ID DAPF_CLOPE Reviewed; 272 AA. AC Q46185; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 31-JAN-2002, sequence version 2. DT 16-JUN-2009, entry version 61. DE RecName: Full=Diaminopimelate epimerase; DE Short=DAP epimerase; DE EC=5.1.1.7; GN Name=dapF; OrderedLocusNames=CPE1846; OS Clostridium perfringens. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1502; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=13 / Type A; RX MEDLINE=21664373; PubMed=11792842; DOI=10.1073/pnas.022493799; RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., RA Shiba T., Ogasawara N., Hattori M., Kuhara S., Hayashi H.; RT "Complete genome sequence of Clostridium perfringens, an anaerobic RT flesh-eater."; RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 168-238. RC STRAIN=CPN50; RX MEDLINE=96032407; PubMed=7559358; RA Katayama S., Dupuy B., Garnier T., Cole S.T.; RT "Rapid expansion of the physical and genetic map of the chromosome of RT Clostridium perfringens CPN50."; RL J. Bacteriol. 177:5680-5685(1995). CC -!- CATALYTIC ACTIVITY: LL-2,6-diaminoheptanedioate = meso- CC diaminoheptanedioate. CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; DL-diaminopimelate from LL-diaminopimelate: step 1/1. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the diaminopimelate epimerase family. CC -!- SEQUENCE CAUTION: CC Sequence=CAA60229.1; Type=Frameshift; Positions=181; 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; BA000016; BAB81552.1; -; Genomic_DNA. DR EMBL; X86511; CAA60229.1; ALT_FRAME; Genomic_DNA. DR RefSeq; NP_562762.1; -. DR HSSP; P44859; 1GQZ. DR GeneID; 990155; -. DR GenomeReviews; BA000016_GR; CPE1846. DR KEGG; cpe:CPE1846; -. DR NMPDR; fig|195102.1.peg.1909; -. DR HOGENOM; Q46185; -. DR OMA; Q46185; NIAFIEN. DR BioCyc; CPER195102:CPE1846-MON; -. DR BRENDA; 5.1.1.7; 2406. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008837; F:diaminopimelate epimerase activity; IEA:HAMAP. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopime...; IEA:HAMAP. DR HAMAP; MF_00197; -; 1. DR InterPro; IPR001653; DAP_epimerase. DR InterPro; IPR018510; DAP_epimerase_CS. 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; Isomerase; KW Lysine biosynthesis. FT CHAIN 1 272 Diaminopimelate epimerase. FT /FTId=PRO_0000149835. FT ACT_SITE 72 72 By similarity. FT ACT_SITE 217 217 By similarity. FT CONFLICT 183 183 E -> D (in Ref. 2). FT CONFLICT 193 193 F -> S (in Ref. 2; CAA60229). FT CONFLICT 201 201 T -> P (in Ref. 2; CAA60229). FT CONFLICT 206 206 T -> P (in Ref. 2; CAA60229). FT CONFLICT 230 230 K -> N (in Ref. 2; CAA60229). SQ SEQUENCE 272 AA; 30084 MW; 60DB1A8527815C05 CRC64; MKFSKMHGNG NDFIVIEDLN NEYLGKEGEI AQKMCHRRFG IGADGILIVR KNENCDIEMV IINSDGSYAA MCGNGIRCFA KYVYEKGIVK KDVLDVLTGD GVKRIFLEIE NDKVKTINVN MGFGDFKPKN IPALCDEEII EKKVSVGNGN FEITSLLMGV PHTIIFEEEK YPIECGRDIE KYELFPQGTN VNFCKVIDRN TMEVRTWERG AGPTLACGTG NCASVIAANK LGLVDKEVKV IVPGGELKVN IEDDGVKMIG NASFICDGTY LF //