ID DAPF_AFIC5 Reviewed; 290 AA. AC B6JAP3; F8BTD9; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 16-DEC-2008, sequence version 1. DT 27-MAR-2024, entry version 78. 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=OCAR_4263, OCA5_c02550; OS Afipia carboxidovorans (strain ATCC 49405 / DSM 1227 / KCTC 32145 / OM5) OS (Oligotropha carboxidovorans). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Nitrobacteraceae; Afipia. OX NCBI_TaxID=504832; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5; RX PubMed=18539730; DOI=10.1128/jb.00614-08; RA Paul D., Bridges S., Burgess S.C., Dandass Y., Lawrence M.L.; RT "Genome sequence of the chemolithoautotrophic bacterium Oligotropha RT carboxidovorans OM5T."; RL J. Bacteriol. 190:5531-5532(2008). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5; RX PubMed=21742883; DOI=10.1128/jb.05619-11; RA Volland S., Rachinger M., Strittmatter A., Daniel R., Gottschalk G., RA Meyer O.; RT "Complete genome sequences of the chemolithoautotrophic Oligotropha RT carboxidovorans strains OM4 and OM5."; RL J. Bacteriol. 193:5043-5043(2011). 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; CP001196; ACI91412.1; -; Genomic_DNA. DR EMBL; CP002826; AEI04984.1; -; Genomic_DNA. DR RefSeq; WP_012561443.1; NC_015684.1. DR AlphaFoldDB; B6JAP3; -. DR SMR; B6JAP3; -. DR STRING; 504832.OCA5_c02550; -. DR KEGG; oca:OCAR_4263; -. DR KEGG; ocg:OCA5_c02550; -. DR PATRIC; fig|504832.7.peg.271; -. DR eggNOG; COG0253; Bacteria. DR HOGENOM; CLU_053306_1_0_5; -. DR OrthoDB; 9805408at2; -. DR UniPathway; UPA00034; UER00025. DR Proteomes; UP000007730; 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..290 FT /note="Diaminopimelate epimerase" FT /id="PRO_1000099253" FT ACT_SITE 78 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT ACT_SITE 226 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 17 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 49 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 69 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 79..80 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 166 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 199 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 217..218 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 SITE 168 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 217 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 290 AA; 31496 MW; 55349272902037E0 CRC64; MTVLANHSFA KMNGIGNEIV IVDLRNTDSQ LSAAEARAIA APGGVPYDQL MVLQKPRMPG TTAFVRIYNN DGSEAGACGN GMRCVAKRVF GESGAQAATF ETRAGLLNCW QGPSPDLYTV DMGTPKFGWQ DIPLAEEFRD TRYIELQIGP IDAPVLHSPS VVSMGNPHAI FWVDDIEAYD LERLGPLLEN HPIFPERANI TLAHVVDRNH IRMRTWERGA GLTLACGSAA CATAVAAARL KRTDRTVEMS LPGGDLTIEW RESDDHVLMT GAAVLEYEGL FDPDLFAALA //