ID   METK1_CATRO             Reviewed;         393 AA.
AC   Q96551;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   02-SEP-2026, entry version 108.
DE   RecName: Full=S-adenosylmethionine synthase 1;
DE            Short=AdoMet synthase 1;
DE            EC=2.5.1.6 {ECO:0000269|PubMed:9037140};
DE   AltName: Full=Methionine adenosyltransferase 1;
DE            Short=MAT 1;
GN   Name=SAMS1;
OS   Catharanthus roseus (Madagascar periwinkle) (Vinca rosea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae; Vinceae;
OC   Catharanthinae; Catharanthus.
OX   NCBI_TaxID=4058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP   BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, PATHWAY, TISSUE
RP   SPECIFICITY, AND INDUCTION.
RX   PubMed=9037140; DOI=10.1023/a:1005711720930;
RA   Schroeder G., Eichel J., Breinig S., Schroeder J.;
RT   "Three differentially expressed S-adenosylmethionine synthetases from
RT   Catharanthus roseus: molecular and functional characterization.";
RL   Plant Mol. Biol. 33:211-222(1997).
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:0000269|PubMed:9037140}.
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:0000269|PubMed:9037140};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:9037140};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:9037140};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000269|PubMed:9037140};
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) (PubMed:9037140).
CC       {ECO:0000250|UniProtKB:P13444, ECO:0000269|PubMed:9037140};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000269|PubMed:9037140};
CC       Name=NH4(+); Xref=ChEBI:CHEBI:28938;
CC         Evidence={ECO:0000269|PubMed:9037140};
CC       Note=Binds 1 potassium ion per subunit. The potassium ion interacts
CC       primarily with the substrate (By similarity). Potassium can be replaced
CC       by NH(4) (in vitro) (PubMed:9037140). {ECO:0000250|UniProtKB:P13444,
CC       ECO:0000269|PubMed:9037140};
CC   -!- ACTIVITY REGULATION: Inhibited by products of SAMS reaction (SAM, Pi,
CC       PPi), substrate analogs (cycloleucine and ethionine), and alternative
CC       nucleotides (GTP, CTP and ADP). Strongly repressed by PPPi.
CC       {ECO:0000269|PubMed:9037140}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=104 uM for L-methionine {ECO:0000269|PubMed:9037140};
CC         KM=252 uM for ATP {ECO:0000269|PubMed:9037140};
CC       pH dependence:
CC         Optimum pH is 7-8.3. {ECO:0000269|PubMed:9037140};
CC       Temperature dependence:
CC         Optimum temperature is 37-45 degrees Celsius.
CC         {ECO:0000269|PubMed:9037140};
CC   -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis;
CC       S-adenosyl-L-methionine from L-methionine: step 1/1.
CC       {ECO:0000269|PubMed:9037140}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in roots, and, to a lower extent,
CC       in hypocotyls and cotyledons. {ECO:0000269|PubMed:9037140}.
CC   -!- INDUCTION: Strongly induced by elicitors from Phytophthora megasperma.
CC       Transiently activated by salt stress,. {ECO:0000269|PubMed:9037140}.
CC   -!- SIMILARITY: Belongs to the AdoMet synthase family. {ECO:0000305}.
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DR   EMBL; Z71271; CAA95856.1; -; mRNA.
DR   AlphaFoldDB; Q96551; -.
DR   SMR; Q96551; -.
DR   BRENDA; 2.5.1.6; 1211.
DR   UniPathway; UPA00315; UER00080.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004478; F:methionine adenosyltransferase activity; EXP:UniProtKB.
DR   GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd18079; S-AdoMet_synt; 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   FunFam; 3.30.300.10:FF:000011; S-adenosylmethionine synthase; 1.
DR   FunFam; 3.30.300.10:FF:000021; S-adenosylmethionine synthetase 1; 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   1: Evidence at protein level;
KW   ATP-binding; Cobalt; Cytoplasm; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; One-carbon metabolism; Potassium; Transferase.
FT   CHAIN           1..393
FT                   /note="S-adenosylmethionine synthase 1"
FT                   /id="PRO_0000174459"
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;  43050 MW;  04371F2B55BE386F CRC64;
     METFLFTSES VNEGHPDKLC DQISDAVLDA CLEQDPDSKV ACETCTKTNM VMVFGEITTK
     ATVDYEKIVR DTCRSIGFVS DDVGLDADNC KVLVNIEQQS PDIAQGVHGH LTKRPEEIGA
     GDQGHMFGYA TDETPEFMPL SHVLATKLGA RLTEVRKNGT CPWLRPDGKT QVTVEYYNEN
     GAMVPVRVHT VVISTQHDET VTNDQIAADL KEHVIKPVIP EKYLDERTIF HLNPSGRFVI
     GGPHGDAGLT GRKIIIDTYG GWGAHGGGAF SGKDPTKVDR SGAYIVRQAA KSIVANGLAR
     RCIVQVSYAI GVPEPLSVFV DTYGTGKIPD KEILKIVKEN FDFRPGMIAI NLDLKRGGSG
     RFLKTAAYGH FGRDDPDFTW EVVKPLKWEK AAN
//