ID   DAPF_FLAPJ              Reviewed;         256 AA.
AC   A6GYX5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 85.
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}; OrderedLocusNames=FP1215;
OS   Flavobacterium psychrophilum (strain ATCC 49511 / DSM 21280 / CIP 103535 /
OS   JIP02/86).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=402612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49511 / DSM 21280 / CIP 103535 / JIP02/86;
RX   PubMed=17592475; DOI=10.1038/nbt1313;
RA   Duchaud E., Boussaha M., Loux V., Bernardet J.-F., Michel C., Kerouault B.,
RA   Mondot S., Nicolas P., Bossy R., Caron C., Bessieres P., Gibrat J.-F.,
RA   Claverol S., Dumetz F., Le Henaff M., Benmansour A.;
RT   "Complete genome sequence of the fish pathogen Flavobacterium
RT   psychrophilum.";
RL   Nat. Biotechnol. 25:763-769(2007).
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; AM398681; CAL43298.1; -; Genomic_DNA.
DR   RefSeq; WP_011963347.1; NC_009613.3.
DR   RefSeq; YP_001296109.1; NC_009613.3.
DR   AlphaFoldDB; A6GYX5; -.
DR   SMR; A6GYX5; -.
DR   STRING; 402612.FP1215; -.
DR   EnsemblBacteria; CAL43298; CAL43298; FP1215.
DR   GeneID; 66553119; -.
DR   KEGG; fps:FP1215; -.
DR   PATRIC; fig|402612.5.peg.1229; -.
DR   eggNOG; COG0253; Bacteria.
DR   HOGENOM; CLU_053306_3_2_10; -.
DR   OrthoDB; 9805408at2; -.
DR   UniPathway; UPA00034; UER00025.
DR   Proteomes; UP000006394; 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;
KW   Reference proteome.
FT   CHAIN           1..256
FT                   /note="Diaminopimelate epimerase"
FT                   /id="PRO_1000099237"
FT   ACT_SITE        72
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00197"
FT   ACT_SITE        197
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         63
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00197"
FT   BINDING         73..74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00197"
FT   BINDING         169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00197"
FT   BINDING         187..188
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00197"
FT   BINDING         198..199
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00197"
FT   SITE            137
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            187
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   256 AA;  28463 MW;  42633776D96E3A8B CRC64;
     MKLYKYQGTG NDFIMIDNRL QIFPKQNTAL IQKLCDRRFG IGADGLILLE NDQSTDFKMV
     YYNSDGNQST MCGNGGRCLV AFAKKLNIIK NKTTFIAIDG LHHATINEND IISLQMKNVE
     EVNIHDNYVF LNTGSPHHVQ FADNLSNFDV KNEGAKIRYS DLYGQAGSNI NFVHQTSPTQ
     FSIRTYERGV EDETLSCGTG ATATAIAMKA TGKTNSNNIT INVQGGKLEV SFNQENSIFT
     NIFLKGPAEF VFETTI
//