(data stored in ACNUC7421 zone)

SWISSPROT: DAPF_EDWI9

ID   DAPF_EDWI9              Reviewed;         274 AA.
AC   C5BBD4;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 47.
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=NT01EI_0114;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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: LL-2,6-diaminoheptanedioate = meso-
CC       diaminoheptanedioate. {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; CP001600; ACR67369.1; -; Genomic_DNA.
DR   RefSeq; WP_015869588.1; NC_012779.2.
DR   ProteinModelPortal; C5BBD4; -.
DR   SMR; C5BBD4; -.
DR   STRING; 634503.NT01EI_0114; -.
DR   EnsemblBacteria; ACR67369; ACR67369; NT01EI_0114.
DR   GeneID; 7959828; -.
DR   KEGG; eic:NT01EI_0114; -.
DR   PATRIC; fig|634503.3.peg.103; -.
DR   eggNOG; ENOG4105E4Z; Bacteria.
DR   eggNOG; COG0253; LUCA.
DR   HOGENOM; HOG000220466; -.
DR   KO; K01778; -.
DR   OMA; MCGNGGR; -.
DR   OrthoDB; POG091H01QC; -.
DR   UniPathway; UPA00034; UER00025.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008837; F:diaminopimelate epimerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
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; C5BBD4.
DR   SWISS-2DPAGE; C5BBD4.
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm; Isomerase;
KW   Lysine biosynthesis; Reference proteome.
FT   CHAIN         1    274       Diaminopimelate epimerase.
FT                                /FTId=PRO_1000204059.
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;  30266 MW;  637061F77C66D8A7 CRC64;
     MQFAKMHGLG NDFMVVDAVT QNVYFSPELI RRLADRHTGV GFDQLLVVEP PYDPDLDFHY
     RIFNADGSEV AQCGNGARCF ARFVRIKGLT NRRDIRVSTQ NSRMTLHVGE DDRVTVNMGE
     PQFEPGRIPF KAAKAEKTYI LRVAQQTVLC GAVSMGNPHC VLQVEDISRA QVELLGPSLE
     SHERFPERVN VGFMQVVERS HIRLRVYERG AGETQACGSG ACAAVAVGIQ QGLLDEQVQV
     DLPGGTLHIR WPGPGTPLLM TGPAAHVYDG FIHL
//

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