ID METK_RICPR Reviewed; 380 AA. AC P56878; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 107. 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=RP777; OS Rickettsia prowazekii (strain Madrid E). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group. OX NCBI_TaxID=272947; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Madrid E; RX PubMed=9823893; DOI=10.1038/24094; RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., RA Kurland C.G.; RT "The genome sequence of Rickettsia prowazekii and the origin of RT mitochondria."; RL Nature 396:133-140(1998). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=B; RX PubMed=10486973; DOI=10.1093/oxfordjournals.molbev.a026208; RA Andersson J.O., Andersson S.G.E.; RT "Genome degradation is an ongoing process in Rickettsia."; RL Mol. Biol. Evol. 16:1178-1191(1999). 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 -!- CAUTION: Non-functional in strain Madrid E. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AJ235273; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={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; AJ235273; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AJ238756; CAB56090.1; -; Genomic_DNA. DR AlphaFoldDB; P56878; -. DR SMR; P56878; -. DR GeneID; 57569900; -. DR UniPathway; UPA00315; UER00080. DR Proteomes; UP000002480; 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; Reference proteome; Transferase. FT CHAIN 1..380 FT /note="S-adenosylmethionine synthase" FT /id="PRO_0000174578" 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 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 380 AA; 42149 MW; D1B29BB64481FBCA CRC64; MKNFVFTSES VSEGHPDKIA DQISDAVLDE ILKHDPNGRV ACETFVTTGL VLVGGEITTN TYVDIEQVVR NKIQEIGYNN PNYGFDGSCC AVISSIIKQS PDIAMGIDNE NEEEIGAGDQ GMVFGYACNE TKSLMPAPIY YAHLLMKRQA YLRKQNILSW LRPDAKSQVT LRYENNKPIV IDSVVLSTQH HPEIQQKDLI EAVIEEIIKP TLPTNLLHKD TKYLINPTGR FVIGGPVADC GLTGRKIIVD SYGGMAKHGG GCFSGKDPTK IDRSAAYMAR YIAKNIVGAG LADRCEIQIS YAIGVADPVS VYAETFGTSK LSNEQTTKLI TEHFDMRPGK IIKNLKLHTQ CYQKTATYGH FGREDENFTW EQLDKVDIFK //