ID   DAPF_SALNS              Reviewed;         274 AA.
AC   B4SZ51;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 77.
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=SNSL254_A4227;
OS   Salmonella newport (strain SL254).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=423368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL254;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(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}.
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DR   EMBL; CP001113; ACF62178.1; -; Genomic_DNA.
DR   RefSeq; WP_001160671.1; NZ_CCMR01000001.1.
DR   AlphaFoldDB; B4SZ51; -.
DR   SMR; B4SZ51; -.
DR   KEGG; see:SNSL254_A4227; -.
DR   HOGENOM; CLU_053306_1_1_6; -.
DR   UniPathway; UPA00034; UER00025.
DR   Proteomes; UP000008824; 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.
FT   CHAIN           1..274
FT                   /note="Diaminopimelate epimerase"
FT                   /id="PRO_1000099264"
FT   ACT_SITE        73
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00197"
FT   ACT_SITE        217
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         44
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00197"
FT   BINDING         64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00197"
FT   BINDING         74..75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00197"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00197"
FT   BINDING         190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00197"
FT   BINDING         208..209
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00197"
FT   BINDING         218..219
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00197"
FT   SITE            159
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            208
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            268
FT                   /note="Important for dimerization"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00197"
SQ   SEQUENCE   274 AA;  30337 MW;  2FBB315B7DA12AE9 CRC64;
     MQFSKMHGLG NDFMVVDAVT QNVFFSPELI RRLSDRHLGV GFDQLLVVEP PYDPELDFHY
     RIFNADGSEV SQCGNGARCF ARFVRLKGLT NKRDIRVSTA NGRMVLSVTE DELVRVNMGE
     PNFEPAQVPF RANKAEKTYI MRAAEQTILC GVVSMGNPHC VIQVDNVDTA AVETLGPVLE
     SHERFPERAN IGFMQVVRRE HIRLRVYERG AGETRACGSG ACAAVAVGIQ QGLLAEEVRV
     ELPGGRLDIA WKGPGHPLYM TGPAAHIYDG FIHL
//