ID DAPB_BLOPB Reviewed; 282 AA. AC Q493S0; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 16-JUN-2009, entry version 27. DE RecName: Full=Dihydrodipicolinate reductase; DE Short=DHPR; DE EC=1.3.1.26; GN Name=dapB; OrderedLocusNames=BPEN_125; OS Blochmannia pennsylvanicus (strain BPEN). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia. OX NCBI_TaxID=291272; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16077009; DOI=10.1101/gr.3771305; RA Degnan P.H., Lazarus A.B., Wernegreen J.J.; RT "Genome sequence of Blochmannia pennsylvanicus indicates parallel RT evolutionary trends among bacterial mutualists of insects."; RL Genome Res. 15:1023-1033(2005). CC -!- CATALYTIC ACTIVITY: 2,3,4,5-tetrahydrodipicolinate + NAD(P)(+) = CC 2,3-dihydrodipicolinate + NAD(P)H. CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; tetrahydrodipicolinate from L-aspartate: step 4/4. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the dihydrodipicolinate reductase 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; CP000016; AAZ40765.1; -; Genomic_DNA. DR RefSeq; YP_277638.1; -. DR GeneID; 3563160; -. DR GenomeReviews; CP000016_GR; BPEN_125. DR KEGG; bpn:BPEN_125; -. DR HOGENOM; Q493S0; -. DR OMA; Q493S0; TIGFSTI. DR BioCyc; CBLO291272:BPEN_125-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0008839; F:dihydrodipicolinate reductase activity; IEA:HAMAP. DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:HAMAP. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR HAMAP; MF_00102; -; 1. DR InterPro; IPR000846; DapB. DR InterPro; IPR011770; DapB_bac/pln. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR PANTHER; PTHR20836; DapB_bac/pln; 1. DR Pfam; PF05173; DapB_C; 1. DR Pfam; PF01113; DapB_N; 1. DR ProDom; PD004105; DapB; 1. DR TIGRFAMs; TIGR00036; dapB; 1. DR PROSITE; PS01298; DAPB; FALSE_NEG. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Diaminopimelate biosynthesis; Lysine biosynthesis; NADP; KW Oxidoreductase. FT CHAIN 1 282 Dihydrodipicolinate reductase. FT /FTId=PRO_0000228329. SQ SEQUENCE 282 AA; 30864 MW; 5309FAC65A17FA81 CRC64; MSDTPLRIAV TGVTGRMGKE IVTCIVKEEK QFSQEIVLGA AITRLNTNIC GMDAGILINT DALGIEITDN LESIKDNFDV LVDFTAPDIS IEYLKFCVNN NKNIVIGTTG FNQIHKNIIL NASHKIGIVF SSNFSIGVAL ISKLLHKITQ VIGNTSDISI IETHHNRKRD IPSGTSLTMQ NIIVNALRSI HSNRIIDSNL DSTTYSPASS YKDILIHSIR AGDVVGEHTV LFAGPGERLE ITHKASDRLI FAHGALRAAF WVGRDKIGLF DISDILEMDT LL //