(data stored in ACNUC9543 zone)

SWISSPROT: METK_YERPA

ID   METK_YERPA              Reviewed;         384 AA.
AC   Q1CB69;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   08-MAY-2019, entry version 80.
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=YPA_0335;
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua;
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(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:
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
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; CP000308; ABG12303.1; -; Genomic_DNA.
DR   RefSeq; WP_002209971.1; NZ_CP009906.1.
DR   SMR; Q1CB69; -.
DR   PRIDE; Q1CB69; -.
DR   EnsemblBacteria; ABG12303; ABG12303; YPA_0335.
DR   KEGG; ypa:YPA_0335; -.
DR   HOGENOM; HOG000245710; -.
DR   KO; K00789; -.
DR   OMA; MPYLRPD; -.
DR   UniPathway; UPA00315; UER00080.
DR   Proteomes; UP000001971; 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   3: Inferred from homology;
DR   PRODOM; Q1CB69.
DR   SWISS-2DPAGE; Q1CB69.
KW   ATP-binding; Complete proteome; Cytoplasm; Magnesium; Metal-binding;
KW   Nucleotide-binding; One-carbon metabolism; Potassium; Transferase.
FT   CHAIN         1    384       S-adenosylmethionine synthase.
FT                                /FTId=PRO_0000303002.
FT   NP_BIND     164    166       ATP. {ECO:0000255|HAMAP-Rule:MF_00086}.
FT   NP_BIND     230    231       ATP. {ECO:0000255|HAMAP-Rule:MF_00086}.
FT   NP_BIND     245    246       ATP. {ECO:0000255|HAMAP-Rule:MF_00086}.
FT   REGION       99    109       Flexible loop. {ECO:0000255|HAMAP-
FT                                Rule:MF_00086}.
FT   METAL        17     17       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00086}.
FT   METAL        43     43       Potassium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00086}.
FT   BINDING      15     15       ATP. {ECO:0000255|HAMAP-Rule:MF_00086}.
FT   BINDING      56     56       Methionine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00086}.
FT   BINDING      99     99       Methionine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00086}.
FT   BINDING     239    239       ATP; shared with neighboring subunit.
FT                                {ECO:0000255|HAMAP-Rule:MF_00086}.
FT   BINDING     239    239       Methionine; shared with neighboring
FT                                subunit. {ECO:0000255|HAMAP-
FT                                Rule:MF_00086}.
FT   BINDING     262    262       ATP; via amide nitrogen; shared with
FT                                neighboring subunit. {ECO:0000255|HAMAP-
FT                                Rule:MF_00086}.
FT   BINDING     266    266       ATP; shared with neighboring subunit.
FT                                {ECO:0000255|HAMAP-Rule:MF_00086}.
FT   BINDING     270    270       Methionine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00086}.
SQ   SEQUENCE   384 AA;  42020 MW;  F07BE244363C0123 CRC64;
     MAKHLFTSES VSEGHPDKIA DQISDAVLDA ILEQDPKARV ACETYVKTGM VLVGGEVTTN
     AWVDIEEITR RTIREIGYVH SDMGFDANSC AVLSAIGKQS PDINQGVDRE NPLEQGAGDQ
     GLMFGYATNE TSVLMPAPIT YAHRLVERQA EVRKNGALPW LRPDAKSQVT FQYDDGKIVG
     IDAVVLSTQH SEDINQKDLH EAVMEEIIKP VLPAEWITAH TKYFINPTGR FVIGGPMGDC
     GLTGRKIIVD TYGGMARHGG GAFSGKDPSK VDRSAAYAAR YVAKNIVAAG LADRCEIQVS
     YAIGVAEPTS IMVEAFGTEK IPADQLTLLV REFFDLRPYG LIKMLDLLHP IYRETAAYGH
     FGREHFPWEK TDKAALLRDA AGLK
//

If you have problems or comments...

PBIL Back to PBIL home page