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 31-JUL-2019, entry version 80. 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; OC Pentapetalae; 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 CC magnesium, 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 CC interacts primarily with the substrate (By similarity). CC {ECO:0000250|UniProtKB:P13444}; CC -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine CC biosynthesis; 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 SMR; Q9LDQ7; -. DR PRIDE; 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; 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 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 S-adenosylmethionine synthase. FT /FTId=PRO_0000363016. FT NP_BIND 167 169 ATP. {ECO:0000250|UniProtKB:Q00266}. FT NP_BIND 235 238 ATP. {ECO:0000250|UniProtKB:Q00266}. FT NP_BIND 252 253 ATP. {ECO:0000250|UniProtKB:P0A817}. FT METAL 9 9 Magnesium. FT {ECO:0000250|UniProtKB:P13444}. FT METAL 43 43 Potassium. FT {ECO:0000250|UniProtKB:P0A817}. FT BINDING 15 15 ATP. {ECO:0000250|UniProtKB:Q00266}. FT BINDING 56 56 Methionine. FT {ECO:0000250|UniProtKB:P0A817}. FT BINDING 99 99 Methionine. FT {ECO:0000250|UniProtKB:P0A817}. FT BINDING 246 246 ATP. {ECO:0000250|UniProtKB:Q00266}. FT BINDING 246 246 Methionine; shared with neighboring FT subunit. {ECO:0000250|UniProtKB:P0A817}. FT BINDING 269 269 ATP; via amide nitrogen; shared with FT neighboring subunit. FT {ECO:0000250|UniProtKB:P0A817}. FT BINDING 273 273 ATP; shared with neighboring subunit. FT {ECO:0000250|UniProtKB:P0A817}. FT BINDING 277 277 ATP; shared with neighboring subunit. FT {ECO:0000250|UniProtKB:P13444}. FT BINDING 277 277 Methionine. FT {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 //