(data stored in ACNUC9543 zone)

SWISSPROT: DAPF_YERPA

ID   DAPF_YERPA              Reviewed;         274 AA.
AC   Q1CBM6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   08-MAY-2019, 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=YPA_0177;
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua;
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- FUNCTION: Catalyzes the stereoinversion of LL-2,6-
CC       diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-
CC       DAP), a precursor of L-lysine and an essential component of the
CC       bacterial peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00197}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=LL-2,6-diaminoheptanedioate = meso-2,6-diaminopimelate;
CC         Xref=Rhea:RHEA:15393, ChEBI:CHEBI:57609, ChEBI:CHEBI:57791;
CC         EC=5.1.1.7; Evidence={ECO:0000255|HAMAP-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
CC       1/1. {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}.
DR   EMBL; CP000308; ABG12146.1; -; Genomic_DNA.
DR   RefSeq; WP_002211471.1; NZ_CP009906.1.
DR   SMR; Q1CBM6; -.
DR   EnsemblBacteria; ABG12146; ABG12146; YPA_0177.
DR   KEGG; ypa:YPA_0177; -.
DR   HOGENOM; HOG000220466; -.
DR   KO; K01778; -.
DR   OMA; MCGNGGR; -.
DR   UniPathway; UPA00034; UER00025.
DR   Proteomes; UP000001971; 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;
DR   PRODOM; Q1CBM6.
DR   SWISS-2DPAGE; Q1CBM6.
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm; Isomerase;
KW   Lysine biosynthesis.
FT   CHAIN         1    274       Diaminopimelate epimerase.
FT                                /FTId=PRO_1000011987.
FT   REGION       74     75       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   REGION      208    209       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   REGION      218    219       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   ACT_SITE     73     73       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   ACT_SITE    217    217       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   BINDING      11     11       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   BINDING      44     44       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   BINDING      64     64       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   BINDING     157    157       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   BINDING     190    190       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   SITE        159    159       Could be important to modulate the pK
FT                                values of the two catalytic cysteine
FT                                residues. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   SITE        208    208       Could be important to modulate the pK
FT                                values of the two catalytic cysteine
FT                                residues. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   SITE        268    268       Important for dimerization.
FT                                {ECO:0000255|HAMAP-Rule:MF_00197}.
SQ   SEQUENCE   274 AA;  30252 MW;  8B66E79E67EB9FF1 CRC64;
     MQFSKMHGLG NDFMVVDAVT QNVYFSPELI RRLADRHTGV GFDQMLVVEP PYDPELDFHY
     RIFNADGSEV SQCGNGARCF ARFVRLKGLT NKREISVSTQ TGRMILSVTE DEQVCVNMGE
     PDFEPQTVPF RAAKAEKTYI LRAAEHTVLC GVVSMGNPHC VMQVDDVSVA NVALLGPVLE
     NHERFPERAN IGFMQVVSRD HIRLRVYERG AGETQACGSG ACAAVAVGVV QDLLNENVHV
     ELPGGSLHIR WQGPGHPLYM TGPATHVYDG FIHL
//

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