ID   A0A109EJG2_9BURK        Unreviewed;       270 AA.
AC   A0A109EJG2;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   22-APR-2020, entry version 13.
DE   RecName: Full=Diaminopimelate epimerase {ECO:0000256|HAMAP-Rule:MF_00197};
DE            Short=DAP epimerase {ECO:0000256|HAMAP-Rule:MF_00197};
DE            EC=5.1.1.7 {ECO:0000256|HAMAP-Rule:MF_00197};
DE   AltName: Full=PLP-independent amino acid racemase {ECO:0000256|HAMAP-Rule:MF_00197};
GN   Name=dapF {ECO:0000256|HAMAP-Rule:MF_00197};
GN   ORFNames=AS149_23715 {ECO:0000313|EMBL:KWU27145.1};
OS   Burkholderia cenocepacia.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=95486 {ECO:0000313|EMBL:KWU27145.1, ECO:0000313|Proteomes:UP000065643};
RN   [1] {ECO:0000313|EMBL:KWU27145.1, ECO:0000313|Proteomes:UP000065643}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEIB S4-3 {ECO:0000313|EMBL:KWU27145.1,
RC   ECO:0000313|Proteomes:UP000065643};
RA   Fernandez-Lopez M.G., Popocal-Ursino E.C., Ortiz-Hernandez L.M.,
RA   Sanchez-Salinas E., Ramos-Quintana F., Villalobos-Lopez M.A.,
RA   Martinez-Ocampo F., Lozano-Aguirre L.F., Dantan-Gonzalez E.;
RT   "Draft Genome Sequence of Burkholderia cenocepacia Strain CEIB S5-2, a
RT   Methyl Parathion and p-Nitrophenol degrading bacterium isolated from
RT   agricultural soils in Morelos, Mexico.";
RL   Submitted (NOV-2015) 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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00197}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00197}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00197}.
CC   -!- SIMILARITY: Belongs to the diaminopimelate epimerase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00197, ECO:0000256|SAAS:SAAS00686236}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00197}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KWU27145.1}.
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DR   EMBL; LNCR01000020; KWU27145.1; -; Genomic_DNA.
DR   RefSeq; WP_050013390.1; NZ_LNCR01000020.1.
DR   EnsemblBacteria; KWU27145; KWU27145; AS149_23715.
DR   UniPathway; UPA00034; UER00025.
DR   Proteomes; UP000065643; Unassembled WGS sequence.
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; IPR001653; DAP_epimerase_DapF.
DR   PANTHER; PTHR31689; PTHR31689; 1.
DR   Pfam; PF01678; DAP_epimerase; 2.
DR   TIGRFAMs; TIGR00652; DapF; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00197};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00197};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00197, ECO:0000256|SAAS:SAAS00118214};
KW   Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00197}.
FT   REGION          205..206
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   REGION          215..216
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   ACT_SITE        77
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         50
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         68
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         154
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         187
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   SITE            156
FT                   /note="Could be important to modulate the pK values of the
FT                   two catalytic cysteine residues"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   SITE            205
FT                   /note="Could be important to modulate the pK values of the
FT                   two catalytic cysteine residues"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
SQ   SEQUENCE   270 AA;  29123 MW;  E4865DD4C7F78010 CRC64;
     MPIAFQKMNA NGDDFVIVDL RDQGHEQAHR VDRDLVRRMG DRHRGIGFNQ LALISDCDDA
     TAYVAFRNPD GSTLDTCGSA TRGAAWKLMR ETGAASVVLR TNRGRLHCSQ DAHGLIKVEM
     GAPRFGWQDI PFAEAADTLA LPLPGTPAAC SMGNPHCTFF FDDVAALDLA TLGPAIETHP
     LFPRKTNVHF VQVIDRTHIR LRIWERGGGV PLGSGSCSCG AVVNGIRRGL LDETVNVECD
     GGNVTVHWDG TGNVFLSGPV AFGFSGVWLS
//