ID Q6ME33_PARUW Unreviewed; 269 AA.
AC Q6ME33;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 13-NOV-2013, entry version 68.
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.
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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 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
//
