ID   METK_ASCIM              Reviewed;         393 AA.
AC   P50304;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=S-adenosylmethionine synthase;
DE            Short=AdoMet synthase;
DE            EC=2.5.1.6 {ECO:0000250|UniProtKB:O60198};
DE   AltName: Full=Methionine adenosyltransferase;
DE            Short=MAT;
OS   Ascobolus immersus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Ascobolaceae; Ascobolus.
OX   NCBI_TaxID=5191;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=RN42;
RX   PubMed=8621082; DOI=10.1016/0378-1119(95)00862-4;
RA   Mautino M.R., Goyon C., Rosa A.L.;
RT   "Cloning and sequence of the Ascobolus immersus S-adenosyl-L-methionine
RT   synthetase-encoding gene.";
RL   Gene 170:155-156(1996).
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:O60198}.
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:0000250|UniProtKB:O60198};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P13444};
CC       Note=Binds 2 magnesium ions per subunit. The magnesium ions interact
CC       primarily with the substrate. {ECO:0000250|UniProtKB:P13444};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000250|UniProtKB:P13444};
CC       Note=Binds 1 potassium ion per subunit. The potassium ion interacts
CC       primarily with the substrate. {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:O60198}.
CC   -!- SIMILARITY: Belongs to the AdoMet synthase family. {ECO:0000305}.
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DR   EMBL; U21548; AAB03805.1; -; Genomic_DNA.
DR   AlphaFoldDB; P50304; -.
DR   SMR; P50304; -.
DR   PRIDE; P50304; -.
DR   UniPathway; UPA00315; UER00080.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004478; F:methionine adenosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IEA:UniProtKB-UniPathway.
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   PANTHER; PTHR11964; PTHR11964; 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; SSF55973; 3.
DR   TIGRFAMs; TIGR01034; metK; 1.
DR   PROSITE; PS00376; ADOMET_SYNTHASE_1; 1.
DR   PROSITE; PS00377; ADOMET_SYNTHASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW   One-carbon metabolism; Potassium; Transferase.
FT   CHAIN           1..393
FT                   /note="S-adenosylmethionine synthase"
FT                   /id="PRO_0000174448"
FT   BINDING         19
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P13444"
FT   BINDING         25
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         53
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250|UniProtKB:P0A817"
FT   BINDING         66
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         109
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         175..177
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         243..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         254
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         254
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         260..261
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         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:P0A817"
FT   BINDING         281
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         285
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         285
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;  43010 MW;  88FB2F2F14B751C3 CRC64;
     MSIPVNPNSF KGSFLFTSES VGEGHPDKIA DQVSDAVLDA CLAEDPLSKV ACETATKTGM
     IMVFGEITTK AHLDYQKIIR NAVKDIGYDD SAKGFDYKTC NVLVAIEQQS PDIAQGLHYE
     KALEELGAGD QGIMFGYATD ETPELLPLTL LLAHQLNANM AKARRDGSLP WLRPDTKTQV
     TIEYEHDGGA VVPKKVKTVV VSAQHSEDIT TEELRKEILE KIIKTTIPAK YLDEDTVFHI
     QPSGLFIIGG PQGDAGLTGR KIIVDTYGGW GAHGGGAFSG KDYSKVDRSA AYLARWIAKS
     LVTAGLVRRC LVQLSYAIGV AEPLSIFVED YGTSAEGRTS DQLVEIIRKN FDMRPGVIVQ
     ELDLAKPIYF QTAKNGHFTN QEFAWEKPKK LNL