ID   METK_PICTO              Reviewed;         402 AA.
AC   Q6L123;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   03-AUG-2022, entry version 84.
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=PTO0744;
OS   Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS   100828).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Picrophilaceae; Picrophilus.
OX   NCBI_TaxID=263820;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX   PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA   Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA   Schepers B., Dock C., Antranikian G., Liebl W.;
RT   "Genome sequence of Picrophilus torridus and its implications for life
RT   around pH 0.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAT43329.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE017261; AAT43329.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_048059597.1; NC_005877.1.
DR   AlphaFoldDB; Q6L123; -.
DR   SMR; Q6L123; -.
DR   STRING; 263820.PTO0744; -.
DR   EnsemblBacteria; AAT43329; AAT43329; PTO0744.
DR   GeneID; 2845125; -.
DR   KEGG; pto:PTO0744; -.
DR   PATRIC; fig|263820.9.peg.779; -.
DR   eggNOG; arCOG01678; Archaea.
DR   HOGENOM; CLU_057642_0_0_2; -.
DR   OMA; IGHPDSI; -.
DR   OrthoDB; 21658at2157; -.
DR   UniPathway; UPA00315; UER00080.
DR   Proteomes; UP000000438; 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; -; 1.
DR   Gene3D; 3.30.300.340; -; 1.
DR   HAMAP; MF_00136; S_AdoMet_synth2; 1.
DR   InterPro; IPR042543; AdoMet_synthase_2.
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   Reference proteome; Transferase.
FT   CHAIN           1..402
FT                   /note="S-adenosylmethionine synthase"
FT                   /id="PRO_0000150034"
FT   BINDING         140..145
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00136"
SQ   SEQUENCE   402 AA;  44464 MW;  6942BF9F1D892FE3 CRC64;
     METLKTRNIQ VEAIKQSPTA SREVEIVERK GIGHPDSVAD GIAEAVSRSL SKYYIKNYGR
     ILHHNTDQVE VVGGQSDPRF GGGVVLEPSY ILISGRATST VNGERIPVKS IAIKAAKDYL
     REHFRDLEID SDVMIDSRIG NGSIDLRGLY DTRKFKANDT SFGVGFAPFT DTETIVKATE
     KYINGDLKKS LPQIGYDIKV MGFRKNRTIN LTVAAAYVDK YVKDPDEYYS VKEELVNKIT
     DNALKYTNND VQVFVNTGDI KDDKVYYLTV TGLSMENGDD GSVGRGNRVN GLITPYRPMS
     MEAAAGKNPV THVGKLYNVL SNIIANDIVK EEGGDIKEVL VRIVSQIGRP VDEPHVASIQ
     VIYEDNVDPS KHKNNITAIA DDRIAHISDL TNMFVDGKLD VF