ID Q6ME33_PARUW Unreviewed; 269 AA.
AC Q6ME33;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 11-JUN-2014, entry version 72.
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; LIVEPPY; -.
DR OrthoDB; EOG6ND0M5; -.
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; 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; 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
FT similarity){EA3}.
FT ACT_SITE 206 206 Proton donor/acceptor (By
FT similarity){EA3}.
FT BINDING 13 13 Substrate (By similarity){EA3}.
FT BINDING 46 46 Substrate (By similarity){EA3}.
FT BINDING 64 64 Substrate (By similarity){EA3}.
FT BINDING 178 178 Substrate (By similarity){EA3}.
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
//
