AC   MF_02122;
DC   Protein; auto
TR   HAMAP; MF_02122; -; 1; level=0
XX
Names: DapD_type2
XX
ID   DAPD
DE   RecName: Full=2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase;
DE            EC=2.3.1.117;
DE   AltName: Full=Tetrahydrodipicolinate N-succinyltransferase;
DE            Short=THDP succinyltransferase;
DE            Short=THP succinyltransferase;
DE   AltName: Full=Tetrahydropicolinate succinylase;
GN   Name=dapD;
XX
CC   -!- FUNCTION: Catalyzes the conversion of the cyclic tetrahydrodipicolinate
CC       (THDP) into the acyclic N-succinyl-L-2-amino-6-oxopimelate using
CC       succinyl-CoA.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = (S)-
CC         2-succinylamino-6-oxoheptanedioate + CoA; Xref=Rhea:RHEA:17325,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate
CC       (succinylase route): step 1/3.
CC   -!- SUBUNIT: Homotrimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the type 2 tetrahydrodipicolinate N-
CC       succinyltransferase family.
XX
DR   NCBIfam; TIGR03535; DapD_actino; 1; trigger=no
DR   NCBIfam; TIGR03536; DapD_gpp; 1; trigger=no
XX
KW   Acyltransferase
KW   Amino-acid biosynthesis
KW   Cytoplasm
KW   Diaminopimelate biosynthesis
KW   Lysine biosynthesis
KW   Transferase
case <FT:4> or <FT:5>
KW   Magnesium
KW   Metal-binding
end case
XX
case <FT:4> or <FT:5>
GO   GO:0000287; F:magnesium ion binding
end case
GO   GO:0008666; F:2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase activity
GO   GO:0009089; P:lysine biosynthetic process via diaminopimelate
GO   GO:0019877; P:diaminopimelate biosynthetic process
GO   GO:0005737; C:cytoplasm
XX
FT   From: DAPD_MYCTU (P9WP21)
FT   ACT_SITE        199
FT                   /note="Acyl-anhydride intermediate"
FT   Condition: E
FT   BINDING         257..258
FT                   /ligand="succinyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57292"
FT   Condition: [ED]-[AGS]
FT   BINDING         290..293
FT                   /ligand="succinyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57292"
FT   Condition: R-[RQ]-x-S
FT   BINDING         166
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="ligand shared between trimeric partners"
FT   Optional; Condition: D
FT   BINDING         183
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="ligand shared between trimeric partners"
FT   Optional; Condition: E
FT   BINDING         201
FT                   /ligand="succinyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57292"
FT   Condition: R
FT   BINDING         216
FT                   /ligand="succinyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57292"
FT   Condition: [GA]
FT   BINDING         219
FT                   /ligand="succinyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57292"
FT   Condition: S
FT   BINDING         242
FT                   /ligand="succinyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57292"
FT   Condition: A
FT   BINDING         265
FT                   /ligand="succinyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57292"
FT   Condition: G
FT   BINDING         277
FT                   /ligand="succinyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57292"
FT   Condition: K
XX
Size: 297-401;
Related: None;
Template: P9WP21;
Scope:
 Bacteria; Actinomycetota
 Bacteria; Pseudomonadota
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: There is another family of DapD (see MF_00811).
XX
# Revision 1.14 2023/06/01
//