(data stored in ACNUC7421 zone)

SWISSPROT: DAPF_PARXL

ID   DAPF_PARXL              Reviewed;         287 AA.
AC   Q146W2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 80.
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=Bxeno_A0089; ORFNames=Bxe_A4373;
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400;
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(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; CP000270; ABE28627.1; -; Genomic_DNA.
DR   RefSeq; WP_011486479.1; NZ_CP008760.1.
DR   SMR; Q146W2; -.
DR   STRING; 266265.Bxe_A4373; -.
DR   EnsemblBacteria; ABE28627; ABE28627; Bxe_A4373.
DR   GeneID; 4005532; -.
DR   KEGG; bxb:DR64_2050; -.
DR   KEGG; bxe:Bxe_A4373; -.
DR   PATRIC; fig|266265.5.peg.92; -.
DR   eggNOG; ENOG4105E4Z; Bacteria.
DR   eggNOG; COG0253; LUCA.
DR   HOGENOM; HOG000220466; -.
DR   KO; K01778; -.
DR   OMA; MCGNGGR; -.
DR   OrthoDB; 1921631at2; -.
DR   BioCyc; BXEN266265:BXE_RS00440-MONOMER; -.
DR   UniPathway; UPA00034; UER00025.
DR   Proteomes; UP000001817; Chromosome 1.
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; Q146W2.
DR   SWISS-2DPAGE; Q146W2.
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm; Isomerase;
KW   Lysine biosynthesis; Reference proteome.
FT   CHAIN         1    287       Diaminopimelate epimerase.
FT                                /FTId=PRO_1000011863.
FT   REGION       76     77       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   REGION      217    218       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   REGION      227    228       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   ACT_SITE     75     75       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   ACT_SITE    226    226       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   BINDING      13     13       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   BINDING      46     46       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   BINDING      66     66       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   BINDING     166    166       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   BINDING     199    199       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   SITE        168    168       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        217    217       Could be important to modulate the pK
FT                                values of the two catalytic cysteine
FT                                residues. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
SQ   SEQUENCE   287 AA;  31177 MW;  0263F6ACC407ED7F CRC64;
     MKLKFTKMHG AGNDFVVLDG YTQPVNLTPA QVRALADRHF GVGADQLLLV EKPTVAGVDF
     RYRIFNCDGG EVEHCGNGAR CFVKFVRERG LTDQRSVRVQ VQKGTITLTM QENGEVLVDM
     GTPVFDPERV PFATKGLEGR REGADTLWPL DVSGTTRWIS VVSMGNPHAV QVVGDVEAFP
     VLAEGPVIER HARFPQRVNA GFMQIVGRNE IRLRVYERGA GETLACGTGA CAAVAAGIRR
     GLLDSPVRVH THGGDLTISW DSTREGEPLL MAGPAVTVFE GEIELPD
//

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