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S-adenosylmethionine synthase (AdoMet synthase) (EC 2.5.1.6) (MAT) (Methionine adenosyltransferase)

 METK_ECOLI              Reviewed;         384 AA.
P0A817; P04384; P30869; Q2M9Q1;
20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 121.
RecName: Full=S-adenosylmethionine synthase {ECO:0000255|HAMAP-Rule:MF_00086};
Short=AdoMet synthase {ECO:0000255|HAMAP-Rule:MF_00086};
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};
AltName: Full=MAT {ECO:0000255|HAMAP-Rule:MF_00086};
AltName: Full=Methionine adenosyltransferase {ECO:0000255|HAMAP-Rule:MF_00086};
Name=metK {ECO:0000255|HAMAP-Rule:MF_00086}; Synonyms=metX;
OrderedLocusNames=b2942, JW2909;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6094561;
Markham G.D., Deparasis J., Gatmaitan J.;
"The sequence of metK, the structural gene for S-adenosylmethionine
synthetase in Escherichia coli.";
J. Biol. Chem. 259:14505-14507(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
STRAIN=K12;
PubMed=8231813; DOI=10.1111/j.1365-2958.1993.tb01742.x;
Satishchandran C., Taylor J.C., Markham G.D.;
"Isozymes of S-adenosylmethionine synthetase are encoded by tandemly
duplicated genes in Escherichia coli.";
Mol. Microbiol. 9:835-846(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-63.
PubMed=2198270; DOI=10.1128/jb.172.8.4631-4640.1990;
Moore R.C., Boyle S.M.;
"Nucleotide sequence and analysis of the speA gene encoding
biosynthetic arginine decarboxylase in Escherichia coli.";
J. Bacteriol. 172:4631-4640(1990).
[6]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, AND SUBUNIT.
PubMed=6251075;
Markham G.D., Hafner E.W., Tabor C.W., Tabor H.;
"S-Adenosylmethionine synthetase from Escherichia coli.";
J. Biol. Chem. 255:9082-9092(1980).
[7]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, BIOPHYSICOCHEMICAL
PROPERTIES, AND MUTAGENESIS OF GLU-43.
PubMed=7629147; DOI=10.1074/jbc.270.31.18277;
McQueney M.S., Markham G.D.;
"Investigation of monovalent cation activation of S-adenosylmethionine
synthetase using mutagenesis and uranyl inhibition.";
J. Biol. Chem. 270:18277-18284(1995).
[8]
FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, PATHWAY, AND MUTAGENESIS OF
CYS-90 AND CYS-240.
STRAIN=B, and K12;
PubMed=7629176; DOI=10.1074/jbc.270.31.18484;
Reczkowski R.S., Markham G.D.;
"Structural and functional roles of cysteine 90 and cysteine 240 in S-
adenosylmethionine synthetase.";
J. Biol. Chem. 270:18484-18490(1995).
[9]
IDENTIFICATION BY 2D-GEL.
PubMed=9298644; DOI=10.1002/elps.1150180805;
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
Neidhardt F.C.;
"Escherichia coli proteome analysis using the gene-protein database.";
Electrophoresis 18:1243-1251(1997).
[10]
FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND MUTAGENESIS OF ARG-245.
STRAIN=B, and K12;
PubMed=9753435; DOI=10.1021/bi9811011;
Reczkowski R.S., Taylor J.C., Markham G.D.;
"The active-site arginine of S-adenosylmethionine synthetase orients
the reaction intermediate.";
Biochemistry 37:13499-13506(1998).
[11]
FUNCTION, CATALYTIC ACTIVITY, PATHWAY, MUTAGENESIS OF ASP-17; ASP-119;
ASP-239 AND ASP-272, AND COFACTOR.
STRAIN=B, and K12;
PubMed=10551856; DOI=10.1074/jbc.274.46.32909;
Taylor J.C., Markham G.D.;
"The bifunctional active site of S-adenosylmethionine synthetase.
Roles of the active site aspartates.";
J. Biol. Chem. 274:32909-32914(1999).
[12]
FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBUNIT, AND MUTAGENESIS OF
HIS-15; LYS-166; LYS-246; LYS-266 AND LYS-270.
STRAIN=B, and K12;
PubMed=10660564; DOI=10.1074/jbc.275.6.4060;
Taylor J.C., Markham G.D.;
"The bifunctional active site of S-adenosylmethionine synthetase.
Roles of the basic residues.";
J. Biol. Chem. 275:4060-4065(2000).
[13]
TRANSCRIPTIONAL START SITE, AND ESSENTIAL GENE.
PubMed=11952912; DOI=10.1046/j.1365-2958.2002.02856.x;
Wei Y., Newman E.B.;
"Studies on the role of the metK gene product of Escherichia coli K-
12.";
Mol. Microbiol. 43:1651-1656(2002).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
PubMed=18723842; DOI=10.1074/mcp.M800187-MCP200;
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
Grishin N.V., Zhao Y.;
"Lysine acetylation is a highly abundant and evolutionarily conserved
modification in Escherichia coli.";
Mol. Cell. Proteomics 8:215-225(2009).
[15]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND
POTASSIUM, SUBUNIT, COFACTOR, AND MASS SPECTROMETRY.
PubMed=8550549; DOI=10.1074/jbc.271.1.136;
Takusagawa F., Kamitori S., Misaki S., Markham G.D.;
"Crystal structure of S-adenosylmethionine synthetase.";
J. Biol. Chem. 271:136-147(1996).
[16]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEXES WITH ATP ANALOGS;
MAGNESIUM AND POTASSIUM, SUBUNIT, AND COFACTOR.
PubMed=8611562; DOI=10.1021/bi952604z;
Takusagawa F., Kamitori S., Markham G.D.;
"Structure and function of S-adenosylmethionine synthetase: crystal
structures of S-adenosylmethionine synthetase with ADP, BrADP, and PPi
at 2.8-A resolution.";
Biochemistry 35:2586-2596(1996).
[17]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS), AND SUBUNIT.
PubMed=8723769; DOI=10.1080/07391102.1996.10508887;
Fu Z., Hu Y., Markham G.D., Takusagawa F.;
"Flexible loop in the structure of S-adenosylmethionine synthetase
crystallized in the tetragonal modification.";
J. Biomol. Struct. Dyn. 13:727-739(1996).
[18]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEXES WITH ATP ANALOG;
L-METHIONINE; POTASSIUM AND MAGNESIUM, SUBUNIT, AND COFACTOR.
PubMed=14967023; DOI=10.1021/bi035611t;
Komoto J., Yamada T., Takata Y., Markham G.D., Takusagawa F.;
"Crystal structure of the S-adenosylmethionine synthetase ternary
complex: a novel catalytic mechanism of S-adenosylmethionine synthesis
from ATP and Met.";
Biochemistry 43:1821-1831(2004).
-!- FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet)
from methionine and ATP. The overall synthetic reaction is
composed of two sequential steps, AdoMet formation and the
subsequent tripolyphosphate hydrolysis which occurs prior to
release of AdoMet from the enzyme (PubMed:6251075, PubMed:7629147,
PubMed:7629176, PubMed:9753435, PubMed:10551856, PubMed:10660564).
Is essential for growth (PubMed:11952912).
{ECO:0000269|PubMed:10551856, ECO:0000269|PubMed:10660564,
ECO:0000269|PubMed:11952912, ECO:0000269|PubMed:6251075,
ECO:0000269|PubMed:7629147, ECO:0000269|PubMed:7629176,
ECO:0000269|PubMed:9753435}.
-!- CATALYTIC ACTIVITY: ATP + L-methionine + H(2)O = phosphate +
diphosphate + S-adenosyl-L-methionine. {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}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_00086,
ECO:0000269|PubMed:10551856, ECO:0000269|PubMed:14967023,
ECO:0000269|PubMed:6251075, ECO:0000269|PubMed:8550549,
ECO:0000269|PubMed:8611562};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:6251075};
Name=Co(2+); Xref=ChEBI:CHEBI:48828;
Evidence={ECO:0000269|PubMed:6251075};
Note=Binds 2 divalent ions per subunit. The ions interact
primarily with the substrate. {ECO:0000244|PDB:1P7L,
ECO:0000244|PDB:1RG9, ECO:0000269|PubMed:14967023,
ECO:0000269|PubMed:8550549, ECO:0000269|PubMed:8611562,
ECO:0000305|PubMed:10551856};
-!- COFACTOR:
Name=K(+); Xref=ChEBI:CHEBI:29103;
Evidence={ECO:0000255|HAMAP-Rule:MF_00086,
ECO:0000269|PubMed:14967023, ECO:0000269|PubMed:6251075,
ECO:0000269|PubMed:7629147, ECO:0000269|PubMed:8550549,
ECO:0000269|PubMed:8611562};
Note=Binds 1 potassium ion per subunit. The potassium ion
interacts primarily with the substrate. {ECO:0000244|PDB:1P7L,
ECO:0000244|PDB:1RG9, ECO:0000269|PubMed:14967023,
ECO:0000269|PubMed:7629147, ECO:0000269|PubMed:8550549,
ECO:0000269|PubMed:8611562};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=3.0 mM for Mg(2+) {ECO:0000269|PubMed:7629147};
KM=0.11 mM for ATP {ECO:0000269|PubMed:7629147};
KM=0.08 mM for L-methionine {ECO:0000269|PubMed:7629147};
-!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine
biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
{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}.
-!- SUBUNIT: Homotetramer; dimer of dimers (PubMed:6251075,
PubMed:7629147, PubMed:7629176, PubMed:10660564, PubMed:8550549,
PubMed:8611562, PubMed:8723769, PubMed:14967023). The active sites
are at the interface between subunits; each dimer has two active
sites (PubMed:8550549, PubMed:8611562, PubMed:8723769,
PubMed:14967023). {ECO:0000269|PubMed:10660564,
ECO:0000269|PubMed:14967023, ECO:0000269|PubMed:6251075,
ECO:0000269|PubMed:7629176, ECO:0000269|PubMed:8550549,
ECO:0000269|PubMed:8611562, ECO:0000269|PubMed:8723769}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-546295, EBI-546295;
P0A6F5:groL; NbExp=2; IntAct=EBI-546295, EBI-543750;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00086}.
-!- INDUCTION: AdoMet activates the tripolyphosphatase reaction.
-!- MASS SPECTROMETRY: Mass=41843; Mass_error=10.5;
Method=Electrospray; Range=2-384;
Evidence={ECO:0000269|PubMed:8550549};
-!- DISRUPTION PHENOTYPE: Cells are resistant to methionine-analogs,
such as DL-ethionine(Et). {ECO:0000269|PubMed:8231813}.
-!- SIMILARITY: Belongs to the AdoMet synthase family.
{ECO:0000255|HAMAP-Rule:MF_00086}.
-!- CAUTION: Was originally thought to differ from MetX, which was
assigned as a second AdoMet synthase before being shown to be
identical to MetK. {ECO:0000305|PubMed:8231813}.
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EMBL; K02129; AAA24164.1; -; Genomic_DNA.
EMBL; U28377; AAA69109.1; -; Genomic_DNA.
EMBL; U00096; AAC75979.1; -; Genomic_DNA.
EMBL; AP009048; BAE77005.1; -; Genomic_DNA.
EMBL; M98266; AAB05197.1; -; Genomic_DNA.
EMBL; M31770; AAA24645.2; -; Genomic_DNA.
PIR; E65079; SYECSM.
RefSeq; NP_417417.1; NC_000913.3.
RefSeq; WP_001062128.1; NZ_LN832404.1.
PDB; 1FUG; X-ray; 3.20 A; A/B=2-384.
PDB; 1MXA; X-ray; 2.80 A; A=2-384.
PDB; 1MXB; X-ray; 2.80 A; A=2-384.
PDB; 1MXC; X-ray; 3.00 A; A=2-384.
PDB; 1P7L; X-ray; 2.50 A; A/B/C/D=2-384.
PDB; 1RG9; X-ray; 2.50 A; A/B/C/D=2-384.
PDB; 1XRA; X-ray; 3.00 A; A=2-384.
PDB; 1XRB; X-ray; 3.00 A; A=2-384.
PDB; 1XRC; X-ray; 3.00 A; A=2-384.
PDBsum; 1FUG; -.
PDBsum; 1MXA; -.
PDBsum; 1MXB; -.
PDBsum; 1MXC; -.
PDBsum; 1P7L; -.
PDBsum; 1RG9; -.
PDBsum; 1XRA; -.
PDBsum; 1XRB; -.
PDBsum; 1XRC; -.
ProteinModelPortal; P0A817; -.
SMR; P0A817; -.
BioGrid; 4260657; 210.
DIP; DIP-35672N; -.
IntAct; P0A817; 39.
MINT; MINT-1233798; -.
STRING; 316385.ECDH10B_3117; -.
iPTMnet; P0A817; -.
SWISS-2DPAGE; P0A817; -.
PaxDb; P0A817; -.
PRIDE; P0A817; -.
EnsemblBacteria; AAC75979; AAC75979; b2942.
EnsemblBacteria; BAE77005; BAE77005; BAE77005.
GeneID; 945389; -.
KEGG; ecj:JW2909; -.
KEGG; eco:b2942; -.
PATRIC; fig|1411691.4.peg.3791; -.
EchoBASE; EB0584; -.
EcoGene; EG10589; metK.
eggNOG; ENOG4105CPH; Bacteria.
eggNOG; COG0192; LUCA.
HOGENOM; HOG000245710; -.
InParanoid; P0A817; -.
KO; K00789; -.
PhylomeDB; P0A817; -.
BioCyc; EcoCyc:S-ADENMETSYN-MONOMER; -.
BioCyc; MetaCyc:S-ADENMETSYN-MONOMER; -.
BRENDA; 2.5.1.6; 2026.
SABIO-RK; P0A817; -.
UniPathway; UPA00315; UER00080.
EvolutionaryTrace; P0A817; -.
PRO; PR:P0A817; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
GO; GO:0004478; F:methionine adenosyltransferase activity; IDA:EcoCyc.
GO; GO:0030955; F:potassium ion binding; IDA:EcoCyc.
GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IMP:EcoCyc.
GO; GO:0033353; P:S-adenosylmethionine cycle; IMP:GO_Central.
HAMAP; MF_00086; S_AdoMet_synth1; 1.
InterPro; IPR022631; ADOMET_SYNTHASE_CS.
InterPro; IPR022630; S-AdoMet_synt_C.
InterPro; IPR022629; S-AdoMet_synt_central.
InterPro; IPR022628; S-AdoMet_synt_N.
InterPro; IPR002133; S-AdoMet_synthetase.
InterPro; IPR022636; S-AdoMet_synthetase_sfam.
PANTHER; PTHR11964; PTHR11964; 1.
Pfam; PF02773; S-AdoMet_synt_C; 1.
Pfam; PF02772; S-AdoMet_synt_M; 1.
Pfam; PF00438; S-AdoMet_synt_N; 1.
PIRSF; PIRSF000497; MAT; 1.
SUPFAM; SSF55973; SSF55973; 3.
TIGRFAMs; TIGR01034; metK; 1.
PROSITE; PS00376; ADOMET_SYNTHASE_1; 1.
PROSITE; PS00377; ADOMET_SYNTHASE_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Cobalt; Complete proteome;
Cytoplasm; Magnesium; Manganese; Metal-binding; Nucleotide-binding;
One-carbon metabolism; Potassium; Reference proteome; Transferase.
INIT_MET 1 1 Removed.
CHAIN 2 384 S-adenosylmethionine synthase.
/FTId=PRO_0000174518.
NP_BIND 164 166 ATP. {ECO:0000244|PDB:1P7L,
ECO:0000244|PDB:1RG9, ECO:0000255|HAMAP-
Rule:MF_00086,
ECO:0000269|PubMed:14967023}.
NP_BIND 230 231 ATP. {ECO:0000244|PDB:1P7L,
ECO:0000244|PDB:1RG9, ECO:0000255|HAMAP-
Rule:MF_00086,
ECO:0000269|PubMed:14967023}.
NP_BIND 245 246 ATP. {ECO:0000244|PDB:1P7L,
ECO:0000244|PDB:1RG9, ECO:0000255|HAMAP-
Rule:MF_00086,
ECO:0000269|PubMed:14967023}.
REGION 99 109 Flexible loop. {ECO:0000255|HAMAP-
Rule:MF_00086,
ECO:0000269|PubMed:14967023}.
METAL 17 17 Magnesium. {ECO:0000244|PDB:1P7L,
ECO:0000244|PDB:1RG9, ECO:0000255|HAMAP-
Rule:MF_00086,
ECO:0000269|PubMed:14967023}.
METAL 43 43 Potassium. {ECO:0000244|PDB:1MXC,
ECO:0000244|PDB:1P7L,
ECO:0000244|PDB:1RG9, ECO:0000255|HAMAP-
Rule:MF_00086,
ECO:0000269|PubMed:14967023,
ECO:0000305|PubMed:7629147}.
BINDING 15 15 ATP. {ECO:0000244|PDB:1P7L,
ECO:0000244|PDB:1RG9, ECO:0000255|HAMAP-
Rule:MF_00086,
ECO:0000269|PubMed:14967023}.
BINDING 56 56 Methionine. {ECO:0000244|PDB:1P7L,
ECO:0000244|PDB:1RG9, ECO:0000255|HAMAP-
Rule:MF_00086,
ECO:0000269|PubMed:14967023}.
BINDING 99 99 Methionine. {ECO:0000244|PDB:1P7L,
ECO:0000244|PDB:1RG9, ECO:0000255|HAMAP-
Rule:MF_00086,
ECO:0000269|PubMed:14967023}.
BINDING 239 239 ATP; shared with neighboring subunit.
{ECO:0000244|PDB:1RG9, ECO:0000255|HAMAP-
Rule:MF_00086,
ECO:0000269|PubMed:14967023}.
BINDING 239 239 Methionine; shared with neighboring
subunit. {ECO:0000244|PDB:1P7L,
ECO:0000255|HAMAP-Rule:MF_00086,
ECO:0000269|PubMed:14967023}.
BINDING 262 262 ATP; via amide nitrogen; shared with
neighboring subunit.
{ECO:0000244|PDB:1P7L,
ECO:0000244|PDB:1RG9, ECO:0000255|HAMAP-
Rule:MF_00086,
ECO:0000269|PubMed:14967023}.
BINDING 266 266 ATP; shared with neighboring subunit.
{ECO:0000244|PDB:1P7L,
ECO:0000244|PDB:1RG9, ECO:0000255|HAMAP-
Rule:MF_00086,
ECO:0000269|PubMed:14967023}.
BINDING 270 270 Methionine. {ECO:0000244|PDB:1P7L,
ECO:0000244|PDB:1RG9, ECO:0000255|HAMAP-
Rule:MF_00086,
ECO:0000269|PubMed:14967023}.
MOD_RES 3 3 N6-acetyllysine.
{ECO:0000269|PubMed:18723842}.
MUTAGEN 15 15 H->N: Loss of activity.
{ECO:0000269|PubMed:10660564}.
MUTAGEN 17 17 D->N,A: Loss of activity.
{ECO:0000269|PubMed:10551856}.
MUTAGEN 43 43 E->K: Misfolding and subject to
proteolytic degradation.
{ECO:0000269|PubMed:7629147}.
MUTAGEN 43 43 E->Q: Nearly abolishes enzyme activity.
Abolishes stimulation of enzyme activity
by potassium.
{ECO:0000269|PubMed:7629147}.
MUTAGEN 90 90 C->A,S: Decrease in the homotetramer
formation capability. Enhanced thermal
stability. {ECO:0000269|PubMed:7629176}.
MUTAGEN 119 119 D->N: Decrease of both AdoMet synthesis
and AdoMet-activated tripolyphosphate
hydrolysis.
{ECO:0000269|PubMed:10551856}.
MUTAGEN 166 166 K->M: Decrease in AdoMet synthesis.
{ECO:0000269|PubMed:10660564}.
MUTAGEN 239 239 D->N: Decrease in AdoMet synthesis.
{ECO:0000269|PubMed:10551856}.
MUTAGEN 240 240 C->A: Decrease in AdoMet synthesis.
{ECO:0000269|PubMed:7629176}.
MUTAGEN 245 245 R->H,L: Loss of activity.
{ECO:0000269|PubMed:9753435}.
MUTAGEN 246 246 K->M: Loss of activity. Modification in
protein conformation.
{ECO:0000269|PubMed:10660564}.
MUTAGEN 266 266 K->A: Loss of activity.
{ECO:0000269|PubMed:10660564}.
MUTAGEN 266 266 K->M: Unstable; trace activity.
{ECO:0000269|PubMed:10660564}.
MUTAGEN 270 270 K->M: Decrease in activity.
{ECO:0000269|PubMed:10660564}.
MUTAGEN 272 272 D->N,A: Loss of activity.
{ECO:0000269|PubMed:10551856}.
CONFLICT 50 61 MVLVGGEITTSA -> IGFSWRRNHHQRP (in Ref. 1
and 5). {ECO:0000305}.
CONFLICT 123 133 MFGYATNETDV -> DVSATQLMKPTC (in Ref. 1;
AAA24164). {ECO:0000305}.
CONFLICT 159 161 PWL -> RV (in Ref. 1 and 2).
{ECO:0000305}.
CONFLICT 172 172 Q -> S (in Ref. 1; AAA24164).
{ECO:0000305}.
CONFLICT 252 252 Y -> T (in Ref. 1; AAA24164).
{ECO:0000305}.
CONFLICT 305 305 V -> L (in Ref. 1; AAA24164).
{ECO:0000305}.
CONFLICT 337 337 Missing (in Ref. 1). {ECO:0000305}.
CONFLICT 339 339 Y -> I (in Ref. 1). {ECO:0000305}.
CONFLICT 375 376 QL -> HV (in Ref. 2). {ECO:0000305}.
CONFLICT 378 378 R -> P (in Ref. 2). {ECO:0000305}.
STRAND 4 11 {ECO:0000244|PDB:1P7L}.
HELIX 16 34 {ECO:0000244|PDB:1P7L}.
STRAND 39 47 {ECO:0000244|PDB:1P7L}.
STRAND 50 58 {ECO:0000244|PDB:1P7L}.
HELIX 65 76 {ECO:0000244|PDB:1P7L}.
HELIX 81 83 {ECO:0000244|PDB:1P7L}.
TURN 87 89 {ECO:0000244|PDB:1P7L}.
STRAND 90 97 {ECO:0000244|PDB:1P7L}.
HELIX 101 107 {ECO:0000244|PDB:1P7L}.
TURN 112 114 {ECO:0000244|PDB:1P7L}.
STRAND 117 119 {ECO:0000244|PDB:1MXB}.
STRAND 121 128 {ECO:0000244|PDB:1P7L}.
HELIX 137 154 {ECO:0000244|PDB:1P7L}.
STRAND 156 158 {ECO:0000244|PDB:1MXA}.
STRAND 161 174 {ECO:0000244|PDB:1P7L}.
STRAND 177 190 {ECO:0000244|PDB:1P7L}.
STRAND 192 194 {ECO:0000244|PDB:1MXA}.
HELIX 196 206 {ECO:0000244|PDB:1P7L}.
TURN 207 211 {ECO:0000244|PDB:1P7L}.
HELIX 214 216 {ECO:0000244|PDB:1P7L}.
STRAND 222 226 {ECO:0000244|PDB:1P7L}.
HELIX 235 238 {ECO:0000244|PDB:1P7L}.
STRAND 239 242 {ECO:0000244|PDB:1MXA}.
TURN 247 254 {ECO:0000244|PDB:1P7L}.
HELIX 271 288 {ECO:0000244|PDB:1P7L}.
STRAND 291 301 {ECO:0000244|PDB:1P7L}.
STRAND 309 314 {ECO:0000244|PDB:1P7L}.
STRAND 319 321 {ECO:0000244|PDB:1P7L}.
HELIX 323 333 {ECO:0000244|PDB:1P7L}.
HELIX 338 345 {ECO:0000244|PDB:1P7L}.
STRAND 348 350 {ECO:0000244|PDB:1FUG}.
HELIX 353 356 {ECO:0000244|PDB:1P7L}.
STRAND 360 362 {ECO:0000244|PDB:1P7L}.
STRAND 364 366 {ECO:0000244|PDB:1MXA}.
TURN 367 369 {ECO:0000244|PDB:1P7L}.
HELIX 373 379 {ECO:0000244|PDB:1P7L}.
TURN 380 382 {ECO:0000244|PDB:1XRA}.
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


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