METK_METJA
ID METK_METJA Reviewed; 406 AA.
AC Q58605;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=MJ1208;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP PROTEIN SEQUENCE OF 3-43; 53-91; 132-178; 186-209; 213-225; 229-239;
RP 250-269; 295-336 AND 347-379, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP PATHWAY, AND SUBUNIT.
RX PubMed=10660563; DOI=10.1074/jbc.275.6.4055;
RA Graham D.E., Bock C.L., Schalk-Hihi C., Lu Z.J., Markham G.D.;
RT "Identification of a highly diverged class of S-adenosylmethionine
RT synthetases in the archaea.";
RL J. Biol. Chem. 275:4055-4059(2000).
CC -!- FUNCTION: Catalyzes the formation of S-adenosylmethionine from
CC methionine and ATP. {ECO:0000269|PubMed:10660563}.
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:0000269|PubMed:10660563};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10660563};
CC -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis;
CC S-adenosyl-L-methionine from L-methionine: step 1/1.
CC {ECO:0000269|PubMed:10660563}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10660563}.
CC -!- SIMILARITY: Belongs to the AdoMet synthase 2 family. {ECO:0000305}.
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DR EMBL; L77117; AAB99212.1; -; Genomic_DNA.
DR PIR; G64450; G64450.
DR RefSeq; WP_010870720.1; NC_000909.1.
DR PDB; 7P82; X-ray; 2.04 A; A/C=1-406.
DR PDB; 7P83; X-ray; 2.22 A; A/C=1-406.
DR PDB; 7P84; X-ray; 2.05 A; A/C=1-406.
DR PDB; 7P8M; X-ray; 1.71 A; A/C=1-406.
DR PDBsum; 7P82; -.
DR PDBsum; 7P83; -.
DR PDBsum; 7P84; -.
DR PDBsum; 7P8M; -.
DR AlphaFoldDB; Q58605; -.
DR SMR; Q58605; -.
DR STRING; 243232.MJ_1208; -.
DR EnsemblBacteria; AAB99212; AAB99212; MJ_1208.
DR GeneID; 1452105; -.
DR KEGG; mja:MJ_1208; -.
DR eggNOG; arCOG01678; Archaea.
DR HOGENOM; CLU_057642_0_0_2; -.
DR InParanoid; Q58605; -.
DR OMA; IGHPDSI; -.
DR OrthoDB; 21658at2157; -.
DR PhylomeDB; Q58605; -.
DR BRENDA; 2.5.1.6; 3260.
DR UniPathway; UPA00315; UER00080.
DR Proteomes; UP000000805; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Direct protein sequencing; Magnesium;
KW Nucleotide-binding; One-carbon metabolism; Reference proteome; Transferase.
FT CHAIN 1..406
FT /note="S-adenosylmethionine synthase"
FT /id="PRO_0000150028"
FT BINDING 141..146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:7P8M"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:7P8M"
FT STRAND 17..25
FT /evidence="ECO:0007829|PDB:7P8M"
FT HELIX 30..53
FT /evidence="ECO:0007829|PDB:7P8M"
FT STRAND 59..67
FT /evidence="ECO:0007829|PDB:7P8M"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:7P8M"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:7P8M"
FT STRAND 84..92
FT /evidence="ECO:0007829|PDB:7P8M"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:7P8M"
FT TURN 99..102
FT /evidence="ECO:0007829|PDB:7P8M"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:7P8M"
FT HELIX 109..124
FT /evidence="ECO:0007829|PDB:7P8M"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:7P8M"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:7P8M"
FT HELIX 145..153
FT /evidence="ECO:0007829|PDB:7P8M"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:7P82"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:7P8M"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:7P8M"
FT HELIX 175..187
FT /evidence="ECO:0007829|PDB:7P8M"
FT HELIX 190..195
FT /evidence="ECO:0007829|PDB:7P8M"
FT STRAND 199..210
FT /evidence="ECO:0007829|PDB:7P8M"
FT STRAND 213..223
FT /evidence="ECO:0007829|PDB:7P8M"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:7P8M"
FT HELIX 230..251
FT /evidence="ECO:0007829|PDB:7P8M"
FT STRAND 255..261
FT /evidence="ECO:0007829|PDB:7P8M"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:7P8M"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:7P8M"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:7P8M"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:7P8M"
FT HELIX 319..335
FT /evidence="ECO:0007829|PDB:7P8M"
FT STRAND 340..348
FT /evidence="ECO:0007829|PDB:7P8M"
FT STRAND 359..367
FT /evidence="ECO:0007829|PDB:7P8M"
FT HELIX 373..389
FT /evidence="ECO:0007829|PDB:7P8M"
FT HELIX 392..399
FT /evidence="ECO:0007829|PDB:7P8M"
SQ SEQUENCE 406 AA; 45252 MW; 457B087EE1243404 CRC64;
MRNIIVKKLD VEPIEERPTE IVERKGLGHP DSICDGIAES VSRALCKMYM EKFGTILHHN
TDQVELVGGH AYPKFGGGVM VSPIYILLSG RATMEILDKE KNEVIKLPVG TTAVKAAKEY
LKKVLRNVDV DKDVIIDCRI GQGSMDLVDV FERQKNEVPL ANDTSFGVGY APLSTTERLV
LETERFLNSD ELKNEIPAVG EDIKVMGLRE GKKITLTIAM AVVDRYVKNI EEYKEVIEKV
RKKVEDLAKK IADGYEVEIH INTADDYERE SVYLTVTGTS AEMGDDGSVG RGNRVNGLIT
PFRPMSMEAA SGKNPVNHVG KIYNILANLI ANDIAKLEGV KECYVRILSQ IGKPINEPKA
LDIEIITEDS YDIKDIEPKA KEIANKWLDN IMEVQKMIVE GKVTTF
