AC   MF_00418;
DC   Protein; auto
TR   HAMAP; MF_00418; -; 1; level=0
XX
Names: DapA
XX
ID   DAPA
DE   RecName: Full=4-hydroxy-tetrahydrodipicolinate synthase;
DE            Short=HTPA synthase;
DE            EC=4.3.3.7;
GN   Name=dapA;
XX
CC   -!- FUNCTION: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde
CC       [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-
CC         2,3,4,5-tetrahydrodipicolinate + H(+) + H2O; Xref=Rhea:RHEA:34171,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:67139, ChEBI:CHEBI:537519; EC=4.3.3.7;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
case (<OC:Bacteria> or <OC:Archaea>) and not (<OC:Staphylococcus> or <OC:Pseudomonas>)
CC   -!- SUBUNIT: Homotetramer; dimer of dimers.
else
CC   -!- SUBUNIT: Homodimer.
end case
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the DapA family.
CC   -!- CAUTION: Was originally thought to be a dihydrodipicolinate synthase
CC       (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde
CC       [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was
CC       shown in E.coli that the product of the enzymatic reaction is not
CC       dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-
CC       dipicolinic acid (HTPA), and that the consecutive dehydration reaction
CC       leading to DHDP is not spontaneous but catalyzed by DapB.
XX
DR   Pfam; PF00701; DHDPS; 1; trigger=no
DR   PRINTS; PR00146; DHPICSNTHASE; 1; trigger=no
DR   NCBIfam; TIGR00674; DapA; 1; trigger=no
DR   PROSITE; PS00665; DHDPS_1; 1; trigger=no
DR   PROSITE; PS00666; DHDPS_2; 1; trigger=no
XX
KW   Cytoplasm
KW   Amino-acid biosynthesis
KW   Diaminopimelate biosynthesis
KW   Lyase
KW   Lysine biosynthesis
KW   Schiff base
XX
GO   GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity
GO   GO:0019877; P:diaminopimelate biosynthetic process
GO   GO:0009085; P:lysine biosynthetic process
GO   GO:0005737; C:cytoplasm
XX
FT   From: DAPA_ECOLI (P0A6L2)
FT   ACT_SITE        133
FT                   /note="Proton donor/acceptor"
FT   Condition: Y
FT   ACT_SITE        161
FT                   /note="Schiff-base intermediate with substrate"
FT   Condition: K
FT   BINDING         45
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT   Condition: [TS]
FT   BINDING         203
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT   Condition: [IVAT]
FT   SITE            44
FT                   /note="Part of a proton relay during catalysis"
FT   Condition: [TS]
FT   SITE            107
FT                   /note="Part of a proton relay during catalysis"
FT   Condition: Y
XX
Size: 283-311;
Related: MF_01237!; MF_00694;
Template: P0A6L2; P9WP25; Q9X1K9; Q57695; Q6GH13; Q5HG25; Q9JZR4; Q9I4W3; Q07607; Q8UGL3;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in HALH5, CLOAB, STRCO
Plasmid: None
Comments: None.
XX
# Revision 1.46 2023/06/01
//