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   23-MAR-2010, entry version 54.
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.
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DR   EMBL; AJ277206; CAB83039.1; -; Genomic_DNA.
DR   EMBL; AB041534; BAA94605.1; -; mRNA.
DR   HSSP; P13444; 1QM4.
DR   SMR; Q9LDQ7; 3-381.
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   SUPFAM; SSF55973; S-AdoMet_synt; 3.
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; 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
//