(data stored in ACNUC7421 zone)

SWISSPROT: METK_SYNFM

ID   METK_SYNFM              Reviewed;         389 AA.
AC   A0LF65;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 79.
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=Sfum_0367;
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-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; CP000478; ABK16067.1; -; Genomic_DNA.
DR   RefSeq; WP_011697240.1; NC_008554.1.
DR   SMR; A0LF65; -.
DR   STRING; 335543.Sfum_0367; -.
DR   PRIDE; A0LF65; -.
DR   EnsemblBacteria; ABK16067; ABK16067; Sfum_0367.
DR   KEGG; sfu:Sfum_0367; -.
DR   eggNOG; ENOG4105CPH; Bacteria.
DR   eggNOG; COG0192; LUCA.
DR   HOGENOM; HOG000245710; -.
DR   KO; K00789; -.
DR   OMA; MPYLRPD; -.
DR   OrthoDB; 1024388at2; -.
DR   BioCyc; SFUM335543:G1G7I-372-MONOMER; -.
DR   UniPathway; UPA00315; UER00080.
DR   Proteomes; UP000001784; 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; A0LF65.
DR   SWISS-2DPAGE; A0LF65.
KW   ATP-binding; Complete proteome; Cytoplasm; Magnesium; Metal-binding;
KW   Nucleotide-binding; One-carbon metabolism; Potassium;
KW   Reference proteome; Transferase.
FT   CHAIN         1    389       S-adenosylmethionine synthase.
FT                                /FTId=PRO_0000302997.
FT   NP_BIND     168    170       ATP. {ECO:0000255|HAMAP-Rule:MF_00086}.
FT   NP_BIND     234    235       ATP. {ECO:0000255|HAMAP-Rule:MF_00086}.
FT   NP_BIND     249    250       ATP. {ECO:0000255|HAMAP-Rule:MF_00086}.
FT   REGION      101    111       Flexible loop. {ECO:0000255|HAMAP-
FT                                Rule:MF_00086}.
FT   METAL        19     19       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00086}.
FT   METAL        45     45       Potassium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00086}.
FT   BINDING      17     17       ATP. {ECO:0000255|HAMAP-Rule:MF_00086}.
FT   BINDING      58     58       Methionine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00086}.
FT   BINDING     101    101       Methionine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00086}.
FT   BINDING     243    243       ATP; shared with neighboring subunit.
FT                                {ECO:0000255|HAMAP-Rule:MF_00086}.
FT   BINDING     243    243       Methionine; shared with neighboring
FT                                subunit. {ECO:0000255|HAMAP-
FT                                Rule:MF_00086}.
FT   BINDING     270    270       ATP; shared with neighboring subunit.
FT                                {ECO:0000255|HAMAP-Rule:MF_00086}.
FT   BINDING     274    274       Methionine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00086}.
SQ   SEQUENCE   389 AA;  42594 MW;  41D431FD150DBE52 CRC64;
     MSMSNFLFTS ESVTEGHPDK VADQISDSIL DAIITEDKTA RVACETLVTT GLAFVAGEIT
     TSSWVDIPDI IRSTIKGIGY NDSSMGFDWS TCAVITSIDK QSPDIAQGVN PGEGLFEEQG
     AGDQGLMFGF ACNETPVFMP MPIYYAHRIT RKLAEVRKNG VLEFLRPDGK SQVTVEYDDH
     RPKRIDTIVV AAQHAPNVSY SMIRESIIEE VIKKVFPPEL IDDKTKYFIN STGRFVIGGP
     MGDCGLTGRK IIADTYGGQG SHGGGCFSGK DPSKVDRTAS YMARYVAKNI VAAGVADKVE
     VQVAYSIGVA EPVSLMIDTF GTGKIPSDRI AEIVRKLFSF KPANMIKQLR LLRPIFKKTA
     CYGHFGRNDP DFTWEKTDMV EPIRELAGI
//

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