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4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7)

 DAPA_ECOLI              Reviewed;         292 AA.
P0A6L2; P05640; P78223;
10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
10-MAY-2005, sequence version 1.
28-MAR-2018, entry version 119.
RecName: Full=4-hydroxy-tetrahydrodipicolinate synthase {ECO:0000255|HAMAP-Rule:MF_00418};
Short=HTPA synthase {ECO:0000255|HAMAP-Rule:MF_00418};
EC=4.3.3.7 {ECO:0000255|HAMAP-Rule:MF_00418};
Name=dapA {ECO:0000255|HAMAP-Rule:MF_00418};
OrderedLocusNames=b2478, JW2463;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3514578; DOI=10.1128/jb.166.1.297-300.1986;
Richaud F., Richaud C., Ratet P., Patte J.-C.;
"Chromosomal location and nucleotide sequence of the Escherichia coli
dapA gene.";
J. Bacteriol. 166:297-300(1986).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9205837; DOI=10.1093/dnares/4.2.91;
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K.,
Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N.,
Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H.,
Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S.,
Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C.,
Yamagata S., Horiuchi T.;
"Construction of a contiguous 874-kb sequence of the Escherichia coli-
K12 genome corresponding to 50.0-68.8 min on the linkage map and
analysis of its sequence features.";
DNA Res. 4:91-113(1997).
[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]
PROTEIN SEQUENCE OF 1-11.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.;
Submitted (FEB-1996) to UniProtKB.
[6]
PROTEIN SEQUENCE OF 1-12.
STRAIN=K12 / EMG2;
PubMed=9298646; DOI=10.1002/elps.1150180807;
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded
in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[7]
PROTEIN SEQUENCE OF 1-4.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M.,
Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D.,
Williams K.L., Hochstrasser D.F.;
"Protein identification with N and C-terminal sequence tags in
proteome projects.";
J. Mol. Biol. 278:599-608(1998).
[8]
PROTEIN SEQUENCE OF 156-167, AND ACTIVE SITE.
PubMed=1463470; DOI=10.1042/bj2880691;
Laber B., Gomis-Rueth F.-X., Romao M.J., Huber R.;
"Escherichia coli dihydrodipicolinate synthase. Identification of the
active site and crystallization.";
Biochem. J. 288:691-695(1992).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 288-292.
STRAIN=K12;
PubMed=2120198; DOI=10.1128/jb.172.10.6035-6041.1990;
Tiedemann A.A., Demarini D.J., Parker J., Smith J.M.;
"DNA sequence of the purC gene encoding 5'-phosphoribosyl-5-
aminoimidazole-4-N-succinocarboxamide synthetase and organization of
the dapA-purC region of Escherichia coli K-12.";
J. Bacteriol. 172:6035-6041(1990).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 288-292.
STRAIN=K12;
PubMed=1885529; DOI=10.1128/jb.173.17.5523-5531.1991;
Bouvier J., Pugsley A.P., Stragier P.;
"A gene for a new lipoprotein in the dapA-purC interval of the
Escherichia coli chromosome.";
J. Bacteriol. 173:5523-5531(1991).
[11]
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).
[12]
ENZYME REGULATION.
PubMed=9048556; DOI=10.1021/bi962264x;
Karsten W.E.;
"Dihydrodipicolinate synthase from Escherichia coli: pH dependent
changes in the kinetic mechanism and kinetic mechanism of allosteric
inhibition by L-lysine.";
Biochemistry 36:1730-1739(1997).
[13]
ENZYME REGULATION, KINETIC PARAMETERS, AND MASS SPECTROMETRY.
PubMed=14580236; DOI=10.1042/BJ20031389;
Dobson R.C., Gerrard J.A., Pearce F.G.;
"Dihydrodipicolinate synthase is not inhibited by its substrate, (S)-
aspartate beta-semialdehyde.";
Biochem. J. 377:757-762(2004).
[14]
SYNTHETIC INHIBITORS.
PubMed=18977662; DOI=10.1016/j.bmc.2008.10.026;
Boughton B.A., Griffin M.D., O'Donnell P.A., Dobson R.C.,
Perugini M.A., Gerrard J.A., Hutton C.A.;
"Irreversible inhibition of dihydrodipicolinate synthase by 4-oxo-
heptenedioic acid analogues.";
Bioorg. Med. Chem. 16:9975-9983(2008).
[15]
FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION OF HTPA AS REACTION
PRODUCT, AND SUBSTRATE SPECIFICITY.
PubMed=20503968; DOI=10.1021/jm100349s;
Devenish S.R., Blunt J.W., Gerrard J.A.;
"NMR studies uncover alternate substrates for dihydrodipicolinate
synthase and suggest that dihydrodipicolinate reductase is also a
dehydratase.";
J. Med. Chem. 53:4808-4812(2010).
[16]
SYNTHETIC INHIBITORS.
PubMed=22386717; DOI=10.1016/j.bmc.2012.01.045;
Boughton B.A., Hor L., Gerrard J.A., Hutton C.A.;
"1,3-Phenylene bis(ketoacid) derivatives as inhibitors of Escherichia
coli dihydrodipicolinate synthase.";
Bioorg. Med. Chem. 20:2419-2426(2012).
[17]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=7853400; DOI=10.1006/jmbi.1994.0078;
Mirwaldt C., Korndoerfer I., Huber R.;
"The crystal structure of dihydrodipicolinate synthase from
Escherichia coli at 2.5-A resolution.";
J. Mol. Biol. 246:227-239(1995).
[18]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
IDENTIFICATION OF HTPA AS REACTION PRODUCT, AND CATALYTIC MECHANISM.
PubMed=8993314; DOI=10.1021/bi962272d;
Blicking S., Renner C., Laber B., Pohlenz H.-D., Holak T.A., Huber R.;
"Reaction mechanism of Escherichia coli dihydrodipicolinate synthase
investigated by X-ray crystallography and NMR spectroscopy.";
Biochemistry 36:24-33(1997).
[19]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF MUTANTS VAL-44; PHE-107 AND
PHE-133, KINETIC PARAMETERS, MUTAGENESIS OF THR-44; TYR-107 AND
TYR-133, AND REACTION MECHANISM.
PubMed=15066435; DOI=10.1016/j.jmb.2004.02.060;
Dobson R.C.J., Valegaard K., Gerrard J.A.;
"The crystal structure of three site-directed mutants of Escherichia
coli dihydrodipicolinate synthase: further evidence for a catalytic
triad.";
J. Mol. Biol. 338:329-339(2004).
[20]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH
ALLOSTERIC INHIBITOR (S)-LYSINE, AND SUBUNIT.
PubMed=16041077; DOI=10.1107/S0907444905016318;
Dobson R.C.J., Griffin M.D.W., Jameson G.B., Gerrard J.A.;
"The crystal structures of native and (S)-lysine-bound
dihydrodipicolinate synthase from Escherichia coli with improved
resolution show new features of biological significance.";
Acta Crystallogr. D 61:1116-1124(2005).
[21]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF MUTANTS ALA-138 AND HIS-138,
AND MUTAGENESIS OF ARG-138.
PubMed=16185069; DOI=10.1021/bi051281w;
Dobson R.C.J., Devenish S.R.A., Turner L.A., Clifford V.R.,
Pearce F.G., Jameson G.B., Gerrard J.A.;
"Role of arginine 138 in the catalysis and regulation of Escherichia
coli dihydrodipicolinate synthase.";
Biochemistry 44:13007-13013(2005).
[22]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH LYSINE
INHIBITOR.
Devenish S.R.A., Dobson R.C.J., Jameson G.B., Gerrard J.A.;
"The co-crystallisation of (S)-lysine-bound dihydrodipicolinate
synthase from E. coli indicates that domain movements are not
responsible for (S)-lysine inhibition.";
Submitted (AUG-2005) to the PDB data bank.
[23]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
PubMed=19052357; DOI=10.1107/S1744309108033654;
Devenish S.R., Gerrard J.A., Jameson G.B., Dobson R.C.;
"The high-resolution structure of dihydrodipicolinate synthase from
Escherichia coli bound to its first substrate, pyruvate.";
Acta Crystallogr. F 64:1092-1095(2008).
[24]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF MUTANT TRP-107, SUBUNIT, AND
MUTAGENESIS OF TYR-107.
PubMed=18937497; DOI=10.1021/bi801094t;
Pearce F.G., Dobson R.C., Weber A., Lane L.A., McCammon M.G.,
Squire M.A., Perugini M.A., Jameson G.B., Robinson C.V., Gerrard J.A.;
"Mutating the tight-dimer interface of dihydrodipicolinate synthase
disrupts the enzyme quaternary structure: toward a monomeric enzyme.";
Biochemistry 47:12108-12117(2008).
[25]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF MUTANT TYR-197, SUBUNIT, AND
MUTAGENESIS OF LEU-197.
PubMed=18556019; DOI=10.1016/j.jmb.2008.05.038;
Griffin M.D., Dobson R.C., Pearce F.G., Antonio L., Whitten A.E.,
Liew C.K., Mackay J.P., Trewhella J., Jameson G.B., Perugini M.A.,
Gerrard J.A.;
"Evolution of quaternary structure in a homotetrameric enzyme.";
J. Mol. Biol. 380:691-703(2008).
[26]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS), ENZYME REGULATION, AND MASS
SPECTROMETRY.
PubMed=18787203; DOI=10.1110/ps.037440.108;
Dobson R.C., Griffin M.D., Devenish S.R., Pearce F.G., Hutton C.A.,
Gerrard J.A., Jameson G.B., Perugini M.A.;
"Conserved main-chain peptide distortions: a proposed role for Ile203
in catalysis by dihydrodipicolinate synthase.";
Protein Sci. 17:2080-2090(2008).
[27]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF MUTANT SER-44, MUTAGENESIS
OF THR-44, ACTIVE SITES, AND REACTION MECHANISM.
PubMed=19505526; DOI=10.1016/j.biochi.2009.05.013;
Dobson R.C., Perugini M.A., Jameson G.B., Gerrard J.A.;
"Specificity versus catalytic potency: The role of threonine 44 in
Escherichia coli dihydrodipicolinate synthase mediated catalysis.";
Biochimie 91:1036-1044(2009).
[28]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF MUTANTS ALA-161 AND ARG-161
OF NATIVE PROTEIN AND IN COMPLEX WITH PYRUVATE, AND MUTAGENESIS OF
LYS-161.
PubMed=20353808; DOI=10.1016/j.biochi.2010.03.004;
Soares da Costa T.P., Muscroft-Taylor A.C., Dobson R.C.,
Devenish S.R., Jameson G.B., Gerrard J.A.;
"How essential is the 'essential' active-site lysine in
dihydrodipicolinate synthase?";
Biochimie 92:837-845(2010).
[29]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH PYRUVATE AND
SUBSTRATE ANALOG INHIBITOR.
PubMed=22552955; DOI=10.1002/prot.24106;
Boughton B.A., Dobson R.C., Hutton C.A.;
"The crystal structure of dihydrodipicolinate synthase from
Escherichia coli with bound pyruvate and succinic acid semialdehyde:
unambiguous resolution of the stereochemistry of the condensation
product.";
Proteins 80:2117-2122(2012).
-!- FUNCTION: Catalyzes the condensation of (S)-aspartate-beta-
semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-
tetrahydrodipicolinate (HTPA). {ECO:0000255|HAMAP-Rule:MF_00418,
ECO:0000269|PubMed:20503968, ECO:0000269|PubMed:8993314}.
-!- CATALYTIC ACTIVITY: Pyruvate + L-aspartate-4-semialdehyde = (4S)-
4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate + H(2)O.
{ECO:0000255|HAMAP-Rule:MF_00418, ECO:0000269|PubMed:20503968,
ECO:0000269|PubMed:8993314}.
-!- ENZYME REGULATION: Is allosterically regulated by the feedback
inhibitor (S)-lysine. Is inhibited by pyruvate analogs such as 3-
fluoropyruvate, 2-ketobutyrate, glyoxylate, and beta-
hydroxypyruvate. Is not inhibited by its substrate, (S)-ASA.
{ECO:0000269|PubMed:14580236, ECO:0000269|PubMed:18787203,
ECO:0000269|PubMed:9048556}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.26 mM for pyruvate {ECO:0000269|PubMed:14580236,
ECO:0000269|PubMed:15066435};
KM=0.11 mM for L-aspartate-4-semialdehyde
{ECO:0000269|PubMed:14580236, ECO:0000269|PubMed:15066435};
Vmax=0.58 umol/sec/mg enzyme {ECO:0000269|PubMed:14580236,
ECO:0000269|PubMed:15066435};
Note=kcat is 124 sec(-1).;
-!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
{ECO:0000255|HAMAP-Rule:MF_00418}.
-!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000255|HAMAP-
Rule:MF_00418, ECO:0000269|PubMed:16041077,
ECO:0000269|PubMed:18556019, ECO:0000269|PubMed:18937497,
ECO:0000269|PubMed:20353808, ECO:0000269|PubMed:22552955,
ECO:0000269|Ref.22}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-907527, EBI-907527;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- MASS SPECTROMETRY: Mass=31272; Mass_error=1; Method=Electrospray;
Range=1-292; Evidence={ECO:0000269|PubMed:14580236};
-!- MASS SPECTROMETRY: Mass=31270; Method=Electrospray; Range=1-292;
Evidence={ECO:0000269|PubMed:18787203};
-!- SIMILARITY: Belongs to the DapA family. {ECO:0000255|HAMAP-
Rule:MF_00418}.
-!- CAUTION: Was originally thought to be a dihydrodipicolinate
synthase (DHDPS), catalyzing the condensation of (S)-aspartate-
beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate
(DHDP). However, it was shown that the product of the enzymatic
reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-
2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the
consecutive dehydration reaction leading to DHDP is not
spontaneous but catalyzed by DapB (PubMed:8993314,
PubMed:20503968). {ECO:0000305|PubMed:20503968,
ECO:0000305|PubMed:8993314}.
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EMBL; M12844; AAA23665.1; -; Genomic_DNA.
EMBL; U00096; AAC75531.1; -; Genomic_DNA.
EMBL; AP009048; BAA16355.1; -; Genomic_DNA.
EMBL; M33928; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X57402; CAA40660.1; -; Genomic_DNA.
PIR; E65023; SYECDP.
RefSeq; NP_416973.1; NC_000913.3.
RefSeq; WP_001311023.1; NZ_LN832404.1.
PDB; 1DHP; X-ray; 2.30 A; A/B=1-292.
PDB; 1S5T; X-ray; 2.30 A; A/B=1-292.
PDB; 1S5V; X-ray; 2.35 A; A/B=1-292.
PDB; 1S5W; X-ray; 2.32 A; A/B=1-292.
PDB; 1YXC; X-ray; 1.90 A; A/B=1-292.
PDB; 1YXD; X-ray; 2.00 A; A/B=1-292.
PDB; 2A6L; X-ray; 2.05 A; A/B=1-292.
PDB; 2A6N; X-ray; 1.94 A; A/B=1-292.
PDB; 2ATS; X-ray; 1.90 A; A/B=1-292.
PDB; 2OJP; X-ray; 1.70 A; A/B=1-292.
PDB; 2PUR; X-ray; 1.70 A; A/B=1-292.
PDB; 3C0J; X-ray; 2.40 A; A/B=1-292.
PDB; 3DEN; X-ray; 2.20 A; A/B=1-292.
PDB; 3DU0; X-ray; 2.00 A; A/B=1-292.
PDB; 3I7Q; X-ray; 2.00 A; A/B=1-292.
PDB; 3I7R; X-ray; 2.10 A; A/B=1-292.
PDB; 3I7S; X-ray; 2.30 A; A/B=1-292.
PDB; 4EOU; X-ray; 2.30 A; A/B=1-292.
PDB; 5T25; X-ray; 1.99 A; A/B=1-292.
PDB; 5T26; X-ray; 2.10 A; A/B=1-292.
PDBsum; 1DHP; -.
PDBsum; 1S5T; -.
PDBsum; 1S5V; -.
PDBsum; 1S5W; -.
PDBsum; 1YXC; -.
PDBsum; 1YXD; -.
PDBsum; 2A6L; -.
PDBsum; 2A6N; -.
PDBsum; 2ATS; -.
PDBsum; 2OJP; -.
PDBsum; 2PUR; -.
PDBsum; 3C0J; -.
PDBsum; 3DEN; -.
PDBsum; 3DU0; -.
PDBsum; 3I7Q; -.
PDBsum; 3I7R; -.
PDBsum; 3I7S; -.
PDBsum; 4EOU; -.
PDBsum; 5T25; -.
PDBsum; 5T26; -.
ProteinModelPortal; P0A6L2; -.
SMR; P0A6L2; -.
BioGrid; 4261968; 55.
IntAct; P0A6L2; 3.
STRING; 316385.ECDH10B_2644; -.
BindingDB; P0A6L2; -.
ChEMBL; CHEMBL4083; -.
SWISS-2DPAGE; P0A6L2; -.
EPD; P0A6L2; -.
PaxDb; P0A6L2; -.
PRIDE; P0A6L2; -.
EnsemblBacteria; AAC75531; AAC75531; b2478.
EnsemblBacteria; BAA16355; BAA16355; BAA16355.
GeneID; 946952; -.
KEGG; ecj:JW2463; -.
KEGG; eco:b2478; -.
PATRIC; fig|1411691.4.peg.4261; -.
EchoBASE; EB0201; -.
EcoGene; EG10205; dapA.
eggNOG; ENOG4105CDP; Bacteria.
eggNOG; COG0329; LUCA.
HOGENOM; HOG000173604; -.
InParanoid; P0A6L2; -.
KO; K01714; -.
OMA; GMDACVP; -.
PhylomeDB; P0A6L2; -.
BioCyc; EcoCyc:DIHYDRODIPICSYN-MONOMER; -.
BioCyc; MetaCyc:DIHYDRODIPICSYN-MONOMER; -.
BRENDA; 4.3.3.7; 2026.
SABIO-RK; P0A6L2; -.
UniPathway; UPA00034; UER00017.
EvolutionaryTrace; P0A6L2; -.
PRO; PR:P0A6L2; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase; IDA:EcoCyc.
GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
GO; GO:0019877; P:diaminopimelate biosynthetic process; IDA:EcoliWiki.
GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
CDD; cd00950; DHDPS; 1.
Gene3D; 3.20.20.70; -; 1.
HAMAP; MF_00418; DapA; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR005263; DapA.
InterPro; IPR002220; DapA-like.
InterPro; IPR020625; Schiff_base-form_aldolases_AS.
InterPro; IPR020624; Schiff_base-form_aldolases_CS.
PANTHER; PTHR12128; PTHR12128; 1.
Pfam; PF00701; DHDPS; 1.
PIRSF; PIRSF001365; DHDPS; 1.
PRINTS; PR00146; DHPICSNTHASE.
SMART; SM01130; DHDPS; 1.
TIGRFAMs; TIGR00674; dapA; 1.
PROSITE; PS00665; DHDPS_1; 1.
PROSITE; PS00666; DHDPS_2; 1.
1: Evidence at protein level;
3D-structure; Allosteric enzyme; Amino-acid biosynthesis;
Complete proteome; Cytoplasm; Diaminopimelate biosynthesis;
Direct protein sequencing; Lyase; Lysine biosynthesis;
Reference proteome; Schiff base.
CHAIN 1 292 4-hydroxy-tetrahydrodipicolinate
synthase.
/FTId=PRO_0000103110.
ACT_SITE 133 133 Proton donor/acceptor.
ACT_SITE 161 161 Schiff-base intermediate with substrate.
BINDING 45 45 Pyruvate. {ECO:0000255|HAMAP-
Rule:MF_00418,
ECO:0000269|PubMed:20353808,
ECO:0000269|PubMed:22552955}.
BINDING 203 203 Pyruvate; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_00418,
ECO:0000269|PubMed:20353808,
ECO:0000269|PubMed:22552955}.
SITE 44 44 Part of a proton relay during catalysis.
SITE 49 49 L-lysine inhibitor binding; via carbonyl
oxygen.
SITE 80 80 L-lysine inhibitor binding.
SITE 84 84 L-lysine inhibitor binding.
SITE 106 106 L-lysine inhibitor binding.
SITE 107 107 Part of a proton relay during catalysis.
MUTAGEN 44 44 T->S: 8% of wild-type activity. 4-fold
decrease in affinity for pyruvate, but
nearly no change in that for (S)-ASA.
{ECO:0000269|PubMed:15066435,
ECO:0000269|PubMed:19505526}.
MUTAGEN 44 44 T->V: Reduced kcat by 99.9%.
{ECO:0000269|PubMed:15066435,
ECO:0000269|PubMed:19505526}.
MUTAGEN 107 107 Y->F: Reduced kcat by 90%.
{ECO:0000269|PubMed:15066435,
ECO:0000269|PubMed:18937497}.
MUTAGEN 107 107 Y->W: Reduced activity by 95%. Reduced
affinity for both substrates. Exists as a
mixture of monomer, dimer and tetramer in
solution. Has significantly lower thermal
stability than the wild-type enzyme.
{ECO:0000269|PubMed:15066435,
ECO:0000269|PubMed:18937497}.
MUTAGEN 133 133 Y->F: Reduced kcat by 99.7%. Reduced
affinity for both substrates.
{ECO:0000269|PubMed:15066435}.
MUTAGEN 138 138 R->A,H: Strongly increased KM for L-
aspartate 4-semialdehyde. No effect on KM
for pyruvate. Reduced activity by 99.7%.
{ECO:0000269|PubMed:16185069}.
MUTAGEN 161 161 K->A: 0.1% of wild-type activity. 3-fold
decrease in affinity for pyruvate, and 2-
fold decrease in that for (S)-ASA.
{ECO:0000269|PubMed:20353808}.
MUTAGEN 161 161 K->R: 0.35% of wild-type activity. 3-fold
decrease in affinity for pyruvate, but
nearly no change in that for (S)-ASA.
{ECO:0000269|PubMed:20353808}.
MUTAGEN 197 197 L->Y,D: 1.4 to 2.5% of wild-type
activity. Decrease in affinity for
pyruvate, but nearly no change in that
for (S)-ASA. Exists as a dimer in
solution. {ECO:0000269|PubMed:18556019}.
CONFLICT 207 207 A -> T (in Ref. 1; AAA23665).
{ECO:0000305}.
CONFLICT 224 224 G -> E (in Ref. 1; AAA23665).
{ECO:0000305}.
STRAND 4 8 {ECO:0000244|PDB:2OJP}.
STRAND 17 19 {ECO:0000244|PDB:2PUR}.
HELIX 21 34 {ECO:0000244|PDB:2OJP}.
STRAND 38 43 {ECO:0000244|PDB:2OJP}.
TURN 44 47 {ECO:0000244|PDB:2OJP}.
HELIX 48 50 {ECO:0000244|PDB:2OJP}.
HELIX 53 67 {ECO:0000244|PDB:2OJP}.
STRAND 73 76 {ECO:0000244|PDB:2OJP}.
HELIX 82 91 {ECO:0000244|PDB:2OJP}.
TURN 92 94 {ECO:0000244|PDB:2OJP}.
STRAND 98 103 {ECO:0000244|PDB:2OJP}.
HELIX 112 123 {ECO:0000244|PDB:2OJP}.
STRAND 130 133 {ECO:0000244|PDB:2OJP}.
HELIX 136 139 {ECO:0000244|PDB:2OJP}.
HELIX 145 152 {ECO:0000244|PDB:2OJP}.
STRAND 157 160 {ECO:0000244|PDB:2OJP}.
HELIX 169 174 {ECO:0000244|PDB:2OJP}.
STRAND 181 186 {ECO:0000244|PDB:2OJP}.
HELIX 188 190 {ECO:0000244|PDB:2OJP}.
HELIX 191 196 {ECO:0000244|PDB:2OJP}.
STRAND 201 205 {ECO:0000244|PDB:2OJP}.
HELIX 206 208 {ECO:0000244|PDB:2OJP}.
HELIX 211 222 {ECO:0000244|PDB:2OJP}.
HELIX 226 242 {ECO:0000244|PDB:2OJP}.
STRAND 245 247 {ECO:0000244|PDB:2OJP}.
HELIX 250 258 {ECO:0000244|PDB:2OJP}.
STRAND 261 263 {ECO:0000244|PDB:2OJP}.
HELIX 276 288 {ECO:0000244|PDB:2OJP}.
SEQUENCE 292 AA; 31270 MW; 3970543296A77C08 CRC64;
MFTGSIVAIV TPMDEKGNVC RASLKKLIDY HVASGTSAIV SVGTTGESAT LNHDEHADVV
MMTLDLADGR IPVIAGTGAN ATAEAISLTQ RFNDSGIVGC LTVTPYYNRP SQEGLYQHFK
AIAEHTDLPQ ILYNVPSRTG CDLLPETVGR LAKVKNIIGI KEATGNLTRV NQIKELVSDD
FVLLSGDDAS ALDFMQLGGH GVISVTANVA ARDMAQMCKL AAEGHFAEAR VINQRLMPLH
NKLFVEPNPI PVKWACKELG LVATDTLRLP MTPITDSGRE TVRAALKHAG LL


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