ID DAPB_BRASB Reviewed; 272 AA. AC A5E8K0; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 12-JUN-2007, sequence version 1. DT 16-JUN-2009, entry version 18. DE RecName: Full=Dihydrodipicolinate reductase; DE Short=DHPR; DE EC=1.3.1.26; GN Name=dapB; OrderedLocusNames=BBta_0197; OS Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=288000; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17540897; DOI=10.1126/science.1139548; RA Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.-C., RA Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L., RA Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., RA Rouy Z., Mangenot S., Segurens B., Dossat C., Franck W.L., RA Chang W.-S., Saunders E., Bruce D., Richardson P., Normand P., RA Dreyfus B., Pignol D., Stacey G., Emerich D., Vermeglio A., RA Medigue C., Sadowsky M.; RT "Legumes symbioses: absence of nod genes in photosynthetic RT bradyrhizobia."; RL Science 316:1307-1312(2007). 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 -!- 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; CP000494; ABQ32494.1; -; Genomic_DNA. DR RefSeq; YP_001236400.1; -. DR GeneID; 5150942; -. DR GenomeReviews; CP000494_GR; BBta_0197. DR KEGG; bbt:BBta_0197; -. DR OMA; A5E8K0; TIGFSTI. 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; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Diaminopimelate biosynthesis; Lysine biosynthesis; NADP; KW Oxidoreductase. FT CHAIN 1 272 Dihydrodipicolinate reductase. FT /FTId=PRO_1000008537. SQ SEQUENCE 272 AA; 27889 MW; 916B50431CD5B294 CRC64; MSKMRLIVAG AGGRMGRALV RAIADSDGAE LAGALEAPGS ELIGKDAGVL AGLPANGIKL SGDLWTMSAE ADGILDFTVP AATIANVAIA AERGIAHIIG TTGLSASDDA VIKSVTKRAI VVQSGNMSLG VNLLSALVKQ VAKSLDAGFD IEILEMHHKH KVDAPSGTAL MLGRAAAEGR GVVLDQHSAR GRDGITGERR SGDIGFASLR GGTAAGDHSV IFAGPSERLV LSHQAEDRMI FAHGALKAAL WAHGKPPGYY TMSDVLGLKD LF //