ID DAPF_ACIB3 Reviewed; 281 AA. AC B7GY71; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-FEB-2009, sequence version 1. DT 27-MAR-2024, entry version 76. 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=ABBFA_000848; OS Acinetobacter baumannii (strain AB307-0294). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae; OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=557600; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AB307-0294; RX PubMed=18931120; DOI=10.1128/jb.00834-08; RA Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J., RA MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M., RA Bonomo R.A., Gill S.R.; RT "Comparative genome sequence analysis of multidrug-resistant Acinetobacter RT baumannii."; RL J. Bacteriol. 190:8053-8064(2008). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-280, AND SUBUNIT. RA Mayclin S.J., Lorimer D.D., Edwards T.E.; RT "Structure of a diaminopimelate epimerase from Acinetobacter baumannii."; RL Submitted (DEC-2015) to the PDB data bank. 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:0000305|Ref.2}. 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; CP001172; ACJ59349.1; -; Genomic_DNA. DR RefSeq; WP_000923484.1; NZ_CP001172.1. DR PDB; 5HA4; X-ray; 1.85 A; A/B=1-280. DR PDBsum; 5HA4; -. DR AlphaFoldDB; B7GY71; -. DR SMR; B7GY71; -. DR HOGENOM; CLU_053306_1_1_6; -. DR UniPathway; UPA00034; UER00025. DR Proteomes; UP000006924; 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 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Cytoplasm; Isomerase; KW Lysine biosynthesis. FT CHAIN 1..281 FT /note="Diaminopimelate epimerase" FT /id="PRO_1000118659" FT ACT_SITE 75 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT ACT_SITE 220 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 160 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 193 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197" FT BINDING 211..212 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 SITE 162 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 211 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" FT STRAND 3..10 FT /evidence="ECO:0007829|PDB:5HA4" FT STRAND 13..19 FT /evidence="ECO:0007829|PDB:5HA4" FT HELIX 29..36 FT /evidence="ECO:0007829|PDB:5HA4" FT TURN 38..40 FT /evidence="ECO:0007829|PDB:5HA4" FT STRAND 45..51 FT /evidence="ECO:0007829|PDB:5HA4" FT STRAND 59..66 FT /evidence="ECO:0007829|PDB:5HA4" FT HELIX 78..88 FT /evidence="ECO:0007829|PDB:5HA4" FT STRAND 99..101 FT /evidence="ECO:0007829|PDB:5HA4" FT STRAND 104..106 FT /evidence="ECO:0007829|PDB:5HA4" FT HELIX 112..114 FT /evidence="ECO:0007829|PDB:5HA4" FT STRAND 116..119 FT /evidence="ECO:0007829|PDB:5HA4" FT HELIX 127..129 FT /evidence="ECO:0007829|PDB:5HA4" FT STRAND 141..144 FT /evidence="ECO:0007829|PDB:5HA4" FT HELIX 146..148 FT /evidence="ECO:0007829|PDB:5HA4" FT STRAND 150..166 FT /evidence="ECO:0007829|PDB:5HA4" FT TURN 170..172 FT /evidence="ECO:0007829|PDB:5HA4" FT HELIX 175..183 FT /evidence="ECO:0007829|PDB:5HA4" FT STRAND 193..201 FT /evidence="ECO:0007829|PDB:5HA4" FT STRAND 204..211 FT /evidence="ECO:0007829|PDB:5HA4" FT TURN 212..214 FT /evidence="ECO:0007829|PDB:5HA4" FT STRAND 215..218 FT /evidence="ECO:0007829|PDB:5HA4" FT HELIX 221..233 FT /evidence="ECO:0007829|PDB:5HA4" FT STRAND 239..245 FT /evidence="ECO:0007829|PDB:5HA4" FT STRAND 248..253 FT /evidence="ECO:0007829|PDB:5HA4" FT STRAND 261..264 FT /evidence="ECO:0007829|PDB:5HA4" FT STRAND 267..274 FT /evidence="ECO:0007829|PDB:5HA4" FT HELIX 276..279 FT /evidence="ECO:0007829|PDB:5HA4" SQ SEQUENCE 281 AA; 31139 MW; 700E4DB6C3C49032 CRC64; MLLEFTKMHG LGNDFMVVDL ISQRAYLDTA TIQRLADRHF GVGFDQLLIV EPPDVPEADF KYRIFNADGS EVEQCGNGVR CFARFVHERH LTNKTNITVQ TKAGIVKPEL GQNGWVRVNM GYPKFLPNEI PFVAEEPEAL YTLELANDQN ISIDVVNMGN PHAVTIVPDV LTADVAGIGP QVESHKRFPE RVNAGFMQVI DDKHVRLRVF ERGVGETLAC GTGACAAAVS GMRRGLLANS VEVELAGGKL QIEWQEGDVV WMTGPTTHVY DGRLDLRYFQ G //