ID   METK1_PETHY             Reviewed;         390 AA.
AC   P48498;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   02-SEP-2026, entry version 102.
DE   RecName: Full=S-adenosylmethionine synthase 1;
DE            Short=AdoMet synthase 1;
DE            EC=2.5.1.6 {ECO:0000250|UniProtKB:Q96551};
DE   AltName: Full=Methionine adenosyltransferase 1;
DE            Short=MAT 1;
GN   Name=SAM1;
OS   Petunia hybrida (Petunia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX   NCBI_TaxID=4102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Violet 26; TISSUE=Corolla;
RX   PubMed=7610179; DOI=10.1104/pp.108.2.841;
RA   Izhaki A., Shoseyov O., Weiss D.;
RT   "A petunia cDNA encoding S-adenosylmethionine synthetase.";
RL   Plant Physiol. 108:841-842(1995).
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   -!- SIMILARITY: Belongs to the AdoMet synthase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X82214; CAA57696.1; -; mRNA.
DR   PIR; S49491; S49491.
DR   AlphaFoldDB; P48498; -.
DR   SMR; P48498; -.
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; ISS: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: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; Transferase.
FT   CHAIN           1..390
FT                   /note="S-adenosylmethionine synthase 1"
FT                   /id="PRO_0000174476"
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   390 AA;  42765 MW;  F449DBE8E9F6605B CRC64;
     METFLFTSES VNEGHPDKLC DQVSDAILDA CLEQDPESKV ACETCTKTNM VMVFGEITTK
     ATVDYEKIVR DTCRGIGFTS ADVGLDADHC KVLVNIEQQS PDIAQGVHGH LTKKPEEIGA
     GDQGHMFGYA TDETPELMPL THVWATKLGA KLTEVRKNKT CPWLRPDGKT QVTVEYRNDN
     GAMIPLRVHT ILISTQHDET VTNDQIAQDL KEHVIKPVVP AEYLDENTIF HLNPSGRFVI
     GGPHGDAGLT GRKIIIDTYG GWGAHGGGAF SGKDPTKVDR SGAYIVRQAA KSVVASGLAR
     RCIVQVSYAI GVAEPLSVFV DTYKTGTIPD KDILTLIKEN FDFRPGMMSI NLDLLRGGNF
     RYQKTAAYGH FGRDDPDFTW ETVKVLNPQA
//