ID   METK_HALSA              Reviewed;         408 AA.
AC   Q9HQ73;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=VNG_1297C;
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=64091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX   PubMed=11016950; DOI=10.1073/pnas.190337797;
RA   Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA   Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA   Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA   Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA   Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA   Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA   Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA   DasSarma S.;
RT   "Genome sequence of Halobacterium species NRC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(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; AE004437; AAG19644.1; -; Genomic_DNA.
DR   PIR; H84284; H84284.
DR   RefSeq; WP_010902940.1; NC_002607.1.
DR   AlphaFoldDB; Q9HQ73; -.
DR   SMR; Q9HQ73; -.
DR   STRING; 64091.VNG_1297C; -.
DR   PaxDb; Q9HQ73; -.
DR   EnsemblBacteria; AAG19644; AAG19644; VNG_1297C.
DR   GeneID; 5953678; -.
DR   GeneID; 62886783; -.
DR   KEGG; hal:VNG_1297C; -.
DR   PATRIC; fig|64091.14.peg.992; -.
DR   HOGENOM; CLU_057642_0_0_2; -.
DR   InParanoid; Q9HQ73; -.
DR   OMA; IGHPDSI; -.
DR   OrthoDB; 21658at2157; -.
DR   PhylomeDB; Q9HQ73; -.
DR   UniPathway; UPA00315; UER00080.
DR   Proteomes; UP000000554; 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..408
FT                   /note="S-adenosylmethionine synthase"
FT                   /id="PRO_0000150026"
FT   BINDING         142..147
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00136"
SQ   SEQUENCE   408 AA;  44115 MW;  E13DB86341E33270 CRC64;
     MTDRNIQVQS LDRSAVEDDA VEIVERKGLG HPDSICDGIA EHVCETLARE YRDRVGHVLH
     FNTDETQLVA GDAAPAFGGG NVIDPIYILV VGRATSHYVE ADGTEHHIPV ESIALEAARE
     YLRETLPHLD LETDVIVDVK LGEGSGDLQD VFTDDDDGPA VPMANDTSFG VGHAPLTETE
     RIVLEAERSL NGPYAEHTPA VGEDVKVMGK REDDHIDLTI AAALVDAHVP DMDAYIAQVE
     AIREHVFDLA TEHTDREVTV HVNTADDYES GSIYLTTTGT SAEQGDDGSV GRGNRANGLI
     TPNRAMSMEA TSGKNPVNHI GKIYNLLSTQ IAEAVVAEVD GIRDLRVRLL SQIGRPIDEP
     HVADVEVVTE DGTAVADVDA EIERIVDAQL ASVTDLTRRV IDGERTTF