ID   METK_ARCFU              Reviewed;         399 AA.
AC   O30186;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=AF_0050;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(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}.
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DR   EMBL; AE000782; AAB91181.1; -; Genomic_DNA.
DR   PIR; B69256; B69256.
DR   RefSeq; WP_010877564.1; NC_000917.1.
DR   AlphaFoldDB; O30186; -.
DR   SMR; O30186; -.
DR   STRING; 224325.AF_0050; -.
DR   EnsemblBacteria; AAB91181; AAB91181; AF_0050.
DR   GeneID; 24793604; -.
DR   KEGG; afu:AF_0050; -.
DR   eggNOG; arCOG01678; Archaea.
DR   HOGENOM; CLU_057642_0_0_2; -.
DR   OMA; IGHPDSI; -.
DR   OrthoDB; 21658at2157; -.
DR   PhylomeDB; O30186; -.
DR   UniPathway; UPA00315; UER00080.
DR   Proteomes; UP000002199; 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   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..399
FT                   /note="S-adenosylmethionine synthase"
FT                   /id="PRO_0000150025"
FT   BINDING         135..140
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   399 AA;  44487 MW;  53CCE147F793841C CRC64;
     MPNIFVEELV HTPIEKQVIE IVERKGIGHP DSLADGMAEA MSRELSREYI RRFGAVLHHN
     TDETQIVAGR SNPQFGGGEV IEPIYVLLVG RATKFFNGEY IPTDKIALKA ARDYIRQHMQ
     NLDPELDVVF NVRLGEGSTD LQDVFRRKSG NVALANDTSF GIGFAPLSET ERLVFNVERR
     IYEEFRKKNP AIGEDVKVMG LREKDRISLT IAAAFVDRYV ANIKEYDAIK EELENFVKEI
     SSEYTEREVE VFVNTADDYE TGCVYLTVTG TSAENGDDGS VGRGNRCNGL ITPGRPMSME
     ASSGKNPINH VGKIYNLLAN QIAARIAEEV EGVEEVYVRI LSQIGKPINE PKALSVQVIP
     KSGYDISKLE RPARDIAEEM IANVGKITDM VIEGKVRTF