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 15-DEC-2009, entry version 50. DE RecName: Full=S-adenosylmethionine synthetase; DE Short=AdoMet synthetase; DE EC=2.5.1.6; DE AltName: Full=Methionine adenosyltransferase; DE Short=MAT; GN Name=SAM; OS Camellia sinensis (Tea). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; 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 overall synthetic reaction is composed of CC two sequential steps, AdoMet formation and the subsequent CC tripolyphosphate hydrolysis which occurs prior to release of CC AdoMet from the enzyme (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + L-methionine + H(2)O = phosphate + CC diphosphate + S-adenosyl-L-methionine. CC -!- COFACTOR: Binds 2 divalent ions per subunit. Magnesium or cobalt CC (By similarity). CC -!- COFACTOR: Binds 1 potassium ion per subunit (By similarity). CC -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine CC biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the AdoMet synthetase family. 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 HSSP; P13444; 1QM4. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0050897; F:cobalt ion binding; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW. DR GO; GO:0004478; F:methionine adenosyltransferase activity; IEA:EC. DR GO; GO:0030955; F:potassium ion binding; IEA:UniProtKB-KW. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW. DR InterPro; IPR002133; S-AdoMet_synthetase. DR PANTHER; PTHR11964; S-AdoMet_synt; 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 PROSITE; PS00376; ADOMET_SYNTHETASE_1; 1. DR PROSITE; PS00377; ADOMET_SYNTHETASE_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 synthetase. FT /FTId=PRO_0000363016. FT NP_BIND 119 124 ATP (Potential). FT NP_BIND 267 274 ATP (Potential). FT METAL 17 17 Magnesium (By similarity). FT METAL 43 43 Potassium (By similarity). FT METAL 271 271 Potassium (By similarity). FT METAL 279 279 Magnesium (By similarity). FT BINDING 147 147 ATP (Potential). 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 //