METK_ECOLI
ID METK_ECOLI Reviewed; 384 AA.
AC P0A817; P04384; P30869; Q2M9Q1;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 147.
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, ECO:0000269|PubMed:10551856, ECO:0000269|PubMed:10660564, ECO:0000269|PubMed:6251075, ECO:0000269|PubMed:7629147, ECO:0000269|PubMed:7629176, ECO:0000269|PubMed:9753435};
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}; Synonyms=metX;
GN OrderedLocusNames=b2942, JW2909;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6094561; DOI=10.1016/s0021-9258(17)42628-7;
RA Markham G.D., Deparasis J., Gatmaitan J.;
RT "The sequence of metK, the structural gene for S-adenosylmethionine
RT synthetase in Escherichia coli.";
RL J. Biol. Chem. 259:14505-14507(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=8231813; DOI=10.1111/j.1365-2958.1993.tb01742.x;
RA Satishchandran C., Taylor J.C., Markham G.D.;
RT "Isozymes of S-adenosylmethionine synthetase are encoded by tandemly
RT duplicated genes in Escherichia coli.";
RL Mol. Microbiol. 9:835-846(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-63.
RX PubMed=2198270; DOI=10.1128/jb.172.8.4631-4640.1990;
RA Moore R.C., Boyle S.M.;
RT "Nucleotide sequence and analysis of the speA gene encoding biosynthetic
RT arginine decarboxylase in Escherichia coli.";
RL J. Bacteriol. 172:4631-4640(1990).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, AND SUBUNIT.
RX PubMed=6251075; DOI=10.1016/s0021-9258(19)70530-4;
RA Markham G.D., Hafner E.W., Tabor C.W., Tabor H.;
RT "S-Adenosylmethionine synthetase from Escherichia coli.";
RL J. Biol. Chem. 255:9082-9092(1980).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF GLU-43.
RX PubMed=7629147; DOI=10.1074/jbc.270.31.18277;
RA McQueney M.S., Markham G.D.;
RT "Investigation of monovalent cation activation of S-adenosylmethionine
RT synthetase using mutagenesis and uranyl inhibition.";
RL J. Biol. Chem. 270:18277-18284(1995).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, PATHWAY, AND MUTAGENESIS OF CYS-90
RP AND CYS-240.
RC STRAIN=B, and K12;
RX PubMed=7629176; DOI=10.1074/jbc.270.31.18484;
RA Reczkowski R.S., Markham G.D.;
RT "Structural and functional roles of cysteine 90 and cysteine 240 in S-
RT adenosylmethionine synthetase.";
RL J. Biol. Chem. 270:18484-18490(1995).
RN [9]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND MUTAGENESIS OF ARG-245.
RC STRAIN=B, and K12;
RX PubMed=9753435; DOI=10.1021/bi9811011;
RA Reczkowski R.S., Taylor J.C., Markham G.D.;
RT "The active-site arginine of S-adenosylmethionine synthetase orients the
RT reaction intermediate.";
RL Biochemistry 37:13499-13506(1998).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, MUTAGENESIS OF ASP-17; ASP-119;
RP ASP-239 AND ASP-272, AND COFACTOR.
RC STRAIN=B, and K12;
RX PubMed=10551856; DOI=10.1074/jbc.274.46.32909;
RA Taylor J.C., Markham G.D.;
RT "The bifunctional active site of S-adenosylmethionine synthetase. Roles of
RT the active site aspartates.";
RL J. Biol. Chem. 274:32909-32914(1999).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBUNIT, AND MUTAGENESIS OF HIS-15;
RP LYS-166; LYS-246; LYS-266 AND LYS-270.
RC STRAIN=B, and K12;
RX PubMed=10660564; DOI=10.1074/jbc.275.6.4060;
RA Taylor J.C., Markham G.D.;
RT "The bifunctional active site of S-adenosylmethionine synthetase. Roles of
RT the basic residues.";
RL J. Biol. Chem. 275:4060-4065(2000).
RN [13]
RP TRANSCRIPTIONAL START SITE, AND ESSENTIAL GENE.
RX PubMed=11952912; DOI=10.1046/j.1365-2958.2002.02856.x;
RA Wei Y., Newman E.B.;
RT "Studies on the role of the metK gene product of Escherichia coli K-12.";
RL Mol. Microbiol. 43:1651-1656(2002).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND
RP POTASSIUM, SUBUNIT, COFACTOR, AND MASS SPECTROMETRY.
RX PubMed=8550549; DOI=10.1074/jbc.271.1.136;
RA Takusagawa F., Kamitori S., Misaki S., Markham G.D.;
RT "Crystal structure of S-adenosylmethionine synthetase.";
RL J. Biol. Chem. 271:136-147(1996).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEXES WITH ATP ANALOGS;
RP MAGNESIUM AND POTASSIUM, SUBUNIT, AND COFACTOR.
RX PubMed=8611562; DOI=10.1021/bi952604z;
RA Takusagawa F., Kamitori S., Markham G.D.;
RT "Structure and function of S-adenosylmethionine synthetase: crystal
RT structures of S-adenosylmethionine synthetase with ADP, BrADP, and PPi at
RT 2.8-A resolution.";
RL Biochemistry 35:2586-2596(1996).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS), AND SUBUNIT.
RX PubMed=8723769; DOI=10.1080/07391102.1996.10508887;
RA Fu Z., Hu Y., Markham G.D., Takusagawa F.;
RT "Flexible loop in the structure of S-adenosylmethionine synthetase
RT crystallized in the tetragonal modification.";
RL J. Biomol. Struct. Dyn. 13:727-739(1996).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEXES WITH ATP ANALOG;
RP L-METHIONINE; POTASSIUM AND MAGNESIUM, SUBUNIT, AND COFACTOR.
RX PubMed=14967023; DOI=10.1021/bi035611t;
RA Komoto J., Yamada T., Takata Y., Markham G.D., Takusagawa F.;
RT "Crystal structure of the S-adenosylmethionine synthetase ternary complex:
RT a novel catalytic mechanism of S-adenosylmethionine synthesis from ATP and
RT Met.";
RL Biochemistry 43:1821-1831(2004).
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 (PubMed:6251075, PubMed:7629147, PubMed:7629176, PubMed:9753435,
CC PubMed:10551856, PubMed:10660564). Is essential for growth
CC (PubMed:11952912). {ECO:0000269|PubMed:10551856,
CC ECO:0000269|PubMed:10660564, ECO:0000269|PubMed:11952912,
CC ECO:0000269|PubMed:6251075, ECO:0000269|PubMed:7629147,
CC ECO:0000269|PubMed:7629176, ECO:0000269|PubMed:9753435}.
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 ECO:0000269|PubMed:10551856, ECO:0000269|PubMed:10660564,
CC ECO:0000269|PubMed:6251075, ECO:0000269|PubMed:7629147,
CC ECO:0000269|PubMed:7629176, ECO:0000269|PubMed:9753435};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00086,
CC ECO:0000269|PubMed:10551856, ECO:0000269|PubMed:14967023,
CC ECO:0000269|PubMed:6251075, ECO:0000269|PubMed:8550549,
CC ECO:0000269|PubMed:8611562};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:6251075};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:6251075};
CC Note=Binds 2 divalent ions per subunit. The ions interact primarily
CC with the substrate. {ECO:0000269|PubMed:14967023,
CC ECO:0000269|PubMed:8550549, ECO:0000269|PubMed:8611562,
CC ECO:0000305|PubMed:10551856, ECO:0007744|PDB:1P7L,
CC ECO:0007744|PDB:1RG9};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00086,
CC ECO:0000269|PubMed:14967023, ECO:0000269|PubMed:6251075,
CC ECO:0000269|PubMed:7629147, ECO:0000269|PubMed:8550549,
CC ECO:0000269|PubMed:8611562};
CC Note=Binds 1 potassium ion per subunit. The potassium ion interacts
CC primarily with the substrate. {ECO:0000269|PubMed:14967023,
CC ECO:0000269|PubMed:7629147, ECO:0000269|PubMed:8550549,
CC ECO:0000269|PubMed:8611562, ECO:0007744|PDB:1P7L,
CC ECO:0007744|PDB:1RG9};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.0 mM for Mg(2+) {ECO:0000269|PubMed:7629147};
CC KM=0.11 mM for ATP {ECO:0000269|PubMed:7629147};
CC KM=0.08 mM for L-methionine {ECO:0000269|PubMed:7629147};
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, ECO:0000269|PubMed:10551856,
CC ECO:0000269|PubMed:10660564, ECO:0000269|PubMed:6251075,
CC ECO:0000269|PubMed:7629147, ECO:0000269|PubMed:7629176,
CC ECO:0000269|PubMed:9753435}.
CC -!- SUBUNIT: Homotetramer; dimer of dimers (PubMed:6251075, PubMed:7629147,
CC PubMed:7629176, PubMed:10660564, PubMed:8550549, PubMed:8611562,
CC PubMed:8723769, PubMed:14967023). The active sites are at the interface
CC between subunits; each dimer has two active sites (PubMed:8550549,
CC PubMed:8611562, PubMed:8723769, PubMed:14967023).
CC {ECO:0000269|PubMed:10660564, ECO:0000269|PubMed:14967023,
CC ECO:0000269|PubMed:6251075, ECO:0000269|PubMed:7629176,
CC ECO:0000269|PubMed:8550549, ECO:0000269|PubMed:8611562,
CC ECO:0000269|PubMed:8723769}.
CC -!- INTERACTION:
CC P0A817; P0A6F5: groEL; NbExp=2; IntAct=EBI-546295, EBI-543750;
CC P0A817; P0A817: metK; NbExp=2; IntAct=EBI-546295, EBI-546295;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00086}.
CC -!- INDUCTION: AdoMet activates the tripolyphosphatase reaction.
CC -!- MASS SPECTROMETRY: Mass=41843; Mass_error=10.5; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8550549};
CC -!- DISRUPTION PHENOTYPE: Cells are resistant to methionine-analogs, such
CC as DL-ethionine(Et). {ECO:0000269|PubMed:8231813}.
CC -!- SIMILARITY: Belongs to the AdoMet synthase family. {ECO:0000255|HAMAP-
CC Rule:MF_00086}.
CC -!- CAUTION: Was originally thought to differ from MetX, which was assigned
CC as a second AdoMet synthase before being shown to be identical to MetK.
CC {ECO:0000305|PubMed:8231813}.
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DR EMBL; K02129; AAA24164.1; -; Genomic_DNA.
DR EMBL; U28377; AAA69109.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75979.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77005.1; -; Genomic_DNA.
DR EMBL; M98266; AAB05197.1; -; Genomic_DNA.
DR EMBL; M31770; AAA24645.2; -; Genomic_DNA.
DR PIR; E65079; SYECSM.
DR RefSeq; NP_417417.1; NC_000913.3.
DR RefSeq; WP_001062128.1; NZ_STEB01000001.1.
DR PDB; 1FUG; X-ray; 3.20 A; A/B=2-384.
DR PDB; 1MXA; X-ray; 2.80 A; A=2-384.
DR PDB; 1MXB; X-ray; 2.80 A; A=2-384.
DR PDB; 1MXC; X-ray; 3.00 A; A=2-384.
DR PDB; 1P7L; X-ray; 2.50 A; A/B/C/D=2-384.
DR PDB; 1RG9; X-ray; 2.50 A; A/B/C/D=2-384.
DR PDB; 1XRA; X-ray; 3.00 A; A=2-384.
DR PDB; 1XRB; X-ray; 3.00 A; A=2-384.
DR PDB; 1XRC; X-ray; 3.00 A; A=2-384.
DR PDB; 7OCK; EM; 3.60 A; B/C/D/E/F/G/H/I=1-384.
DR PDBsum; 1FUG; -.
DR PDBsum; 1MXA; -.
DR PDBsum; 1MXB; -.
DR PDBsum; 1MXC; -.
DR PDBsum; 1P7L; -.
DR PDBsum; 1RG9; -.
DR PDBsum; 1XRA; -.
DR PDBsum; 1XRB; -.
DR PDBsum; 1XRC; -.
DR PDBsum; 7OCK; -.
DR AlphaFoldDB; P0A817; -.
DR SMR; P0A817; -.
DR BioGRID; 4260657; 257.
DR DIP; DIP-35672N; -.
DR IntAct; P0A817; 39.
DR MINT; P0A817; -.
DR STRING; 511145.b2942; -.
DR iPTMnet; P0A817; -.
DR SWISS-2DPAGE; P0A817; -.
DR jPOST; P0A817; -.
DR PaxDb; P0A817; -.
DR PRIDE; P0A817; -.
DR EnsemblBacteria; AAC75979; AAC75979; b2942.
DR EnsemblBacteria; BAE77005; BAE77005; BAE77005.
DR GeneID; 66673177; -.
DR GeneID; 945389; -.
DR KEGG; ecj:JW2909; -.
DR KEGG; eco:b2942; -.
DR PATRIC; fig|1411691.4.peg.3791; -.
DR EchoBASE; EB0584; -.
DR eggNOG; COG0192; Bacteria.
DR HOGENOM; CLU_041802_1_1_6; -.
DR InParanoid; P0A817; -.
DR OMA; MPYLRPD; -.
DR PhylomeDB; P0A817; -.
DR BioCyc; EcoCyc:S-ADENMETSYN-MON; -.
DR BioCyc; MetaCyc:S-ADENMETSYN-MON; -.
DR BRENDA; 2.5.1.6; 2026.
DR SABIO-RK; P0A817; -.
DR UniPathway; UPA00315; UER00080.
DR EvolutionaryTrace; P0A817; -.
DR PRO; PR:P0A817; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0004478; F:methionine adenosyltransferase activity; IDA:EcoCyc.
DR GO; GO:0030955; F:potassium ion binding; IDA:EcoCyc.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IMP:EcoCyc.
DR GO; GO:0033353; P:S-adenosylmethionine cycle; IMP:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cobalt; Cytoplasm; Magnesium;
KW Manganese; Metal-binding; Nucleotide-binding; One-carbon metabolism;
KW Potassium; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..384
FT /note="S-adenosylmethionine synthase"
FT /id="PRO_0000174518"
FT REGION 99..109
FT /note="Flexible loop"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086,
FT ECO:0000269|PubMed:14967023"
FT BINDING 15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086,
FT ECO:0000269|PubMed:14967023, ECO:0007744|PDB:1P7L,
FT ECO:0007744|PDB:1RG9"
FT BINDING 17
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086,
FT ECO:0000269|PubMed:14967023, ECO:0007744|PDB:1P7L,
FT ECO:0007744|PDB:1RG9"
FT BINDING 43
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086,
FT ECO:0000269|PubMed:14967023, ECO:0000305|PubMed:7629147,
FT ECO:0007744|PDB:1MXC, ECO:0007744|PDB:1P7L,
FT ECO:0007744|PDB:1RG9"
FT BINDING 56
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086,
FT ECO:0000269|PubMed:14967023, ECO:0007744|PDB:1P7L,
FT ECO:0007744|PDB:1RG9"
FT BINDING 99
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086,
FT ECO:0000269|PubMed:14967023, ECO:0007744|PDB:1P7L,
FT ECO:0007744|PDB:1RG9"
FT BINDING 164..166
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086,
FT ECO:0000269|PubMed:14967023, ECO:0007744|PDB:1P7L,
FT ECO:0007744|PDB:1RG9"
FT BINDING 230..231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086,
FT ECO:0000269|PubMed:14967023, ECO:0007744|PDB:1P7L,
FT ECO:0007744|PDB:1RG9"
FT BINDING 239
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086,
FT ECO:0000269|PubMed:14967023, ECO:0007744|PDB:1RG9"
FT BINDING 239
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086,
FT ECO:0000269|PubMed:14967023, ECO:0007744|PDB:1P7L"
FT BINDING 245..246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086,
FT ECO:0000269|PubMed:14967023, ECO:0007744|PDB:1P7L,
FT ECO:0007744|PDB:1RG9"
FT BINDING 262
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086,
FT ECO:0000269|PubMed:14967023, ECO:0007744|PDB:1P7L,
FT ECO:0007744|PDB:1RG9"
FT BINDING 266
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086,
FT ECO:0000269|PubMed:14967023, ECO:0007744|PDB:1P7L,
FT ECO:0007744|PDB:1RG9"
FT BINDING 270
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086,
FT ECO:0000269|PubMed:14967023, ECO:0007744|PDB:1P7L,
FT ECO:0007744|PDB:1RG9"
FT MOD_RES 3
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MUTAGEN 15
FT /note="H->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10660564"
FT MUTAGEN 17
FT /note="D->N,A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10551856"
FT MUTAGEN 43
FT /note="E->K: Misfolding and subject to proteolytic
FT degradation."
FT /evidence="ECO:0000269|PubMed:7629147"
FT MUTAGEN 43
FT /note="E->Q: Nearly abolishes enzyme activity. Abolishes
FT stimulation of enzyme activity by potassium."
FT /evidence="ECO:0000269|PubMed:7629147"
FT MUTAGEN 90
FT /note="C->A,S: Decrease in the homotetramer formation
FT capability. Enhanced thermal stability."
FT /evidence="ECO:0000269|PubMed:7629176"
FT MUTAGEN 119
FT /note="D->N: Decrease of both AdoMet synthesis and AdoMet-
FT activated tripolyphosphate hydrolysis."
FT /evidence="ECO:0000269|PubMed:10551856"
FT MUTAGEN 166
FT /note="K->M: Decrease in AdoMet synthesis."
FT /evidence="ECO:0000269|PubMed:10660564"
FT MUTAGEN 239
FT /note="D->N: Decrease in AdoMet synthesis."
FT /evidence="ECO:0000269|PubMed:10551856"
FT MUTAGEN 240
FT /note="C->A: Decrease in AdoMet synthesis."
FT /evidence="ECO:0000269|PubMed:7629176"
FT MUTAGEN 245
FT /note="R->H,L: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9753435"
FT MUTAGEN 246
FT /note="K->M: Loss of activity. Modification in protein
FT conformation."
FT /evidence="ECO:0000269|PubMed:10660564"
FT MUTAGEN 266
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10660564"
FT MUTAGEN 266
FT /note="K->M: Unstable; trace activity."
FT /evidence="ECO:0000269|PubMed:10660564"
FT MUTAGEN 270
FT /note="K->M: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:10660564"
FT MUTAGEN 272
FT /note="D->N,A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10551856"
FT CONFLICT 50..61
FT /note="MVLVGGEITTSA -> IGFSWRRNHHQRP (in Ref. 1 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 123..133
FT /note="MFGYATNETDV -> DVSATQLMKPTC (in Ref. 1; AAA24164)"
FT /evidence="ECO:0000305"
FT CONFLICT 159..161
FT /note="PWL -> RV (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="Q -> S (in Ref. 1; AAA24164)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="Y -> T (in Ref. 1; AAA24164)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="V -> L (in Ref. 1; AAA24164)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="Missing (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="Y -> I (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 375..376
FT /note="QL -> HV (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="R -> P (in Ref. 2)"
FT /evidence="ECO:0000305"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:1P7L"
FT HELIX 16..34
FT /evidence="ECO:0007829|PDB:1P7L"
FT STRAND 39..47
FT /evidence="ECO:0007829|PDB:1P7L"
FT STRAND 50..58
FT /evidence="ECO:0007829|PDB:1P7L"
FT HELIX 65..76
FT /evidence="ECO:0007829|PDB:1P7L"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:1P7L"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:1P7L"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:1P7L"
FT HELIX 101..107
FT /evidence="ECO:0007829|PDB:1P7L"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:1P7L"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:1MXB"
FT STRAND 121..128
FT /evidence="ECO:0007829|PDB:1P7L"
FT HELIX 137..154
FT /evidence="ECO:0007829|PDB:1P7L"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:1MXA"
FT STRAND 161..174
FT /evidence="ECO:0007829|PDB:1P7L"
FT STRAND 177..190
FT /evidence="ECO:0007829|PDB:1P7L"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:1MXA"
FT HELIX 196..206
FT /evidence="ECO:0007829|PDB:1P7L"
FT TURN 207..211
FT /evidence="ECO:0007829|PDB:1P7L"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:1P7L"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:1P7L"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:1P7L"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:1MXA"
FT TURN 247..254
FT /evidence="ECO:0007829|PDB:1P7L"
FT HELIX 271..288
FT /evidence="ECO:0007829|PDB:1P7L"
FT STRAND 291..301
FT /evidence="ECO:0007829|PDB:1P7L"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:1P7L"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:1P7L"
FT HELIX 323..333
FT /evidence="ECO:0007829|PDB:1P7L"
FT HELIX 338..345
FT /evidence="ECO:0007829|PDB:1P7L"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:1FUG"
FT HELIX 353..356
FT /evidence="ECO:0007829|PDB:1P7L"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:1P7L"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:1MXA"
FT TURN 367..369
FT /evidence="ECO:0007829|PDB:1P7L"
FT HELIX 373..379
FT /evidence="ECO:0007829|PDB:1P7L"
FT TURN 380..382
FT /evidence="ECO:0007829|PDB:1XRA"
SQ SEQUENCE 384 AA; 41952 MW; 97FA8CF17B542941 CRC64;
MAKHLFTSES VSEGHPDKIA DQISDAVLDA ILEQDPKARV ACETYVKTGM VLVGGEITTS
AWVDIEEITR NTVREIGYVH SDMGFDANSC AVLSAIGKQS PDINQGVDRA DPLEQGAGDQ
GLMFGYATNE TDVLMPAPIT YAHRLVQRQA EVRKNGTLPW LRPDAKSQVT FQYDDGKIVG
IDAVVLSTQH SEEIDQKSLQ EAVMEEIIKP ILPAEWLTSA TKFFINPTGR FVIGGPMGDC
GLTGRKIIVD TYGGMARHGG GAFSGKDPSK VDRSAAYAAR YVAKNIVAAG LADRCEIQVS
YAIGVAEPTS IMVETFGTEK VPSEQLTLLV REFFDLRPYG LIQMLDLLHP IYKETAAYGH
FGREHFPWEK TDKAQLLRDA AGLK
