METK_BURPS
ID METK_BURPS Reviewed; 395 AA.
AC Q63YH5;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=BPSL0212;
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243;
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
RN [2] {ECO:0007744|PDB:3IML}
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
RX PubMed=23382856; DOI=10.1371/journal.pone.0053851;
RA Baugh L., Gallagher L.A., Patrapuvich R., Clifton M.C., Gardberg A.S.,
RA Edwards T.E., Armour B., Begley D.W., Dieterich S.H., Dranow D.M.,
RA Abendroth J., Fairman J.W., Fox D. III, Staker B.L., Phan I., Gillespie A.,
RA Choi R., Nakazawa-Hewitt S., Nguyen M.T., Napuli A., Barrett L.,
RA Buchko G.W., Stacy R., Myler P.J., Stewart L.J., Manoil C.,
RA Van Voorhis W.C.;
RT "Combining functional and structural genomics to sample the essential
RT Burkholderia structome.";
RL PLoS ONE 8:E53851-E53851(2013).
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}.
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DR EMBL; BX571965; CAH34199.1; -; Genomic_DNA.
DR RefSeq; WP_004199069.1; NZ_CP009538.1.
DR RefSeq; YP_106840.1; NC_006350.1.
DR PDB; 3IML; X-ray; 2.35 A; A/B/C/D=1-395.
DR PDBsum; 3IML; -.
DR AlphaFoldDB; Q63YH5; -.
DR SMR; Q63YH5; -.
DR STRING; 272560.BPSL0212; -.
DR EnsemblBacteria; CAH34199; CAH34199; BPSL0212.
DR GeneID; 56594441; -.
DR KEGG; bps:BPSL0212; -.
DR PATRIC; fig|272560.51.peg.1505; -.
DR eggNOG; COG0192; Bacteria.
DR OMA; MPYLRPD; -.
DR UniPathway; UPA00315; UER00080.
DR EvolutionaryTrace; Q63YH5; -.
DR Proteomes; UP000000605; Chromosome 1.
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; Reference proteome;
KW Transferase.
FT CHAIN 1..395
FT /note="S-adenosylmethionine synthase"
FT /id="PRO_0000174505"
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 167..169
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 233..234
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
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 242
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 248..249
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 265
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 269
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 273
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:3IML"
FT HELIX 17..35
FT /evidence="ECO:0007829|PDB:3IML"
FT STRAND 40..47
FT /evidence="ECO:0007829|PDB:3IML"
FT STRAND 49..59
FT /evidence="ECO:0007829|PDB:3IML"
FT HELIX 66..77
FT /evidence="ECO:0007829|PDB:3IML"
FT STRAND 92..100
FT /evidence="ECO:0007829|PDB:3IML"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:3IML"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:3IML"
FT HELIX 140..157
FT /evidence="ECO:0007829|PDB:3IML"
FT STRAND 164..177
FT /evidence="ECO:0007829|PDB:3IML"
FT STRAND 180..193
FT /evidence="ECO:0007829|PDB:3IML"
FT HELIX 199..209
FT /evidence="ECO:0007829|PDB:3IML"
FT TURN 210..214
FT /evidence="ECO:0007829|PDB:3IML"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:3IML"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:3IML"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:3IML"
FT TURN 250..257
FT /evidence="ECO:0007829|PDB:3IML"
FT HELIX 274..291
FT /evidence="ECO:0007829|PDB:3IML"
FT STRAND 296..304
FT /evidence="ECO:0007829|PDB:3IML"
FT STRAND 312..317
FT /evidence="ECO:0007829|PDB:3IML"
FT HELIX 326..336
FT /evidence="ECO:0007829|PDB:3IML"
FT HELIX 341..348
FT /evidence="ECO:0007829|PDB:3IML"
FT HELIX 356..359
FT /evidence="ECO:0007829|PDB:3IML"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:3IML"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:3IML"
FT HELIX 379..386
FT /evidence="ECO:0007829|PDB:3IML"
SQ SEQUENCE 395 AA; 42641 MW; 5BE3808C1364B8C3 CRC64;
MANDYLFTSE SVSEGHPDKV ADQISDAILD AILAQDKYSR VAAETLCNTG LVVLAGEITT
TANIDYIQIA RDTIKRIGYD NTDYGIDYRG CAVLVAYDKQ SPDIAQGVDR AHDNNLDQGA
GDQGLMFGYA CDETPELMPL PIHLSHRLVE RQANLRRDGR LPWLRPDAKS QVTVRYVDGK
PHSIDTVVLS TQHAPEIDLP ALREAVIEEV IKPTLPADLI KGDIKFLVNP TGRFVIGGPQ
GDCGLTGRKI IVDTYGGAAP HGGGAFSGKD PSKVDRSAAY AGRYVAKNIV AAGLASRALI
QVSYAIGVAE PTSVMVNTFG TGRVSDETIT KLVREHFDLR PKGIIQMLDL LRPIYEKTAA
YGHFGREEPE FSWEAADKAL ALAEAAGVEP AVQVA
