(data stored in ACNUC7421 zone)

SWISSPROT: METK_PARXL

ID   METK_PARXL              Reviewed;         396 AA.
AC   Q146W0;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   11-DEC-2019, entry version 83.
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=Bxeno_A0091;
GN   ORFNames=Bxe_A4371;
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400;
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA   Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA   Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA   Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT   shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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}.
DR   EMBL; CP000270; ABE28629.1; -; Genomic_DNA.
DR   RefSeq; WP_011486481.1; NZ_CP008760.1.
DR   SMR; Q146W0; -.
DR   STRING; 266265.Bxe_A4371; -.
DR   EnsemblBacteria; ABE28629; ABE28629; Bxe_A4371.
DR   GeneID; 4005534; -.
DR   KEGG; bxb:DR64_2048; -.
DR   KEGG; bxe:Bxe_A4371; -.
DR   PATRIC; fig|266265.5.peg.95; -.
DR   eggNOG; ENOG4105CPH; Bacteria.
DR   eggNOG; COG0192; LUCA.
DR   HOGENOM; HOG000245710; -.
DR   KO; K00789; -.
DR   OMA; MPYLRPD; -.
DR   OrthoDB; 1024388at2; -.
DR   BioCyc; BXEN266265:BXE_RS00450-MONOMER; -.
DR   UniPathway; UPA00315; UER00080.
DR   Proteomes; UP000001817; 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   3: Inferred from homology;
DR   PRODOM; Q146W0.
DR   SWISS-2DPAGE; Q146W0.
KW   ATP-binding; Cytoplasm; Magnesium; Metal-binding; Nucleotide-binding;
KW   One-carbon metabolism; Potassium; Reference proteome; Transferase.
FT   CHAIN           1..396
FT                   /note="S-adenosylmethionine synthase"
FT                   /id="PRO_0000302902"
FT   NP_BIND         167..169
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT   NP_BIND         233..234
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT   NP_BIND         248..249
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT   REGION          100..110
FT                   /note="Flexible loop"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT   METAL           18
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT   METAL           44
FT                   /note="Potassium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT   BINDING         16
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT   BINDING         57
FT                   /note="Methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT   BINDING         100
FT                   /note="Methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT   BINDING         242
FT                   /note="ATP; shared with neighboring subunit"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT   BINDING         242
FT                   /note="Methionine; shared with neighboring subunit"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT   BINDING         265
FT                   /note="ATP; via amide nitrogen; shared with neighboring
FT                   subunit"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT   BINDING         269
FT                   /note="ATP; shared with neighboring subunit"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT   BINDING         273
FT                   /note="Methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
SQ   SEQUENCE   396 AA;  42723 MW;  644EE4EEFF7C7A8D CRC64;
     MANDYLFTSE SVSEGHPDKV ADQISDAILD AILAQDKYSR VAAETLCNTG LVVLAGEITT
     TANVDYIQVA RNTIKRIGYD NTDYGIDYRG CAVLVAYDKQ SPDIAQGVDR AHDNNLDQGA
     GDQGLMFGYA CEETPELMPL PIHLSHRLVE RQANLRRDGR LPWLRPDAKS QVTVRYVDGK
     PHSIDTVVLS TQHSPDIDLG TLREAVIEEV IKPTLPADLI KGDIKFLVNP TGRFVIGGPQ
     GDCGLTGRKI IVDTYGGAAP HGGGAFSGKD PSKVDRSAAY AGRYVAKNIV AAGLASRCLI
     QVSYAIGVAQ PTSVMVNTFG TGRVSDAVIT RLVQEHFDLR PKGIIQMLDL LRPIYEKSAA
     YGHFGREEPE FTWESTDKAL ALAEAAGTEP VAALAE
//

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