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1DHP

DIHYDRODIPICOLINATE SYNTHASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008652biological_processamino acid biosynthetic process
A0008840molecular_function4-hydroxy-tetrahydrodipicolinate synthase activity
A0009085biological_processlysine biosynthetic process
A0009089biological_processlysine biosynthetic process via diaminopimelate
A0016829molecular_functionlyase activity
A0019752biological_processcarboxylic acid metabolic process
A0019877biological_processdiaminopimelate biosynthetic process
A0042802molecular_functionidentical protein binding
B0003824molecular_functioncatalytic activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008652biological_processamino acid biosynthetic process
B0008840molecular_function4-hydroxy-tetrahydrodipicolinate synthase activity
B0009085biological_processlysine biosynthetic process
B0009089biological_processlysine biosynthetic process via diaminopimelate
B0016829molecular_functionlyase activity
B0019752biological_processcarboxylic acid metabolic process
B0019877biological_processdiaminopimelate biosynthetic process
B0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K A 293
ChainResidue
AALA152
AVAL154
ALYS155
AILE157

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K B 293
ChainResidue
BHOH400
BALA152
BVAL154
BLYS155
BILE157

site_idS1
Number of Residues1
DetailsPYRUVATE BINDING RESIDUE.
ChainResidue
ALYS161

Functional Information from PROSITE/UniProt
site_idPS00665
Number of Residues18
DetailsDHDPS_1 Dihydrodipicolinate synthase signature 1. AIVsvGTTGESatlnhdE
ChainResidueDetails
AALA38-GLU55

site_idPS00666
Number of Residues31
DetailsDHDPS_2 Dihydrodipicolinate synthase signature 2. YNVPsrTgcdLlpetvgrlakvkn.IiGIKEA
ChainResidueDetails
ATYR133-ALA163

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Schiff-base intermediate with substrate"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00418","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20353808","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22552955","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsSite: {"description":"Part of a proton relay during catalysis"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"L-lysine inhibitor binding; via carbonyl oxygen"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsSite: {"description":"L-lysine inhibitor binding"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 8993314, 18787203
ChainResidueDetails
ALYS161
ATYR133
AILE203

site_idMCSA1
Number of Residues6
DetailsM-CSA 267
ChainResidueDetails
ATHR44hydrogen bond acceptor, hydrogen bond donor
ATYR107hydrogen bond donor
ATYR133activator, electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay
AARG138electrostatic stabiliser
ALYS161covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
AILE203activator, increase electrophilicity, polar interaction, steric role

site_idMCSA2
Number of Residues6
DetailsM-CSA 267
ChainResidueDetails
BTHR44hydrogen bond acceptor, hydrogen bond donor
BTYR107hydrogen bond donor
BTYR133activator, electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay
BARG138electrostatic stabiliser
BLYS161covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
BILE203activator, increase electrophilicity, polar interaction, steric role

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PDB entries from 2025-07-23

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