(data stored in ACNUC7421 zone)

SWISSPROT: METK_ANADE

ID   METK_ANADE              Reviewed;         390 AA.
AC   Q2IM98;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   11-DEC-2019, entry version 86.
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=Adeh_0154;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N.,
RA   Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R.,
RA   Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000251; ABC79931.1; -; Genomic_DNA.
DR   RefSeq; WP_011419214.1; NC_007760.1.
DR   SMR; Q2IM98; -.
DR   STRING; 290397.Adeh_0154; -.
DR   EnsemblBacteria; ABC79931; ABC79931; Adeh_0154.
DR   KEGG; ade:Adeh_0154; -.
DR   eggNOG; ENOG4105CPH; Bacteria.
DR   eggNOG; COG0192; LUCA.
DR   HOGENOM; HOG000245710; -.
DR   KO; K00789; -.
DR   OMA; MPYLRPD; -.
DR   BioCyc; ADEH290397:G1G5W-158-MONOMER; -.
DR   UniPathway; UPA00315; UER00080.
DR   Proteomes; UP000001935; 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; Q2IM98.
DR   SWISS-2DPAGE; Q2IM98.
KW   ATP-binding; Cytoplasm; Magnesium; Metal-binding; Nucleotide-binding;
KW   One-carbon metabolism; Potassium; Reference proteome; Transferase.
FT   CHAIN           1..390
FT                   /note="S-adenosylmethionine synthase"
FT                   /id="PRO_0000240980"
FT   NP_BIND         160..162
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT   NP_BIND         226..227
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT   NP_BIND         241..242
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT   REGION          101..111
FT                   /note="Flexible loop"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT   METAL           19
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT   METAL           45
FT                   /note="Potassium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT   BINDING         17
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT   BINDING         58
FT                   /note="Methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT   BINDING         101
FT                   /note="Methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT   BINDING         235
FT                   /note="ATP; shared with neighboring subunit"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT   BINDING         235
FT                   /note="Methionine; shared with neighboring subunit"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT   BINDING         258
FT                   /note="ATP; via amide nitrogen; shared with neighboring
FT                   subunit"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT   BINDING         262
FT                   /note="ATP; shared with neighboring subunit"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT   BINDING         266
FT                   /note="Methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
SQ   SEQUENCE   390 AA;  41883 MW;  3B9FF06521F43705 CRC64;
     MPLQDFLFTS ESVTEGHPDK MADQISDAVL DAVLRQDPKG RVACETLLKT GYVMIAGEIT
     TKARIDYPKL ARETVRRIGY TSGDMGFDAN TCAVLVAVDQ QSPDIGQGVD TGGAGDQGMM
     FGYACDETPE LMPAPIQYAH AVTKQLAKAR RAGLDLLRPD GKSQVSVEYR DGRPARIDTV
     VVSTQHAESV SNKRLHEAVR EQVIAKALPK RLVDRKTRIL INPTGRFVIG GPMGDTGVTG
     RKIIVDTYGG MGRHGGGAFS GKDPSKVDRS AAYMGRYIAK NVVAAGLAAR CEVQVAYAIG
     VAEPVSVMVD TFGTAKVPEG KIARAVREVF GLTPRAIIEG LDLLRPVYEK TAAYGHFGRT
     EKTFTWERTD KKDALADAAG LSKIRAVAGV
//

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