ID DAPF_MYCA1 Reviewed; 294 AA. AC A0QIQ8; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 1. DT 27-MAR-2024, entry version 92. 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=MAV_3619; OS Mycobacterium avium (strain 104). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium avium complex (MAC). OX NCBI_TaxID=243243; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=104; RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., RA Fraser C.M.; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. 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; CP000479; ABK67759.1; -; Genomic_DNA. DR RefSeq; WP_011725573.1; NC_008595.1. DR AlphaFoldDB; A0QIQ8; -. DR SMR; A0QIQ8; -. DR KEGG; mav:MAV_3619; -. DR HOGENOM; CLU_053306_4_0_11; -. DR UniPathway; UPA00034; UER00025. DR Proteomes; UP000001574; 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. FT CHAIN 1..294 FT /note="Diaminopimelate epimerase" FT /id="PRO_1000011906" FT ACT_SITE 87 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT ACT_SITE 230 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 11 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 78 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 88..89 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 167 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 203 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 221..222 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 231..232 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT SITE 169 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 221 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 294 AA; 30025 MW; 764CBE9BFCAC27BF CRC64; MKFAKGHGTE NDFVLLCDTP AELRLTAAGV AALCDRRRGL GADGVLRVTT AGAAAAAGVL DRLPDGVAGD DWYMDYRNSD GSVAQMCGNG VRVFAHYLRA SGLETRDEFV VGSLAGPRPV TVHAADATGA DVSVDMGKAN TLGSGGKAFE ATVGGRRFAG LAVDVGNPHL ACLDPELSVD ELAALDVAAP VSFDAAQFPD GVNVEVLTAP AAGVVHMRVH ERGVGETRSC GTGTVAAAVA ALTAAGADTG TLTVRVPGGD VVVTVTDATS YLRGPSVLVA HGEISEEWWQ QAQR //