ID Q9LDQ7_CAMSI Unreviewed; 393 AA. AC Q9LDQ7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 08-APR-2008, entry version 40. DE S-adenosylmethionine synthetase (EC 2.5.1.6). 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. 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. 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 (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + L-methionine + H(2)O = phosphate + CC diphosphate + S-adenosyl-L-methionine. CC -!- COFACTOR: Binds 1 potassium ion per subunit (By similarity). CC -!- COFACTOR: Binds 2 divalent ions per subunit. Magnesium or cobalt CC (By similarity). CC -!- PATHWAY: Activated methyl cycle. CC -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine CC biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. CC -!- PATHWAY: Context: Activated methyl cycle. 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; AB041534; BAA94605.1; -; mRNA. DR EMBL; AJ277206; CAB83039.1; -; Genomic_DNA. DR HSSP; P13444; 1QM4. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. 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:InterPro. DR GO; GO:0030955; F:potassium ion binding; IEA:UniProtKB-KW. DR GO; GO:0006730; P:one-carbon compound metabolic process; IEA:InterPro. 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 TIGRFAMs; TIGR01034; metK; 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; Magnesium; Metal-binding; Nucleotide-binding; KW One-carbon metabolism; Potassium; Transferase. 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 //