METK_THEAC
ID METK_THEAC Reviewed; 400 AA.
AC Q9HM12;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=S-adenosylmethionine synthase;
DE Short=AdoMet synthase;
DE EC=2.5.1.6;
DE AltName: Full=Methionine adenosyltransferase;
GN Name=mat; OrderedLocusNames=Ta0059;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
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}.
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DR EMBL; AL445063; CAC11207.1; -; Genomic_DNA.
DR RefSeq; WP_010900487.1; NC_002578.1.
DR AlphaFoldDB; Q9HM12; -.
DR SMR; Q9HM12; -.
DR STRING; 273075.Ta0059; -.
DR EnsemblBacteria; CAC11207; CAC11207; CAC11207.
DR GeneID; 1455721; -.
DR KEGG; tac:Ta0059; -.
DR eggNOG; arCOG01678; Archaea.
DR HOGENOM; CLU_057642_0_0_2; -.
DR OMA; IGHPDSI; -.
DR OrthoDB; 21658at2157; -.
DR UniPathway; UPA00315; UER00080.
DR Proteomes; UP000001024; 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..400
FT /note="S-adenosylmethionine synthase"
FT /id="PRO_0000150043"
FT BINDING 136..141
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 400 AA; 44402 MW; E0DDB8574726285E CRC64;
MERNISVEEL HQIPTPKKEV EIVERKGIGH PDSVADGIAE AVSRSLSKYY IEHYGRILHH
NTDQVEVVGG QSAPKYGGGL VLEPTYILLS GRATTKVGND RVPFKSITIK AARDYLREHF
RHLDVDADVM IDSRIGQGSV DLVEVYDTKK LEANDTSFGV GFAPLSETET MVLNTEKYLN
GELKKKMPMV GYDIKVMGFR QKDTINLTVA AAMVDKYIHD ADEYFNIKDE LKQLVLDNAV
EYTDKEVKVY INTADIKEDG KAVGYLTVTG MSMENGDDGS VGRGNRVNGL ITPYRAMSME
AAAGKNPVTH VGKLYNVLSN KIANDIVKEE GNDIAEVLVR IVSQIGRPID DPHVASVQVI
YEGNVDHSKH KNNIRNLVDD RLAHISDLTM EFVEGKIPVF
