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