AC MF_00197; DC Protein; auto TR HAMAP; MF_00197; -; 1; level=0 XX Names: DAP_epimerase XX ID DAPF DE RecName: Full=Diaminopimelate epimerase; DE Short=DAP epimerase; DE EC=5.1.1.7; DE AltName: Full=PLP-independent amino acid racemase; GN Name=dapF; XX case CC -!- FUNCTION: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate CC (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- CC lysine and an essential component of the bacterial peptidoglycan. end case case CC -!- FUNCTION: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate CC (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- CC lysine. end case CC -!- CATALYTIC ACTIVITY: CC Reaction=(2S,6S)-2,6-diaminoheptanedioate = meso-2,6- CC diaminoheptanedioate; Xref=Rhea:RHEA:15393, ChEBI:CHEBI:57609, CC ChEBI:CHEBI:57791; EC=5.1.1.7; CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the diaminopimelate epimerase family. XX DR Pfam; PF01678; DAP_epimerase; 1; trigger=no DR NCBIfam; TIGR00652; DapF; 1; trigger=no DR PROSITE; PS01326; DAP_EPIMERASE; 1; trigger=no XX KW Cytoplasm KW Amino-acid biosynthesis KW Isomerase KW Lysine biosynthesis XX GO GO:0008837; F:diaminopimelate epimerase activity GO GO:0009089; P:lysine biosynthetic process via diaminopimelate GO GO:0005737; C:cytoplasm XX FT From: DAPF_HAEIN (P44859) FT BINDING 74..75 FT /ligand="substrate" FT Condition: [GI]-N FT BINDING 208..209 FT /ligand="substrate" FT Condition: E-R FT BINDING 218..219 FT /ligand="substrate" FT Condition: G-[ST] FT ACT_SITE 73 FT /note="Proton donor" FT Condition: C FT ACT_SITE 217 FT /note="Proton acceptor" FT Condition: C FT BINDING 11 FT /ligand="substrate" FT Condition: N FT BINDING 44 FT /ligand="substrate" FT Condition: Q FT BINDING 64 FT /ligand="substrate" FT Condition: [NQ] FT BINDING 157 FT /ligand="substrate" FT Condition: N FT BINDING 190 FT /ligand="substrate" FT Condition: N FT SITE 159 FT /note="Could be important to modulate the pK values of the FT two catalytic cysteine residues" FT Condition: H FT SITE 208 FT /note="Could be important to modulate the pK values of the FT two catalytic cysteine residues" FT Condition: E case FT SITE 268 FT /note="Important for dimerization" FT Condition: [YF] end case XX Size: 249-333; Related: None; Template: P0A6K1; P44859; Q8NP73; P9WP19; Scope: Bacteria Archaea Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: DcsC (S.lavendulae) belongs to the same group of racemases/epimerases as diaminopimelate epimerase (DapF) and also utilizes a two-base mechanism involving a pair of cysteine residues, however it function as racemase with O-ureido-L-serine as a substrate. XX # Revision 1.36 2023/06/01 //