(data stored in ACNUC29543 zone)

SWISSPROT: METK_SYNR3

ID   METK_SYNR3              Reviewed;         407 AA.
AC   A5GR07;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 73.
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=SynRCC307_0413;
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307;
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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; CT978603; CAK27316.1; -; Genomic_DNA.
DR   RefSeq; WP_011934831.1; NC_009482.1.
DR   SMR; A5GR07; -.
DR   STRING; 316278.SynRCC307_0413; -.
DR   PRIDE; A5GR07; -.
DR   EnsemblBacteria; CAK27316; CAK27316; SynRCC307_0413.
DR   KEGG; syr:SynRCC307_0413; -.
DR   eggNOG; ENOG4105CPH; Bacteria.
DR   eggNOG; COG0192; LUCA.
DR   HOGENOM; HOG000245710; -.
DR   KO; K00789; -.
DR   OMA; MPYLRPD; -.
DR   OrthoDB; 1024388at2; -.
DR   BioCyc; SSP316278:G1GJL-411-MONOMER; -.
DR   UniPathway; UPA00315; UER00080.
DR   Proteomes; UP000001115; 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; A5GR07.
DR   SWISS-2DPAGE; A5GR07.
KW   ATP-binding; Complete proteome; Cytoplasm; Magnesium; Metal-binding;
KW   Nucleotide-binding; One-carbon metabolism; Potassium;
KW   Reference proteome; Transferase.
FT   CHAIN         1    407       S-adenosylmethionine synthase.
FT                                /FTId=PRO_1000007959.
FT   NP_BIND     171    173       ATP. {ECO:0000255|HAMAP-Rule:MF_00086}.
FT   NP_BIND     248    249       ATP. {ECO:0000255|HAMAP-Rule:MF_00086}.
FT   NP_BIND     263    264       ATP. {ECO:0000255|HAMAP-Rule:MF_00086}.
FT   REGION      100    110       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     100    100       Methionine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00086}.
FT   BINDING     257    257       ATP; shared with neighboring subunit.
FT                                {ECO:0000255|HAMAP-Rule:MF_00086}.
FT   BINDING     257    257       Methionine; shared with neighboring
FT                                subunit. {ECO:0000255|HAMAP-
FT                                Rule:MF_00086}.
FT   BINDING     280    280       ATP; via amide nitrogen; shared with
FT                                neighboring subunit. {ECO:0000255|HAMAP-
FT                                Rule:MF_00086}.
FT   BINDING     284    284       ATP; shared with neighboring subunit.
FT                                {ECO:0000255|HAMAP-Rule:MF_00086}.
FT   BINDING     288    288       Methionine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00086}.
SQ   SEQUENCE   407 AA;  43271 MW;  005CFDE2F94734B8 CRC64;
     MSRYVFTSES VTEGHPDKIC DQVSDAVLDA LLAQDPASRV ACETVVNTGL CIITGEVTTT
     ARVDFNTLVR GVIADIGYSS AKAGGFDANS CAVLVALDQQ SPDIAQGVDE ADDHAGDPLD
     KVGAGDQGIM FGYACDETPE LMPLPISLAH RLARRLAEVR HNGTLGYLLP DGKTQVSVVY
     EDDQPVAIDT ILISTQHIAE IDGISDEKGL RERISADLWT HVVEPATADL SLKPSKDTTK
     YLVNPTGKFV VGGPQGDAGL TGRKIIVDTY GGYARHGGGA FSGKDPTKVD RSAAYAARFV
     AKALVAAGLA RKAEVQLSYA IGVAKPVSIL VESFGTSSHS NDELTELVNA NFDLRPGAII
     ENFKLRNLPQ QRGGNFYREV AAYGHFGRSD LNLPWEDVSV IAAKLKG
//

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