ID METK_CAMSI Reviewed; 393 AA. AC Q9LDQ7; DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 14-DEC-2022, entry version 85. DE RecName: Full=S-adenosylmethionine synthase; DE Short=AdoMet synthase; DE EC=2.5.1.6 {ECO:0000250|UniProtKB:Q96551}; DE AltName: Full=Methionine adenosyltransferase; DE Short=MAT; GN Name=SAM; OS Camellia sinensis (Tea). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; Ericales; Theaceae; Camellia. OX NCBI_TaxID=4442; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Feng Y.F., Liang Y.R.; RT "Cloning of S-adenosylmethionine synthetase gene in tea plant."; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Leaf; RA Feng Y.F., Liang Y.R.; RT "S-adenosylmethionine synthetase gene."; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. 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=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: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; AJ277206; CAB83039.1; -; Genomic_DNA. DR EMBL; AB041534; BAA94605.1; -; mRNA. DR AlphaFoldDB; Q9LDQ7; -. DR SMR; Q9LDQ7; -. DR UniPathway; UPA00315; UER00080. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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; 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 TIGRFAMs; TIGR01034; metK; 1. 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..393 FT /note="S-adenosylmethionine synthase" FT /id="PRO_0000363016" 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 393 AA; 42800 MW; 67F3D2C50DA42682 CRC64; METFLFTSES VNEGHPDKLC DQISDAVLDA CLEQDQDSKV ACETCTKTNM VMVFGEITTK AAVDYEKIVR DTCRTIGFVS DDVGLDADNC KVLVNIEQQS PDIAQGVHGH LTKRPEEIGA GDQGHMFGYA TDETSELMPL SHVLATKLGA RLTEVRKNGT CPWLRPDGKT QVTVEYYNEK GATVPIRVHT LLISTQHDET VTNDEIAADL KEHVIKPVIP DKYLDEKTIF HLNPSGRFVI GGPHGDAGLT GRKIIIDTYG GWGAHGGGAF SGKDPTKVDR SGAYIVRQAA KSIVANGLAR RCIVQVSYAI GVPEPLSVFV DTYGTGKIPD KEILKIVKES FDFRPGMIAI NLDLKRGGNS RFLKTAAYGH FGRDDPDFTW ESGEAPQVGQ TSS //