METK_THEKO
ID METK_THEKO Reviewed; 405 AA.
AC Q5JF22;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, 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=TK0545;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
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; AP006878; BAD84734.1; -; Genomic_DNA.
DR RefSeq; WP_011249500.1; NC_006624.1.
DR PDB; 4L4Q; X-ray; 2.00 A; A/B/C/D=1-405.
DR PDBsum; 4L4Q; -.
DR AlphaFoldDB; Q5JF22; -.
DR SMR; Q5JF22; -.
DR STRING; 69014.TK0545; -.
DR EnsemblBacteria; BAD84734; BAD84734; TK0545.
DR GeneID; 3233990; -.
DR KEGG; tko:TK0545; -.
DR PATRIC; fig|69014.16.peg.533; -.
DR eggNOG; arCOG01678; Archaea.
DR HOGENOM; CLU_057642_0_0_2; -.
DR InParanoid; Q5JF22; -.
DR OMA; IGHPDSI; -.
DR OrthoDB; 21658at2157; -.
DR PhylomeDB; Q5JF22; -.
DR UniPathway; UPA00315; UER00080.
DR Proteomes; UP000000536; 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; Magnesium; Nucleotide-binding;
KW One-carbon metabolism; Reference proteome; Transferase.
FT CHAIN 1..405
FT /note="S-adenosylmethionine synthase"
FT /id="PRO_0000150039"
FT BINDING 139..144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00136"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:4L4Q"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:4L4Q"
FT STRAND 21..29
FT /evidence="ECO:0007829|PDB:4L4Q"
FT HELIX 34..57
FT /evidence="ECO:0007829|PDB:4L4Q"
FT STRAND 63..71
FT /evidence="ECO:0007829|PDB:4L4Q"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:4L4Q"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:4L4Q"
FT STRAND 88..100
FT /evidence="ECO:0007829|PDB:4L4Q"
FT HELIX 107..122
FT /evidence="ECO:0007829|PDB:4L4Q"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:4L4Q"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:4L4Q"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:4L4Q"
FT HELIX 145..154
FT /evidence="ECO:0007829|PDB:4L4Q"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:4L4Q"
FT HELIX 174..186
FT /evidence="ECO:0007829|PDB:4L4Q"
FT HELIX 189..194
FT /evidence="ECO:0007829|PDB:4L4Q"
FT STRAND 198..209
FT /evidence="ECO:0007829|PDB:4L4Q"
FT STRAND 212..222
FT /evidence="ECO:0007829|PDB:4L4Q"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:4L4Q"
FT HELIX 229..250
FT /evidence="ECO:0007829|PDB:4L4Q"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:4L4Q"
FT TURN 265..268
FT /evidence="ECO:0007829|PDB:4L4Q"
FT STRAND 272..277
FT /evidence="ECO:0007829|PDB:4L4Q"
FT HELIX 278..281
FT /evidence="ECO:0007829|PDB:4L4Q"
FT TURN 313..315
FT /evidence="ECO:0007829|PDB:4L4Q"
FT HELIX 317..335
FT /evidence="ECO:0007829|PDB:4L4Q"
FT STRAND 339..347
FT /evidence="ECO:0007829|PDB:4L4Q"
FT STRAND 358..366
FT /evidence="ECO:0007829|PDB:4L4Q"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:4L4Q"
FT HELIX 376..388
FT /evidence="ECO:0007829|PDB:4L4Q"
FT TURN 389..391
FT /evidence="ECO:0007829|PDB:4L4Q"
FT HELIX 392..398
FT /evidence="ECO:0007829|PDB:4L4Q"
SQ SEQUENCE 405 AA; 44615 MW; 13F0938F4ED2E6B2 CRC64;
MAGKVRNIVV EELVRTPVEM QKVELVERKG IGHPDSIADG IAEAVSRALS REYVKRYGII
LHHNTDQVEV VGGRAYPQFG GGEVIKPIYI LLSGRAVEMV DREFFPVHEI ALKAAKDYLR
KAVRHLDLEH HVIIDSRIGQ GSVDLVGVFN KAKKNPIPLA NDTSFGVGYA PLSETEKIVL
ETEKYLNSDE FKKKYPAVGE DIKVMGLRKG DEIDLTIAAA IVDSEVDNPD DYMAVKEAIY
EAAKGIVESH TERPTNIYVN TADDPKEGIY YITVTGTSAE AGDDGSVGRG NRVNGLITPN
RHMSMEAAAG KNPVSHVGKI YNILSMLIAN DIAEQVEGVE EVYVRILSQI GKPIDEPLVA
SVQIIPKKGY SIDVLQKPAY EIADEWLANI TKIQKMILED KVNVF
