ID   METK2_SOLLC             Reviewed;         393 AA.
AC   P43281;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   04-NOV-2026, entry version 137.
DE   RecName: Full=S-adenosylmethionine synthase 2;
DE            Short=AdoMet synthase 2;
DE            EC=2.5.1.6 {ECO:0000250|UniProtKB:Q96551};
DE   AltName: Full=Methionine adenosyltransferase 2;
DE            Short=MAT 2;
GN   Name=SAM2;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=cv. Rutgers; TISSUE=Seedling;
RX   PubMed=8018871; DOI=10.1007/bf00023239;
RA   Espartero J., Pintor-Toro J.A., Pardo J.M.;
RT   "Differential accumulation of S-adenosylmethionine synthetase transcripts
RT   in response to salt stress.";
RL   Plant Mol. Biol. 25:217-227(1994).
CC   -!- FUNCTION: Catalyzes the formation of S-adenosylmethionine from
CC       methionine and ATP. The reaction comprises two steps that are both
CC       catalyzed by the same enzyme: formation of S-adenosylmethionine
CC       (AdoMet) and triphosphate, and subsequent hydrolysis of the
CC       triphosphate. {ECO:0000250|UniProtKB:Q96551}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-methionine + ATP + H2O = S-adenosyl-L-methionine + phosphate
CC         + diphosphate; 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:0000250|UniProtKB:Q96551};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q96551};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q96551};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000250|UniProtKB:Q96551};
CC       Note=Binds 2 divalent ions per subunit. The metal ions interact
CC       primarily with the substrate (By similarity). Can utilize magnesium,
CC       manganese or cobalt (in vitro) (By similarity).
CC       {ECO:0000250|UniProtKB:P13444, ECO:0000250|UniProtKB:Q96551};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000250|UniProtKB:Q96551};
CC       Note=Binds 1 potassium ion per subunit. The potassium ion interacts
CC       primarily with the substrate (By similarity).
CC       {ECO:0000250|UniProtKB:P13444};
CC   -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis;
CC       S-adenosyl-L-methionine from L-methionine: step 1/1.
CC       {ECO:0000250|UniProtKB:Q96551}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in roots. Also present in stems
CC       and leaves. {ECO:0000269|PubMed:8018871}.
CC   -!- INDUCTION: Repressed in roots by ABA and mannitol.
CC       {ECO:0000269|PubMed:8018871}.
CC   -!- SIMILARITY: Belongs to the AdoMet synthase family. {ECO:0000305}.
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DR   EMBL; Z24742; CAA80866.1; -; Genomic_DNA.
DR   PIR; S46539; S38875.
DR   RefSeq; NP_001296305.1; NM_001309376.1.
DR   AlphaFoldDB; P43281; -.
DR   SMR; P43281; -.
DR   FunCoup; P43281; 2654.
DR   STRING; 4081.P43281; -.
DR   PaxDb; 4081-P43281; -.
DR   GeneID; 101247506; -.
DR   KEGG; sly:101247506; -.
DR   eggNOG; KOG1506; Eukaryota.
DR   HOGENOM; CLU_041802_0_1_1; -.
DR   InParanoid; P43281; -.
DR   OMA; ACDETAN; -.
DR   OrthoDB; 5852090at2759; -.
DR   PhylomeDB; P43281; -.
DR   UniPathway; UPA00315; UER00080.
DR   Proteomes; UP000004994; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004478; F:methionine adenosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IBA:GO_Central.
DR   CDD; cd18079; S-AdoMet_synt; 1.
DR   FunFam; 3.30.300.10:FF:000001; S-adenosylmethionine synthase; 1.
DR   FunFam; 3.30.300.10:FF:000003; S-adenosylmethionine synthase; 1.
DR   FunFam; 3.30.300.10:FF:000004; S-adenosylmethionine synthase; 1.
DR   Gene3D; 3.30.300.10; -; 3.
DR   HAMAP; MF_00086; S_AdoMet_synth1; 1.
DR   InterPro; IPR022631; ADOMET_SYNTHASE_CS.
DR   InterPro; IPR022630; S-AdoMet_synt_C.
DR   InterPro; IPR022629; S-AdoMet_synt_central.
DR   InterPro; IPR022628; S-AdoMet_synt_N.
DR   InterPro; IPR002133; S-AdoMet_synthetase.
DR   InterPro; IPR022636; S-AdoMet_synthetase_sfam.
DR   NCBIfam; TIGR01034; metK; 1.
DR   PANTHER; PTHR11964; S-ADENOSYLMETHIONINE SYNTHETASE; 1.
DR   Pfam; PF02773; S-AdoMet_synt_C; 1.
DR   Pfam; PF02772; S-AdoMet_synt_M; 1.
DR   Pfam; PF00438; S-AdoMet_synt_N; 1.
DR   PIRSF; PIRSF000497; MAT; 1.
DR   SUPFAM; SSF55973; S-adenosylmethionine synthetase; 3.
DR   PROSITE; PS00376; ADOMET_SYNTHASE_1; 1.
DR   PROSITE; PS00377; ADOMET_SYNTHASE_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cobalt; Cytoplasm; Magnesium; Metal-binding;
KW   Nucleotide-binding; One-carbon metabolism; Potassium; Reference proteome;
KW   Transferase.
FT   CHAIN           1..393
FT                   /note="S-adenosylmethionine synthase 2"
FT                   /id="PRO_0000174465"
FT   BINDING         9
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P13444"
FT   BINDING         15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:Q00266"
FT   BINDING         43
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250|UniProtKB:P0A817"
FT   BINDING         56
FT                   /ligand="L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:57844"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P0A817"
FT   BINDING         99
FT                   /ligand="L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:57844"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P0A817"
FT   BINDING         167..169
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:Q00266"
FT   BINDING         235..238
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:Q00266"
FT   BINDING         246
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:Q00266"
FT   BINDING         246
FT                   /ligand="L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:57844"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /evidence="ECO:0000250|UniProtKB:P0A817"
FT   BINDING         252..253
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P0A817"
FT   BINDING         269
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /evidence="ECO:0000250|UniProtKB:P0A817"
FT   BINDING         273
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /evidence="ECO:0000250|UniProtKB:P0A817"
FT   BINDING         277
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /evidence="ECO:0000250|UniProtKB:P13444"
FT   BINDING         277
FT                   /ligand="L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:57844"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P0A817"
SQ   SEQUENCE   393 AA;  43082 MW;  4E77D0D1B21BFD79 CRC64;
     METFLFTSES VNEGHPDKLC DQVSDAVLDA CLAQDPESKV ACETCTKTNL VMVFGEITTK
     ANIDYEKIVR DTCREIGFVS PDVGLDADNC RVLVNIEQQS PDIAQGVHGH LTKRPEEIGA
     GDQGHMFGYA TDETPELMPL SHVLATKLGA RLTEVRKNGT CSWLRPDGKT QVTVEYHNDN
     GAMVPLRVHT VLISTQHDET VTNDEIARDL KEHVIKPVIP EKYLDENTIF HLNPSGRFVI
     GGPHGDAGLT GRKIIIDTYG GWGAHGGGAF SGKDPTKVDR SGAYIVRQAA KSIVANGLAR
     RCIVQVSYAI GVPEPLSVFV DTYGTGKIPD KEILNIVKEN FDFRPGMISI NLDLLRGGNG
     RFLKTAAYGH FGRDDPDFTW EVVKPLKWDK PEA
//