NCBI_TaxID=397948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700844 / DSM 13496 / JCM 10307 / IC-167;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M.,
RA   Saltikov C., House C.H., Richardson P.;
RT   "Complete sequence of Caldivirga maquilingensis IC-167.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000852; ABW01700.1; -; Genomic_DNA.
DR   RefSeq; WP_012185919.1; NC_009954.1.
DR   AlphaFoldDB; A8MD44; -.
DR   SMR; A8MD44; -.
DR   STRING; 397948.Cmaq_0865; -.
DR   EnsemblBacteria; ABW01700; ABW01700; Cmaq_0865.
DR   GeneID; 5708918; -.
DR   KEGG; cma:Cmaq_0865; -.
DR   eggNOG; arCOG01678; Archaea.
DR   HOGENOM; CLU_057642_0_0_2; -.
DR   OMA; IGHPDSI; -.
DR   OrthoDB; 21658at2157; -.
DR   UniPathway; UPA00315; UER00080.
DR   Proteomes; UP000001137; 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   Reference proteome; Transferase.
FT   CHAIN           1..408
FT                   /note="S-adenosylmethionine synthase"
FT                   /id="PRO_1000076442"
FT   BINDING         140..145
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00136"
SQ   SEQUENCE   408 AA;  44934 MW;  73260C8762CF4A53 CRC64;
     MARNIVVSGI RRPPTEDLPV ELVERKGLGH PDYIADSISE YVSRELSKYY MENFGTILHH
     NVDKVLVIGG NAQVKFGGGE IIEPIRIIVS GRATTEVKSS TGVVKVPIGS IILSAARKFI
     IDNFRFLNPD QHLVIDYKVG QGSVDLVGVY ELGVSSGGVP LANDTSIGVG FAPLTVTERL
     VYETERLLNS REFKARYPEV GEDVKVMGLR RGRKITLTVA SALVSRLIKD KDHYISVKED
     VVNAIYDNAV KLANGYEVEV HLNTADNPEH GIYYLTYTGT SAEHGDDGMT GRGNRANGLI
     TPMRPMSMEA TAGKNPVSHI GKIYYVLANM IAKRIHDEVK GTREVYVYLL SQIGKPIDNP
     LIANVEIITN EGEVTSEMKR EAEAITDEEI SRVTRLTSMF VKGEITPF