METK_THET2
ID METK_THET2 Reviewed; 395 AA.
AC Q72I53;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=S-adenosylmethionine synthase {ECO:0000255|HAMAP-Rule:MF_00086};
DE Short=AdoMet synthase {ECO:0000255|HAMAP-Rule:MF_00086};
DE EC=2.5.1.6 {ECO:0000255|HAMAP-Rule:MF_00086};
DE AltName: Full=MAT {ECO:0000255|HAMAP-Rule:MF_00086};
DE AltName: Full=Methionine adenosyltransferase {ECO:0000255|HAMAP-Rule:MF_00086};
GN Name=metK {ECO:0000255|HAMAP-Rule:MF_00086}; OrderedLocusNames=TT_C1279;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
CC -!- FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from
CC methionine and ATP. The overall synthetic reaction is composed of two
CC sequential steps, AdoMet formation and the subsequent tripolyphosphate
CC hydrolysis which occurs prior to release of AdoMet from the enzyme.
CC {ECO:0000255|HAMAP-Rule:MF_00086}.
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_00086};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00086};
CC Note=Binds 2 divalent ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00086};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00086};
CC Note=Binds 1 potassium ion per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00086};
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_00086}.
CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000255|HAMAP-
CC Rule:MF_00086}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00086}.
CC -!- SIMILARITY: Belongs to the AdoMet synthase family. {ECO:0000255|HAMAP-
CC Rule:MF_00086}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS81621.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE017221; AAS81621.1; ALT_INIT; Genomic_DNA.
DR PDB; 5H9U; X-ray; 2.67 A; A/B/C/D=1-395.
DR PDBsum; 5H9U; -.
DR AlphaFoldDB; Q72I53; -.
DR SMR; Q72I53; -.
DR STRING; 262724.TT_C1279; -.
DR PRIDE; Q72I53; -.
DR EnsemblBacteria; AAS81621; AAS81621; TT_C1279.
DR KEGG; tth:TT_C1279; -.
DR eggNOG; COG0192; Bacteria.
DR HOGENOM; CLU_041802_1_1_0; -.
DR OMA; MPYLRPD; -.
DR BRENDA; 2.5.1.6; 2305.
DR UniPathway; UPA00315; UER00080.
DR Proteomes; UP000000592; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 HAMAP; MF_00086; S_AdoMet_synth1; 1.
DR InterPro; IPR022631; ADOMET_SYNTHASE_CS.
DR InterPro; IPR022630; S-AdoMet_synt_C.
DR InterPro; IPR022629; S-AdoMet_synt_central.
DR InterPro; IPR022628; S-AdoMet_synt_N.
DR InterPro; IPR002133; S-AdoMet_synthetase.
DR InterPro; IPR022636; S-AdoMet_synthetase_sfam.
DR PANTHER; PTHR11964; PTHR11964; 1.
DR Pfam; PF02773; S-AdoMet_synt_C; 1.
DR Pfam; PF02772; S-AdoMet_synt_M; 1.
DR Pfam; PF00438; S-AdoMet_synt_N; 1.
DR PIRSF; PIRSF000497; MAT; 1.
DR SUPFAM; SSF55973; SSF55973; 3.
DR TIGRFAMs; TIGR01034; metK; 1.
DR PROSITE; PS00376; ADOMET_SYNTHASE_1; 1.
DR PROSITE; PS00377; ADOMET_SYNTHASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Magnesium; Metal-binding;
KW Nucleotide-binding; One-carbon metabolism; Potassium; Transferase.
FT CHAIN 1..395
FT /note="S-adenosylmethionine synthase"
FT /id="PRO_0000174614"
FT REGION 100..110
FT /note="Flexible loop"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT BINDING 16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT BINDING 18
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT BINDING 44
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT BINDING 57
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT BINDING 100
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT BINDING 175..177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT BINDING 242..243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT BINDING 251
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT BINDING 251
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT BINDING 257..258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT BINDING 274
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT BINDING 278
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT BINDING 282
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:5H9U"
FT HELIX 17..35
FT /evidence="ECO:0007829|PDB:5H9U"
FT STRAND 40..48
FT /evidence="ECO:0007829|PDB:5H9U"
FT STRAND 51..59
FT /evidence="ECO:0007829|PDB:5H9U"
FT HELIX 66..77
FT /evidence="ECO:0007829|PDB:5H9U"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:5H9U"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:5H9U"
FT STRAND 91..100
FT /evidence="ECO:0007829|PDB:5H9U"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:5H9U"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:5H9U"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:5H9U"
FT STRAND 132..139
FT /evidence="ECO:0007829|PDB:5H9U"
FT HELIX 148..165
FT /evidence="ECO:0007829|PDB:5H9U"
FT STRAND 172..185
FT /evidence="ECO:0007829|PDB:5H9U"
FT STRAND 188..201
FT /evidence="ECO:0007829|PDB:5H9U"
FT HELIX 207..217
FT /evidence="ECO:0007829|PDB:5H9U"
FT HELIX 219..222
FT /evidence="ECO:0007829|PDB:5H9U"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:5H9U"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:5H9U"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:5H9U"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:5H9U"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:5H9U"
FT TURN 263..266
FT /evidence="ECO:0007829|PDB:5H9U"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:5H9U"
FT HELIX 283..300
FT /evidence="ECO:0007829|PDB:5H9U"
FT STRAND 305..313
FT /evidence="ECO:0007829|PDB:5H9U"
FT STRAND 321..326
FT /evidence="ECO:0007829|PDB:5H9U"
FT HELIX 335..345
FT /evidence="ECO:0007829|PDB:5H9U"
FT HELIX 350..357
FT /evidence="ECO:0007829|PDB:5H9U"
FT HELIX 365..368
FT /evidence="ECO:0007829|PDB:5H9U"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:5H9U"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:5H9U"
FT HELIX 386..393
FT /evidence="ECO:0007829|PDB:5H9U"
SQ SEQUENCE 395 AA; 43247 MW; 202DEAEE7D744057 CRC64;
MRALRLVTSE SVTEGHPDKL ADRISDAILD ALIAQDKKAR VAAETLVTTG LVFVAGEITT
EGYVDIPNLV RKTVREVGYT RAKYGFDADT CAVLTAIDEQ SPDIAGGVNL SYEWRVLKST
DPLDRVGAGD QGLMFGYATD ETPELMPLPI TLAHRLTMRL AEVRKTGLLP YLRPDGKAQV
TVVYEGDKPL YVKTVVVSAQ HSPEVEQEQL REDLIREVVR QAIPPEYLKD GETEYLINPS
GRFILGGPHA DTGLTGRKII VDTYGGAVPH GGGAFSGKDP TKVDRSASYY ARYMAKNIVA
AGLARRALVE LAYAIGKARP VSLRVETFGT GVLPDEKLTE IAKKVFDPRP LAIIEELDLL
RPIYTPTSAY GHFGRPGFPW EETDRVEALR REAGL
