METK_THEGJ
ID METK_THEGJ Reviewed; 405 AA.
AC C5A4B7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=S-adenosylmethionine synthase {ECO:0000255|HAMAP-Rule:MF_00136};
DE Short=AdoMet synthase {ECO:0000255|HAMAP-Rule:MF_00136};
DE EC=2.5.1.6 {ECO:0000255|HAMAP-Rule:MF_00136};
DE AltName: Full=Methionine adenosyltransferase {ECO:0000255|HAMAP-Rule:MF_00136};
GN Name=mat {ECO:0000255|HAMAP-Rule:MF_00136}; OrderedLocusNames=TGAM_0577;
OS Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=593117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15229 / JCM 11827 / EJ3;
RX PubMed=19558674; DOI=10.1186/gb-2009-10-6-r70;
RA Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M.,
RA Anthouard V., Forterre P., Wincker P., Confalonieri F.;
RT "Genome analysis and genome-wide proteomics of Thermococcus gammatolerans,
RT the most radioresistant organism known amongst the Archaea.";
RL Genome Biol. 10:R70.1-R70.23(2007).
CC -!- FUNCTION: Catalyzes the formation of S-adenosylmethionine from
CC methionine and ATP. {ECO:0000255|HAMAP-Rule:MF_00136}.
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:0000255|HAMAP-Rule:MF_00136};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00136};
CC -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis;
CC S-adenosyl-L-methionine from L-methionine: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00136}.
CC -!- SIMILARITY: Belongs to the AdoMet synthase 2 family.
CC {ECO:0000255|HAMAP-Rule:MF_00136}.
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DR EMBL; CP001398; ACS33079.1; -; Genomic_DNA.
DR RefSeq; WP_015858197.1; NC_012804.1.
DR AlphaFoldDB; C5A4B7; -.
DR SMR; C5A4B7; -.
DR STRING; 593117.TGAM_0577; -.
DR PaxDb; C5A4B7; -.
DR EnsemblBacteria; ACS33079; ACS33079; TGAM_0577.
DR GeneID; 7987200; -.
DR KEGG; tga:TGAM_0577; -.
DR PATRIC; fig|593117.10.peg.575; -.
DR eggNOG; arCOG01678; Archaea.
DR HOGENOM; CLU_057642_0_0_2; -.
DR OMA; IGHPDSI; -.
DR OrthoDB; 21658at2157; -.
DR UniPathway; UPA00315; UER00080.
DR Proteomes; UP000001488; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004478; F:methionine adenosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.300.280; -; 2.
DR HAMAP; MF_00136; S_AdoMet_synth2; 1.
DR InterPro; IPR027790; AdoMet_synthase_2_family.
DR InterPro; IPR042544; AdoMet_synthase_3.
DR InterPro; IPR002795; S-AdoMet_synthetase_arc.
DR PANTHER; PTHR36697; PTHR36697; 1.
DR Pfam; PF01941; AdoMet_Synthase; 1.
PE 3: Inferred from homology;
KW ATP-binding; Magnesium; Nucleotide-binding; One-carbon metabolism;
KW Transferase.
FT CHAIN 1..405
FT /note="S-adenosylmethionine synthase"
FT /id="PRO_1000203220"
FT BINDING 139..144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00136"
SQ SEQUENCE 405 AA; 44529 MW; F2AE74D45F02948B CRC64;
MVEKVRNIVV EELVRTPVEM QEVELVERKG IGHPDSIADG IAEAVSRALS REYLKRYGII
LHHNTDQVEV VGGRAYPQFG GGEVIKPIYI LLSGRAVELV DREEFPVHQV AIKAAKDYLK
KAVRHLDIEN HVVIDSRIGQ GSVDLVGVFN KAKENPIPLA NDTSFGVGYA PLSETERIVL
ETEKLLNSEE FKKKCPAVGE DIKVMGLRKG DEIDLTIAAA IVDSEVSNPD DYMAVKEEIY
EAAKGVVEEH TQRPTKIFVN TADDPKNGIY YITVTGTSAE AGDDGSVGRG NRVNGLITPN
RHMSMEAAAG KNPVSHVGKI YNLLSMLIAN DIAEQVEGVQ EVYVRILSQI GKPIDEPLVA
SIQIIPKKGY SIDVLQKPAY EIADAWLADV TKIQKMILDD KLNVF