ID   METK_SULIN              Reviewed;         404 AA.
AC   C3NF87;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 57.
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=YN1551_0861;
OS   Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=419942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y.N.15.51 / Yellowstone #2;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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; CP001404; ACP47983.1; -; Genomic_DNA.
DR   RefSeq; WP_012717247.1; NC_012623.1.
DR   AlphaFoldDB; C3NF87; -.
DR   SMR; C3NF87; -.
DR   EnsemblBacteria; ACP47983; ACP47983; YN1551_0861.
DR   GeneID; 7809543; -.
DR   KEGG; sin:YN1551_0861; -.
DR   HOGENOM; CLU_057642_0_0_2; -.
DR   OMA; IGHPDSI; -.
DR   UniPathway; UPA00315; UER00080.
DR   Proteomes; UP000006818; 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   Transferase.
FT   CHAIN           1..404
FT                   /note="S-adenosylmethionine synthase"
FT                   /id="PRO_1000203218"
FT   BINDING         139..144
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00136"
SQ   SEQUENCE   404 AA;  44683 MW;  60C66B7A9A82BAE7 CRC64;
     MRNINVQLNP LSDIEKLQVE LVERKGLGHP DYIADAVAEE ASRKLSLYYL KKYGVILHHN
     LDKTLVVGGQ ATPRFKGGDV IQPIYIVVAG RATTEVKTES GIEQIPVGTI IIESVKEWIR
     NNFRYLDAEK HLIVDYKIGK GSTDLVGIFE AGKRVPLSND TSFGVGFAPF TKLEKLVYET
     ERHLNSKQFK AKLPEVGEDI KVMGLRRGNE VDLTIAMATI SELIEDVNHY INVKEQAKNK
     ILDLASKIAP DYDVRIYVNT GDKIDKNILY LTVTGTSAEH GDDGMTGRGN RGVGLITPMR
     PMSLEATAGK NPVNHVGKLY NVLANLIANK IAQEVKDVKF SQVQVLGQIG RPIDDPLIAN
     VDVITYDGKL NDETKNEISG IVDEMLSSFN KLTELILEGK ATLF