ID DAPF_LACPL Reviewed; 332 AA. AC Q88V90; F9UQB7; DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 20-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 99. DE RecName: Full=Diaminopimelate epimerase {ECO:0000255|HAMAP-Rule:MF_00197}; DE Short=DAP epimerase {ECO:0000255|HAMAP-Rule:MF_00197}; DE EC=5.1.1.7 {ECO:0000255|HAMAP-Rule:MF_00197}; DE AltName: Full=PLP-independent amino acid racemase {ECO:0000255|HAMAP-Rule:MF_00197}; GN Name=dapF {ECO:0000255|HAMAP-Rule:MF_00197}; GN OrderedLocusNames=lp_2185; OS Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) OS (Lactobacillus plantarum). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactiplantibacillus. OX NCBI_TaxID=220668; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1; RX PubMed=12566566; DOI=10.1073/pnas.0337704100; RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P., RA Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J., RA Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M., RA Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M., RA Siezen R.J.; RT "Complete genome sequence of Lactobacillus plantarum WCFS1."; RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION. RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1; RX PubMed=22156394; DOI=10.1128/jb.06275-11; RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M., RA Kleerebezem M., van Hijum S.A.; RT "Complete resequencing and reannotation of the Lactobacillus plantarum RT WCFS1 genome."; RL J. Bacteriol. 194:195-196(2012). 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. CC {ECO:0000255|HAMAP-Rule:MF_00197}. 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00197}; 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 {ECO:0000255|HAMAP-Rule:MF_00197}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00197}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00197}. CC -!- SIMILARITY: Belongs to the diaminopimelate epimerase family. CC {ECO:0000255|HAMAP-Rule:MF_00197}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL935263; CCC79406.1; -; Genomic_DNA. DR RefSeq; WP_003644607.1; NC_004567.2. DR RefSeq; YP_004889920.1; NC_004567.2. DR AlphaFoldDB; Q88V90; -. DR SMR; Q88V90; -. DR STRING; 220668.lp_2185; -. DR EnsemblBacteria; CCC79406; CCC79406; lp_2185. DR KEGG; lpl:lp_2185; -. DR PATRIC; fig|220668.9.peg.1847; -. DR eggNOG; COG0253; Bacteria. DR HOGENOM; CLU_053306_3_1_9; -. DR OrthoDB; 9805408at2; -. DR PhylomeDB; Q88V90; -. DR UniPathway; UPA00034; UER00025. DR Proteomes; UP000000432; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008837; F:diaminopimelate epimerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule. DR HAMAP; MF_00197; DAP_epimerase; 1. DR InterPro; IPR018510; DAP_epimerase_AS. DR InterPro; IPR001653; DAP_epimerase_DapF. DR NCBIfam; TIGR00652; DapF; 1. DR PANTHER; PTHR31689:SF0; DIAMINOPIMELATE EPIMERASE; 1. DR PANTHER; PTHR31689; DIAMINOPIMELATE EPIMERASE, CHLOROPLASTIC; 1. DR Pfam; PF01678; DAP_epimerase; 2. DR SUPFAM; SSF54506; Diaminopimelate epimerase-like; 2. DR PROSITE; PS01326; DAP_EPIMERASE; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Cytoplasm; Isomerase; Lysine biosynthesis; KW Reference proteome. FT CHAIN 1..332 FT /note="Diaminopimelate epimerase" FT /id="PRO_0000149845" FT ACT_SITE 82 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT ACT_SITE 236 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 13 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 73 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 83..84 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 172 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 209 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 227..228 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 237..238 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT SITE 174 FT /note="Could be important to modulate the pK values of the FT two catalytic cysteine residues" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT SITE 227 FT /note="Could be important to modulate the pK values of the FT two catalytic cysteine residues" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" SQ SEQUENCE 332 AA; 35962 MW; 1D5FF6C6E05441E0 CRC64; MAVKMIKVHG SGNDFYLLDQ TQFQAPLSDA DLKQLAINIC KRDGAGLYDG ADGVLVVDKS EHPQVLGRMR VINADGTEAS MCGNGLRTVA RYLGTQNSQE DFRVQTMYAD LKVQAVADFA AHVPAYSVEI SPVTFDAQTL GMHANNDATT IINEKIPALS ADLKFSAVAV PNPHLIAFVD HDTLVGPELG RIGEWMNDGK NQIFPDGVNV SFVEVLGPNS IFVRTFERGV GFTNACGTAM SASSLMYVLL HQESTDFNQE IHVTNPGGMV KTVVHQGADE EYWMELIGNA TFVRIVTLPL EDALQGDYSP VTATETGEQV AYEDFVANLA KA //