DAPF_CLOPE
ID DAPF_CLOPE Reviewed; 272 AA.
AC Q46185;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 124.
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=CPE1846;
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A;
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 168-238.
RC STRAIN=CPN50;
RX PubMed=7559358; DOI=10.1128/jb.177.19.5680-5685.1995;
RA Katayama S., Dupuy B., Garnier T., Cole S.T.;
RT "Rapid expansion of the physical and genetic map of the chromosome of
RT Clostridium perfringens CPN50.";
RL J. Bacteriol. 177:5680-5685(1995).
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 -!- SEQUENCE CAUTION:
CC Sequence=CAA60229.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BA000016; BAB81552.1; -; Genomic_DNA.
DR EMBL; X86511; CAA60229.1; ALT_FRAME; Genomic_DNA.
DR RefSeq; WP_011010638.1; NC_003366.1.
DR AlphaFoldDB; Q46185; -.
DR SMR; Q46185; -.
DR STRING; 195102.gene:10491110; -.
DR EnsemblBacteria; BAB81552; BAB81552; BAB81552.
DR KEGG; cpe:CPE1846; -.
DR HOGENOM; CLU_053306_3_0_9; -.
DR OMA; HVAMRVH; -.
DR UniPathway; UPA00034; UER00025.
DR Proteomes; UP000000818; 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 PANTHER; PTHR31689; PTHR31689; 1.
DR Pfam; PF01678; DAP_epimerase; 2.
DR TIGRFAMs; TIGR00652; DapF; 1.
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..272
FT /note="Diaminopimelate epimerase"
FT /id="PRO_0000149835"
FT ACT_SITE 72
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 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 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 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 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 CONFLICT 183
FT /note="E -> D (in Ref. 2; CAA60229)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="F -> S (in Ref. 2; CAA60229)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="T -> P (in Ref. 2; CAA60229)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="T -> P (in Ref. 2; CAA60229)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="K -> N (in Ref. 2; CAA60229)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 272 AA; 30084 MW; 60DB1A8527815C05 CRC64;
MKFSKMHGNG NDFIVIEDLN NEYLGKEGEI AQKMCHRRFG IGADGILIVR KNENCDIEMV
IINSDGSYAA MCGNGIRCFA KYVYEKGIVK KDVLDVLTGD GVKRIFLEIE NDKVKTINVN
MGFGDFKPKN IPALCDEEII EKKVSVGNGN FEITSLLMGV PHTIIFEEEK YPIECGRDIE
KYELFPQGTN VNFCKVIDRN TMEVRTWERG AGPTLACGTG NCASVIAANK LGLVDKEVKV
IVPGGELKVN IEDDGVKMIG NASFICDGTY LF
