AC MF_01690; DC Protein; auto TR HAMAP; MF_01690; -; 1; level=0 XX Names: DapE XX ID DAPE DE RecName: Full=Succinyl-diaminopimelate desuccinylase; DE Short=SDAP desuccinylase; DE EC=3.5.1.18; DE AltName: Full=N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase; GN Name=dapE; XX CC -!- FUNCTION: Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic CC acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), CC an intermediate involved in the bacterial biosynthesis of lysine and CC meso-diaminopimelic acid, an essential component of bacterial cell CC walls. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate = (2S,6S)- CC 2,6-diaminoheptanedioate + succinate; Xref=Rhea:RHEA:22608, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:30031, ChEBI:CHEBI:57609, CC ChEBI:CHEBI:58087; EC=3.5.1.18; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Note=Binds 2 Zn(2+) or Co(2+) ions per subunit.; CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate CC (succinylase route): step 3/3. CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the peptidase M20A family. DapE subfamily. XX DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1; trigger=no DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1; trigger=no DR Pfam; PF07687; M20_dimer; 1; trigger=no DR Pfam; PF01546; Peptidase_M20; 1; trigger=no DR NCBIfam; TIGR01246; DapE_proteo; 1; trigger=no DR NCBIfam; TIGR01910; DapE-ArgE; 1; trigger=no XX KW Amino-acid biosynthesis KW Cobalt KW Diaminopimelate biosynthesis KW Hydrolase KW Lysine biosynthesis KW Metal-binding KW Zinc XX GO GO:0008270; F:zinc ion binding GO GO:0009014; F:succinyl-diaminopimelate desuccinylase activity GO GO:0050897; F:cobalt ion binding GO GO:0009089; P:lysine biosynthetic process via diaminopimelate GO GO:0019877; P:diaminopimelate biosynthetic process XX FT From: DAPE_HAEIN (P44514) FT ACT_SITE 69 FT Condition: D FT ACT_SITE 134 FT /note="Proton acceptor" FT Condition: E FT BINDING 67 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT Condition: H FT BINDING 100 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT Condition: D FT BINDING 100 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT Condition: D FT BINDING 135 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT Condition: E FT BINDING 163 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT Condition: E FT BINDING 349 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT Condition: H XX Size: 363-425; Related: None; Template: Q8ZN75; P44514; P0AED7; Q9JYL2; Q9KQ52; Scope: Bacteria; Pseudomonadota Fusion: Nter: None Cter: None Duplicate: in ALTMD, SHELP, RUEST Plasmid: in PSESY, RUEST Comments: None XX # Revision 1.19 2023/06/01 //