ID DAPF_SHEON Reviewed; 275 AA. AC Q8E9H5; DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 112. 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=SO_4308; OS Shewanella oneidensis (strain MR-1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=211586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MR-1; RX PubMed=12368813; DOI=10.1038/nbt749; RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C., RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A., RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C., RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R., RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J., RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J., RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V., RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.; RT "Genome sequence of the dissimilatory metal ion-reducing bacterium RT Shewanella oneidensis."; RL Nat. Biotechnol. 20:1118-1123(2002). 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; AE014299; AAN57277.1; -; Genomic_DNA. DR RefSeq; NP_719833.1; NC_004347.2. DR RefSeq; WP_011073967.1; NZ_CP053946.1. DR AlphaFoldDB; Q8E9H5; -. DR SMR; Q8E9H5; -. DR STRING; 211586.SO_4308; -. DR PaxDb; 211586-SO_4308; -. DR KEGG; son:SO_4308; -. DR PATRIC; fig|211586.12.peg.4171; -. DR eggNOG; COG0253; Bacteria. DR HOGENOM; CLU_053306_1_1_6; -. DR OrthoDB; 9805408at2; -. DR PhylomeDB; Q8E9H5; -. DR BioCyc; SONE211586:G1GMP-3979-MONOMER; -. DR UniPathway; UPA00034; UER00025. DR Proteomes; UP000008186; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0008837; F:diaminopimelate epimerase activity; IBA:GO_Central. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IBA:GO_Central. 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..275 FT /note="Diaminopimelate epimerase" FT /id="PRO_0000149870" FT ACT_SITE 74 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT ACT_SITE 218 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 12 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 45 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 65 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 75..76 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 158 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 191 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 209..210 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 219..220 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT SITE 160 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 209 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 269 FT /note="Important for dimerization" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" SQ SEQUENCE 275 AA; 30063 MW; D0AA0D84D196D5D0 CRC64; MIQFTKMHGL GNDFMVVDGI TQNVFFSPEQ IRRLADRNFG VGFDQLLLVE PPYDPDLDFH YRIFNADGGE VENCGNGARC FARFVRNKGL TNKNKIRVST SAGKMTLRLE RDGTVTVNMG VPVLEPSQIP FKAKKAEKTY LLQTPQQTFL CGAASMGNPH CVLDVEDVAN ANVAEIGALL TKHERFPRGV NVGFMQVVNA GHIKLRVYER GAAETLACGT GACAAVVVGQ IQGKLDQQVQ VDLPGGSLTI NWEGEGKPLW MTGPAQHVYD GQIQL //