ID METK_HELAH Reviewed; 385 AA. AC Q17YQ7; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 25-JUL-2006, sequence version 1. DT 27-MAR-2024, entry version 104. 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}; GN OrderedLocusNames=Hac_0382; OS Helicobacter acinonychis (strain Sheeba). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=382638; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sheeba; RX PubMed=16789826; DOI=10.1371/journal.pgen.0020120; RA Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G., RA Gressmann H., Achtman M., Schuster S.C.; RT "Who ate whom? Adaptive Helicobacter genomic changes that accompanied a RT host jump from early humans to large felines."; RL PLoS Genet. 2:1097-1110(2006). 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; Evidence={ECO:0000255|HAMAP- CC 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; Evidence={ECO:0000255|HAMAP- CC 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}. 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; AM260522; CAJ99219.1; -; Genomic_DNA. DR RefSeq; WP_011577334.1; NC_008229.1. DR AlphaFoldDB; Q17YQ7; -. DR SMR; Q17YQ7; -. DR STRING; 382638.Hac_0382; -. DR KEGG; hac:Hac_0382; -. DR eggNOG; COG0192; Bacteria. DR HOGENOM; CLU_041802_1_1_7; -. DR OrthoDB; 9801686at2; -. DR BioCyc; HACI382638:HAC_RS01730-MONOMER; -. DR UniPathway; UPA00315; UER00080. DR Proteomes; UP000000775; 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 CDD; cd18079; S-AdoMet_synt; 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:SF1; S-ADENOSYLMETHIONINE SYNTHASE ISOFORM TYPE-1; 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 3: Inferred from homology; KW ATP-binding; Cytoplasm; Magnesium; Metal-binding; Nucleotide-binding; KW One-carbon metabolism; Potassium; Transferase. FT CHAIN 1..385 FT /note="S-adenosylmethionine synthase" FT /id="PRO_0000302922" FT REGION 100..110 FT /note="Flexible loop" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086" FT BINDING 16 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 18 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086" FT BINDING 44 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086" FT BINDING 57 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 100 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 385 AA; 42358 MW; FA68A27F9790647A CRC64; MKDSFLFTSE SVTEGHPDKM ADQISDAVLD YIIERDKKAK VACETLVSNG FCVITGELKT SIYAPMQEIA REVVKKIGYT DALYGFDYRS AAVLNGIGEQ SPDINQGVDR EDGEIGAGDQ GLVFGYACKE TQMLMPLPIH LAHQLTFALA QKRKDNTLPF LRPDGKSQVS VRYENNKPIS IDTIVISTQH SPEVSQKHLK EAVIEEIVYK VLPKEYLHDN IKFFVNPTGK FVIGGPQGDA GLTGRKIIVD TYGGSCPHGG GAFSGKDPSK VDRSAAYAAR YVAKNLVASG VCDRATVQLA YAIGVVEPVS IYVNTHNTSK YSSAELEKCV KLVFKLTPKG IIESLDLLRP IYSLTSSYGH FGRELEAFTW EKTNKAEEIK AFFKH //