METK_PYRNV
ID METK_PYRNV Reviewed; 402 AA.
AC B1YC36;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=Tneu_1975;
OS Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 /
OS V24Sta) (Thermoproteus neutrophilus).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=444157;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M.,
RA Saltikov C., House C.H., Richardson P.;
RT "Complete sequence of Thermoproteus neutrophilus V24Sta.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001014; ACB40890.1; -; Genomic_DNA.
DR AlphaFoldDB; B1YC36; -.
DR SMR; B1YC36; -.
DR STRING; 444157.Tneu_1975; -.
DR EnsemblBacteria; ACB40890; ACB40890; Tneu_1975.
DR KEGG; tne:Tneu_1975; -.
DR eggNOG; arCOG01678; Archaea.
DR HOGENOM; CLU_057642_0_0_2; -.
DR OMA; IGHPDSI; -.
DR UniPathway; UPA00315; UER00080.
DR Proteomes; UP000001694; 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..402
FT /note="S-adenosylmethionine synthase"
FT /id="PRO_1000095956"
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; 44257 MW; 9B6C1CF76D9595DD CRC64;
MIVVEKVDKT PVAKRLVEIV ERKGQGHPDY IADGISEWVS RYLSRYYLER FGVILHHNVD
KTLVVGGQAS PRFGGGEVLQ PIYILVSGRA TSEVRLKDGV VKIPLGPIII QAARDWIKQH
FRYLDPDAHT VIDYKIGQGS ADLVGIYDLG VKSVPLANDT SVGVGYAPLT PLEQLVYKTE
RLLNSRDFKA KYPEVGEDVK VMGVRVGNEV KLTVAAAMIS RLVKDKSHYL SVKDDVKKAV
EDLASKVAPD YKIDVTINAA DKPEHGIFYL TVTGTSAEHG DDGMTGRGNR ANGLITPMRS
MSLEAAAGKN PVSHVGKIYN VVAQRIADRI YAEAKDIVEV YVEIVSQIGK PINEPKILNI
EIIKEGALTG EVKNEAEAIA REELEKITRV TEYILRGEVS LY