ID DAPF_ALCBS Reviewed; 281 AA. AC Q0VM18; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 02-SEP-2026, entry version 109. 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=ABO_2332; OS Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 / OS SK2). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Oceanospirillales; Alcanivoracaceae; Alcanivorax. OX NCBI_TaxID=393595; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2; RX PubMed=16878126; DOI=10.1038/nbt1232; RA Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M., RA Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C., RA Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B., RA McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O., RA Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J., RA Weidner S., Kaiser O., Golyshin P.N.; RT "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium RT Alcanivorax borkumensis."; RL Nat. Biotechnol. 24:997-1004(2006). CC -!- FUNCTION: Catalyzes the stereoinversion of LL-2,6-diaminopimelate (L,L- CC DAP) to meso-diaminopimelate (meso-DAP), a precursor of L-lysine and an CC essential component of the bacterial peptidoglycan. {ECO:0000255|HAMAP- CC Rule:MF_00197}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2S,6S)-2,6-diaminopimelate = meso-2,6-diaminopimelate; CC Xref=Rhea:RHEA:15393, ChEBI:CHEBI:57609, ChEBI:CHEBI:57791; CC EC=5.1.1.7; Evidence={ECO:0000255|HAMAP-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; AM286690; CAL17780.1; -; Genomic_DNA. DR RefSeq; WP_011589606.1; NC_008260.1. DR AlphaFoldDB; Q0VM18; -. DR SMR; Q0VM18; -. DR STRING; 393595.ABO_2332; -. DR KEGG; abo:ABO_2332; -. DR eggNOG; COG0253; Bacteria. DR HOGENOM; CLU_053306_1_1_6; -. DR OrthoDB; 9805408at2; -. DR UniPathway; UPA00034; UER00025. DR Proteomes; UP000008871; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0008837; F:diaminopimelate epimerase activity; IEA:UniProtKB-UniRule. DR FunFam; 3.10.310.10:FF:000001; Diaminopimelate epimerase; 1. DR Gene3D; 3.10.310.10; Diaminopimelate Epimerase, Chain A, domain 1; 2. 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; 1. 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..281 FT /note="Diaminopimelate epimerase" FT /id="PRO_1000011831" FT ACT_SITE 79 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT ACT_SITE 223 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 51 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 70 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 80..81 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 163 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 196 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 214..215 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 224..225 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT SITE 165 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 214 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 273 FT /note="Important for dimerization" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" SQ SEQUENCE 281 AA; 30363 MW; 05F53C8683062678 CRC64; MNLRFTKMHG LGNDFMVIDG IRQSLPETGL PLPADEIRRL ADRKFGVGFD QMLIVQPAQG DADFRYRILN ADGSEVSQCG NGARCFARFV REQGLTDKKS IRVETAAGQM TLSVTDDDQI TVDMGAPRWA PDAIPMTAKA EADNYFLVSG TQAWDVGAVG LGNPHCTLLV ENVDTAPVDT VGPLLESHEQ FPERANVGFM QIVSRNEIRL RVYERGAGET LACGSGACAA VVIGQRRDWL DDTVTVHLPG GTLHVCYDGQ GGIQMTGPAS HVYDGAIEIA L //