AC   MF_02120;
DC   Protein; auto
TR   HAMAP; MF_02120; -; 1; level=0
XX
Names: LysA
XX
ID   DCDA
DE   RecName: Full=Diaminopimelate decarboxylase;
DE            Short=DAP decarboxylase;
DE            Short=DAPDC;
DE            EC=4.1.1.20;
GN   Name=lysA;
XX
CC   -!- FUNCTION: Specifically catalyzes the decarboxylation of meso-
CC       diaminopimelate (meso-DAP) to L-lysine.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + meso-2,6-diaminoheptanedioate = CO2 + L-lysine;
CC         Xref=Rhea:RHEA:15101, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:32551, ChEBI:CHEBI:57791; EC=4.1.1.20;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC       LysA subfamily.
XX
DR   PROSITE; PS00878; ODR_DC_2_1; 1; trigger=no
DR   PROSITE; PS00879; ODR_DC_2_2; 1; trigger=no
DR   Pfam; PF02784; Orn_Arg_deC_N; 1; trigger=no
DR   Pfam; PF00278; Orn_DAP_Arg_deC; 1; trigger=no
DR   PRINTS; PR01181; DAPDCRBXLASE; 1; trigger=no
DR   PRINTS; PR01179; ODADCRBXLASE; 1; trigger=no
DR   NCBIfam; TIGR01048; LysA; 1; trigger=no
XX
KW   Amino-acid biosynthesis
KW   Decarboxylase
KW   Lyase
KW   Lysine biosynthesis
KW   Pyridoxal phosphate
XX
GO   GO:0008836; F:diaminopimelate decarboxylase activity
GO   GO:0030170; F:pyridoxal phosphate binding
GO   GO:0009089; P:lysine biosynthetic process via diaminopimelate
XX
FT   From: DCDA_MYCTU (P9WIU7)
FT   BINDING         300..303
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: E-x-G-R
FT   BINDING         258
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: G
FT   BINDING         303
FT                   /ligand="substrate"
FT   Condition: R
FT   BINDING         344
FT                   /ligand="substrate"
FT   Condition: R
FT   BINDING         348
FT                   /ligand="substrate"
FT   Condition: Y
FT   BINDING         376
FT                   /ligand="substrate"
FT   Condition: E
FT   BINDING         405
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: Y
FT   BINDING         405
FT                   /ligand="substrate"
FT   Condition: Y
FT   MOD_RES         72
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT   Condition: K
XX
Size: 379-474;
Related: None;
Template: P9WIU7; P00861; E0IWI3; Q58497; B4XMC6; Q5HG20; O67262; Q9X1K5; Q9KVL7;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: RHEA:15102;
XX
# Revision 1.12 2023/06/01
//