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METK_PYRAE
ID   METK_PYRAE              Reviewed;         402 AA.
AC   Q8ZYP7;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=PAE0677;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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; AE009441; AAL62946.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZYP7; -.
DR   SMR; Q8ZYP7; -.
DR   STRING; 178306.PAE0677; -.
DR   EnsemblBacteria; AAL62946; AAL62946; PAE0677.
DR   KEGG; pai:PAE0677; -.
DR   PATRIC; fig|178306.9.peg.491; -.
DR   eggNOG; arCOG01678; Archaea.
DR   HOGENOM; CLU_057642_0_0_2; -.
DR   InParanoid; Q8ZYP7; -.
DR   OMA; IGHPDSI; -.
DR   UniPathway; UPA00315; UER00080.
DR   Proteomes; UP000002439; 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   Reference proteome; Transferase.
FT   CHAIN           1..402
FT                   /note="S-adenosylmethionine synthase"
FT                   /id="PRO_0000150036"
FT   BINDING         137..142
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00136"
SQ   SEQUENCE   402 AA;  44258 MW;  E4548DFD3AA6D8B1 CRC64;
     MIVVGKVDKT PVAKRLVEIV ERKGQGHPDY IADGVAEWVS KYLSKYYLER FGVILHHNVD
     KTLVVGGQAS PRFGGGEILQ PIYILVSGRA TYEVRTKEGV VKIPLGPIVM QAARDWIKNH
     FRYLDPDVHV VIDYRIGQGS ADLVGIYDLG VRGIPLANDT SVGVGYAPLT PLEELVYKTE
     RLLNSRDFKA KYPEVGEDVK VMGVRVGKEV KLTIATAMIS RLVKDKSHYL SVKDDVKKAV
     EDLASKIAPE YSVEVTINAA DKPEHGIFYL TVTGTSAEHG DDGMTGRGNR ANGLITPMRS
     MSLEAAAGKN PVSHVGKIYN VVAQKIADRI YKEVKDVIEV YVEIVSQIGK PINEPKILNI
     EIIKDGELTG EVKNEVEAIA KEELGRITQV TDLILRGEVS LY
 
 
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