AC   MF_01642;
DC   Protein; auto
TR   HAMAP; MF_01642; -; 1; level=0
XX
Names: DapL_aminotrans_1
XX
ID   DAPAT
DE   RecName: Full=LL-diaminopimelate aminotransferase;
DE            Short=DAP-AT;
DE            Short=DAP-aminotransferase;
DE            Short=LL-DAP-aminotransferase;
DE            EC=2.6.1.83;
GN   Name=dapL;
XX
CC   -!- FUNCTION: Involved in the synthesis of meso-diaminopimelate (m-DAP or
CC       DL-DAP), required for both lysine and peptidoglycan biosynthesis.
CC       Catalyzes the direct conversion of tetrahydrodipicolinate to LL-
CC       diaminopimelate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S,6S)-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)-
CC         2,3,4,5-tetrahydrodipicolinate + H(+) + H2O + L-glutamate;
CC         Xref=Rhea:RHEA:23988, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:16845, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:57609; EC=2.6.1.83;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate
CC       (aminotransferase route): step 1/1.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. LL-diaminopimelate aminotransferase subfamily.
XX
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1; trigger=no
DR   Pfam; PF00155; Aminotran_1_2; 1; trigger=no
XX
KW   Aminotransferase
KW   Pyridoxal phosphate
KW   Transferase
XX
GO   GO:0010285; F:L,L-diaminopimelate aminotransferase activity
GO   GO:0030170; F:pyridoxal phosphate binding
GO   GO:0033362; P:lysine biosynthetic process via diaminopimelate, diaminopimelate-aminotransferase pathway
XX
FT   From: DAPAT_CHLTR (O84395)
FT   BINDING         104..105
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: [AST]-K
FT   BINDING         233..235
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: S-x-S
FT   BINDING         14
FT                   /ligand="substrate"
FT   Condition: Y
FT   BINDING         41
FT                   /ligand="substrate"
FT   Condition: G
FT   BINDING         71
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: Y
FT   BINDING         105
FT                   /ligand="substrate"
FT   Condition: K
FT   BINDING         128
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: [YF]
FT   BINDING         128
FT                   /ligand="substrate"
FT   Condition: [YF]
FT   BINDING         174
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: N
FT   BINDING         174
FT                   /ligand="substrate"
FT   Condition: N
FT   BINDING         205
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: Y
FT   BINDING         244
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: R
FT   BINDING         275
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: N
FT   BINDING         275
FT                   /ligand="substrate"
FT   Condition: N
FT   BINDING         369
FT                   /ligand="substrate"
FT   Condition: R
FT   MOD_RES         236
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT   Condition: K
XX
Size: 386-416;
Related: None;
Template: O84395; Q6MDE0; Q55828; O26158; Q18T09; Q72NJ3; Q2RK33; Q5LC03; A3DK17; Q7NDX4; A0LEA5;
Scope:
 Bacteria; Aquificae
 Bacteria; Bacteroidota
 Bacteria; Chlamydiota
 Bacteria; Chloroflexota
 Bacteria; Cyanobacteriota
 Bacteria; Clostridia
 Bacteria; Deltaproteobacteria
 Bacteria; Spirochaetota
 Archaea; Methanobacteriales
Fusion:
 Nter: None
 Cter: None
Duplicate: in NOSS1, TRIV2
Plasmid: None
Comments: None
XX
# Revision 1.27 2023/02/17
//