GenomeNet

Database: UniProt/TrEMBL
Entry: Q6ME33_PARUW
LinkDB: Q6ME33_PARUW
Original site: Q6ME33_PARUW 
ID   Q6ME33_PARUW            Unreviewed;       269 AA.
AC   Q6ME33;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   19-FEB-2014, entry version 70.
DE   RecName: Full=Diaminopimelate epimerase;
DE            Short=DAP epimerase;
DE            EC=5.1.1.7;
GN   Name=dapF; OrderedLocusNames=pc0442;
OS   Protochlamydia amoebophila (strain UWE25).
OC   Bacteria; Chlamydiae; Chlamydiales; Parachlamydiaceae;
OC   Candidatus Protochlamydia.
OX   NCBI_TaxID=264201;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UWE25;
RX   PubMed=15073324; DOI=10.1126/science.1096330;
RA   Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U.,
RA   Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D.,
RA   Rattei T., Mewes H.-W., Wagner M.;
RT   "Illuminating the evolutionary history of chlamydiae.";
RL   Science 304:728-730(2004).
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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: LL-2,6-diaminoheptanedioate = meso-
CC       diaminoheptanedioate.
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the diaminopimelate epimerase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BX908798; CAF23166.1; -; Genomic_DNA.
DR   RefSeq; YP_007441.1; NC_005861.1.
DR   ProteinModelPortal; Q6ME33; -.
DR   STRING; 264201.pc0442; -.
DR   PRIDE; Q6ME33; -.
DR   EnsemblBacteria; CAF23166; CAF23166; pc0442.
DR   GeneID; 2780463; -.
DR   KEGG; pcu:pc0442; -.
DR   PATRIC; 31996186; VBICanPro72727_0446.
DR   eggNOG; COG0253; -.
DR   HOGENOM; HOG000220466; -.
DR   KO; K01778; -.
DR   OMA; LAKQVCH; -.
DR   OrthoDB; EOG6ND0M5; -.
DR   ProtClustDB; CLSK2762174; -.
DR   BioCyc; PAMO264201:GH0M-453-MONOMER; -.
DR   UniPathway; UPA00034; UER00025.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008837; F:diaminopimelate epimerase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_00197; DAP_epimerase; 1.
DR   InterPro; IPR018510; DAP_epimerase_AS.
DR   InterPro; IPR001653; DAP_epimerase_DapF.
DR   PANTHER; PTHR31689:SF0; PTHR31689:SF0; 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; Complete proteome; Cytoplasm; Disulfide bond;
KW   Isomerase; Lysine biosynthesis.
FT   REGION       73     75       Substrate binding (By similarity).
FT   REGION      196    197       Substrate binding (By similarity).
FT   REGION      207    208       Substrate binding (By similarity).
FT   ACT_SITE     73     73       Proton donor/acceptor (By similarity).
FT   ACT_SITE    206    206       Proton donor/acceptor (By similarity).
FT   BINDING      13     13       Substrate (By similarity).
FT   BINDING      46     46       Substrate (By similarity).
FT   BINDING      64     64       Substrate (By similarity).
FT   BINDING     178    178       Substrate (By similarity).
FT   SITE        146    146       Important for catalytic activity (By
FT                                similarity).
FT   SITE        196    196       Important for catalytic activity (By
FT                                similarity).
FT   DISULFID     73    206       Size: 249-333 (By similarity).
SQ   SEQUENCE   269 AA;  30111 MW;  860051C3331CA36A CRC64;
     MQWSFTKYVG CGNDFILFDN RNGKFPFSIP LIQQLCHRQW GVGADGIILL ENSTIAHARM
     RIFNADGSEA EMCGNGLRCL IDWMESLNIL HSIYSIETNN HVLKAWKSAS NITIEMGSPN
     KLNWNVPISF ESKIYYVHSL NTGVPHIILF AENIEQFPLE RMGPFIRYHP LWKPDGTNFS
     IVQHLHGQTF MIRTYERGVE AETLACGTGA TAAALAAAFQ YRLSAPISMQ TRSGICLEIG
     FTLLNQKFTN VTMTGPALAV FNGSIKLES
//
DBGET integrated database retrieval system