ID DAPF_CHRSD Reviewed; 277 AA. AC Q1QSV1; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 1. DT 27-MAR-2024, entry version 114. 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=Csal_3113; OS Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 / OS NCIMB 13768 / 1H11). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Chromohalobacter. OX NCBI_TaxID=290398; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11; RX PubMed=22675587; DOI=10.4056/sigs.2285059; RA Copeland A., O'Connor K., Lucas S., Lapidus A., Berry K.W., Detter J.C., RA Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Bruce D., RA Goodwin L., Han C., Tapia R., Saunders E., Schmutz J., Brettin T., RA Larimer F., Land M., Hauser L., Vargas C., Nieto J.J., Kyrpides N.C., RA Ivanova N., Goker M., Klenk H.P., Csonka L.N., Woyke T.; RT "Complete genome sequence of the halophilic and highly halotolerant RT Chromohalobacter salexigens type strain (1H11(T))."; RL Stand. Genomic Sci. 5:379-388(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; CP000285; ABE60457.1; -; Genomic_DNA. DR RefSeq; WP_011508403.1; NC_007963.1. DR AlphaFoldDB; Q1QSV1; -. DR SMR; Q1QSV1; -. DR STRING; 290398.Csal_3113; -. DR KEGG; csa:Csal_3113; -. DR eggNOG; COG0253; Bacteria. DR HOGENOM; CLU_053306_1_1_6; -. DR OrthoDB; 9805408at2; -. DR UniPathway; UPA00034; UER00025. DR Proteomes; UP000000239; 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; 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..277 FT /note="Diaminopimelate epimerase" FT /id="PRO_1000011868" FT ACT_SITE 75 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT ACT_SITE 219 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 46 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 66 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 76..77 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 159 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 192 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 210..211 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 220..221 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT SITE 161 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 210 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 270 FT /note="Important for dimerization" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" SQ SEQUENCE 277 AA; 30583 MW; 07A121EAA12FD10B CRC64; MLLHFTKMHG LGNDFVVIDL ITQRARLDTE RIRQLADRHV GIGFDQLLLV EPPRDPEMDF RYRIFNADGN EVENCGNGAR CFARFVRDNR LTHKREIRVE TQAGPLTLRV EDDERIRVDM GVPRFAPEVV PFDAPADAPA HCLEVDGETW DIGAVSMGNP HAVLRVDDVA QAPVARLGPL IERHPRFPRG VNVGFLQVVS RHEARLRVFE RGSGETLACG TGACAAVAHG IRRGWLESPV DVHLPGGTLT LAWPAPDASL MMTGPATSVF EGRIALP //