METK_SALA4
ID METK_SALA4 Reviewed; 384 AA.
AC B5F5L4;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=S-adenosylmethionine synthase {ECO:0000255|HAMAP-Rule:MF_00086};
DE Short=AdoMet synthase {ECO:0000255|HAMAP-Rule:MF_00086};
DE EC=2.5.1.6 {ECO:0000255|HAMAP-Rule:MF_00086};
DE AltName: Full=MAT {ECO:0000255|HAMAP-Rule:MF_00086};
DE AltName: Full=Methionine adenosyltransferase {ECO:0000255|HAMAP-Rule:MF_00086};
GN Name=metK {ECO:0000255|HAMAP-Rule:MF_00086}; OrderedLocusNames=SeAg_B3252;
OS Salmonella agona (strain SL483).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=454166;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL483;
RX PubMed=21602358; DOI=10.1128/jb.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(2011).
CC -!- FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from
CC methionine and ATP. The overall synthetic reaction is composed of two
CC sequential steps, AdoMet formation and the subsequent tripolyphosphate
CC hydrolysis which occurs prior to release of AdoMet from the enzyme.
CC {ECO:0000255|HAMAP-Rule:MF_00086}.
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_00086};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00086};
CC Note=Binds 2 divalent ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00086};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00086};
CC Note=Binds 1 potassium ion per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00086};
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_00086}.
CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000255|HAMAP-
CC Rule:MF_00086}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00086}.
CC -!- SIMILARITY: Belongs to the AdoMet synthase family. {ECO:0000255|HAMAP-
CC Rule:MF_00086}.
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DR EMBL; CP001138; ACH51819.1; -; Genomic_DNA.
DR RefSeq; WP_001062143.1; NC_011149.1.
DR AlphaFoldDB; B5F5L4; -.
DR SMR; B5F5L4; -.
DR EnsemblBacteria; ACH51819; ACH51819; SeAg_B3252.
DR KEGG; sea:SeAg_B3252; -.
DR HOGENOM; CLU_041802_1_1_6; -.
DR OMA; MPYLRPD; -.
DR UniPathway; UPA00315; UER00080.
DR Proteomes; UP000008819; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 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; Cytoplasm; Magnesium; Metal-binding; Nucleotide-binding;
KW One-carbon metabolism; Potassium; Transferase.
FT CHAIN 1..384
FT /note="S-adenosylmethionine synthase"
FT /id="PRO_1000093077"
FT REGION 99..109
FT /note="Flexible loop"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
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:0000255|HAMAP-Rule:MF_00086"
FT BINDING 17
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT BINDING 43
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
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:0000255|HAMAP-Rule:MF_00086"
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:0000255|HAMAP-Rule:MF_00086"
FT BINDING 164..166
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:0000255|HAMAP-Rule:MF_00086"
FT BINDING 230..231
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:0000255|HAMAP-Rule:MF_00086"
FT BINDING 239
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT BINDING 239
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT BINDING 245..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:0000255|HAMAP-Rule:MF_00086"
FT BINDING 262
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT BINDING 266
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT BINDING 270
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:0000255|HAMAP-Rule:MF_00086"
SQ SEQUENCE 384 AA; 41939 MW; 71E8C92346633FED CRC64;
MAKHLFTSES VSEGHPDKIA DQISDAVLDA ILQQDPKARV ACETYVKTGM VLVGGEITTS
AWVDIEEITR NTVREIGYVH SDMGFDANSC AVLSAIGKQS PDINQGVDRA DPLEQGAGDQ
GLMFGYATNE TDVLMPAPVT YAHRLVQRQA EVRKNGTLPW LRPDAKSQVT FQYDDGKIVG
IDAVVLSTQH AEDIDQKSLQ EAVMEEIIKP ILPSEWLNTS TKFFINPTGR FVIGGPMGDC
GLTGRKIIVD TYGGMARHGG GAFSGKDPSK VDRSAAYAAR YVAKNIVAAG LADRCEIQVS
YAIGVAEPTS IMVETFGTEK VPAEQLILLV REFFDLRPYG LIQMLDLLHP IYKETAAYGH
FGRENFPWEK TDKAQLLRDA AGLK
