(data stored in ACNUC7421 zone)

SWISSPROT: METK_PSEAB

ID   METK_PSEAB              Reviewed;         396 AA.
AC   Q02TL9;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   30-AUG-2017, entry version 70.
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};
GN   OrderedLocusNames=PA14_07090;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
CC   -!- FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet)
CC       from methionine and ATP. The overall synthetic reaction is
CC       composed of two sequential steps, AdoMet formation and the
CC       subsequent tripolyphosphate hydrolysis which occurs prior to
CC       release of AdoMet from the enzyme. {ECO:0000255|HAMAP-
CC       Rule:MF_00086}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-methionine + H(2)O = phosphate +
CC       diphosphate + S-adenosyl-L-methionine. {ECO:0000255|HAMAP-
CC       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
CC       biosynthesis; 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.
CC       {ECO:0000255|HAMAP-Rule:MF_00086}.
DR   EMBL; CP000438; ABJ15509.1; -; Genomic_DNA.
DR   RefSeq; WP_003084948.1; NC_008463.1.
DR   ProteinModelPortal; Q02TL9; -.
DR   SMR; Q02TL9; -.
DR   PRIDE; Q02TL9; -.
DR   EnsemblBacteria; ABJ15509; ABJ15509; PA14_07090.
DR   KEGG; pau:PA14_07090; -.
DR   HOGENOM; HOG000245710; -.
DR   KO; K00789; -.
DR   OMA; PGHFLFT; -.
DR   UniPathway; UPA00315; UER00080.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004478; F:methionine adenosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
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; Q02TL9.
DR   SWISS-2DPAGE; Q02TL9.
KW   ATP-binding; Complete proteome; Cytoplasm; Magnesium; Metal-binding;
KW   Nucleotide-binding; One-carbon metabolism; Potassium; Transferase.
FT   CHAIN         1    396       S-adenosylmethionine synthase.
FT                                /FTId=PRO_0000302964.
FT   NP_BIND     165    167       ATP. {ECO:0000255|HAMAP-Rule:MF_00086}.
FT   NP_BIND     246    247       ATP. {ECO:0000255|HAMAP-Rule:MF_00086}.
FT   REGION      100    110       Flexible loop. {ECO:0000255|HAMAP-
FT                                Rule:MF_00086}.
FT   METAL        18     18       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00086}.
FT   METAL        44     44       Potassium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00086}.
FT   BINDING      16     16       ATP. {ECO:0000255|HAMAP-Rule:MF_00086}.
FT   BINDING      57     57       Methionine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00086}.
FT   BINDING     100    100       Methionine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00086}.
FT   BINDING     240    240       ATP; shared with neighboring subunit.
FT                                {ECO:0000255|HAMAP-Rule:MF_00086}.
FT   BINDING     240    240       Methionine; shared with neighboring
FT                                subunit. {ECO:0000255|HAMAP-
FT                                Rule:MF_00086}.
FT   BINDING     263    263       ATP; via amide nitrogen; shared with
FT                                neighboring subunit. {ECO:0000255|HAMAP-
FT                                Rule:MF_00086}.
FT   BINDING     267    267       ATP; shared with neighboring subunit.
FT                                {ECO:0000255|HAMAP-Rule:MF_00086}.
FT   BINDING     271    271       Methionine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00086}.
SQ   SEQUENCE   396 AA;  42709 MW;  E0FD2A96E97E5D81 CRC64;
     MSEYSVFTSE SVSEGHPDKI ADQISDAVLD AIIAKDKYAR VACETLVKTG VAIIAGEVTT
     SAWVDLEELV RKVIIDIGYD SSDVGFDGAT CGVLNIIGKQ SVDINQGVDR AKPEDQGAGD
     QGLMFGYASN ETDVLMPAPI CFSHRLVERQ AEARKSGLLP WLRPDAKSQV TCRYEGGKVV
     GIDAVVLSTQ HNPEVSYNDL RDGVMELIIK QVLPAELLHK DTQFHINPTG NFVIGGPVGD
     CGLTGRKIIV DSYGGMARHG GGAFSGKDPS KVDRSAAYAG RYVAKNIVAA GLAERCEIQV
     SYAIGVAQPT SISINTFGTG KVSDEKIVQL VREHFDLRPY AITKMLDLLH PMYQPTAAYG
     HFGRHPFELT VDGDTFTAFT WEKTDKAALL RDAAGL
//

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