ID   METK_METTM              Reviewed;         401 AA.
AC   P26498; D9PYN3;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=S-adenosylmethionine synthase;
DE            Short=AdoMet synthase;
DE            EC=2.5.1.6;
DE   AltName: Full=Methionine adenosyltransferase;
GN   Name=mat; Synonyms=metK; OrderedLocusNames=MTBMA_c17630;
OS   Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS   14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS   thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=79929;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=8376340; DOI=10.1128/jb.175.18.5945-5952.1993;
RA   Jenal U., Thurner C., Leisinger T.;
RT   "Transcription of the ileS operon in the archaeon Methanobacterium
RT   thermoautotrophicum Marburg.";
RL   J. Bacteriol. 175:5945-5952(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=20802048; DOI=10.1128/jb.00844-10;
RA   Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA   Gottschalk G., Thauer R.K.;
RT   "Complete genome sequence of Methanothermobacter marburgensis, a
RT   methanoarchaeon model organism.";
RL   J. Bacteriol. 192:5850-5851(2010).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 184-401.
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=2037598; DOI=10.1016/s0021-9258(18)99261-6;
RA   Jenal U., Rechsteiner T., Tan P.-Y., Buehlmann E., Meile L., Leisinger T.;
RT   "Isoleucyl-tRNA synthetase of Methanobacterium thermoautotrophicum Marburg.
RT   Cloning of the gene, nucleotide sequence, and localization of a base change
RT   conferring resistance to pseudomonic acid.";
RL   J. Biol. Chem. 266:10570-10577(1991).
CC   -!- FUNCTION: Catalyzes the formation of S-adenosylmethionine from
CC       methionine and ATP. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis;
CC       S-adenosyl-L-methionine from L-methionine: step 1/1.
CC   -!- SIMILARITY: Belongs to the AdoMet synthase 2 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X66398; CAA47022.1; -; Genomic_DNA.
DR   EMBL; CP001710; ADL59331.1; -; Genomic_DNA.
DR   EMBL; M59245; AAA72949.1; -; Genomic_DNA.
DR   RefSeq; WP_013296541.1; NC_014408.1.
DR   AlphaFoldDB; P26498; -.
DR   SMR; P26498; -.
DR   STRING; 79929.MTBMA_c17630; -.
DR   EnsemblBacteria; ADL59331; ADL59331; MTBMA_c17630.
DR   GeneID; 9705474; -.
DR   KEGG; mmg:MTBMA_c17630; -.
DR   PATRIC; fig|79929.8.peg.1700; -.
DR   HOGENOM; CLU_057642_0_0_2; -.
DR   OMA; IGHPDSI; -.
DR   OrthoDB; 21658at2157; -.
DR   UniPathway; UPA00315; UER00080.
DR   Proteomes; UP000000345; 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..401
FT                   /note="S-adenosylmethionine synthase"
FT                   /id="PRO_0000150033"
FT   BINDING         135..140
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   401 AA;  43738 MW;  29F03FCACF07CA3F CRC64;
     MRNIIVEPLN QTPIEDQKVE IVERKGIGHP DSISDGIAES VSRALCNAYL DRFGAIMHHN
     TDEVQITAGE SAPQFGGGEV IKPIEILLTG RGIAEVDGEK IGLDRIAISA AKEYLRDNII
     NLDVETCTVV ECKIGHGSGD LRDVFARKGR APLSNDTSFG VGFAPFSETE RIVMEAENLL
     NSPEFKKKYP AVGEDIKVMG LRENDNITLT VACAMVDRYV SDLEEYLEIK NVVKDEVFKL
     ASGITERNLE VFVNTADRCE DDEPSVYITV TGTSAEMGDD GSVGRGNRAN GLITPNRPMS
     MEATSGKNPI NHVGKIYNLL SNQMAADIVE SIEGVKQVHI MILSQIGKPI DHPKAATAQV
     ILEDGYTMDD ITGKVSGVMD AWLEDIPSIT EMLVKGQLRT F