ID DAPB_BUCAP Reviewed; 273 AA. AC Q8K9Z5; DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 25-NOV-2008, entry version 47. DE RecName: Full=Dihydrodipicolinate reductase; DE Short=DHPR; DE EC=1.3.1.26; GN Name=dapB; OrderedLocusNames=BUsg_139; OS Buchnera aphidicola subsp. Schizaphis graminum. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Buchnera. OX NCBI_TaxID=98794; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22084549; PubMed=12089438; DOI=10.1126/science.1071278; RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.; RT "50 million years of genomic stasis in endosymbiotic bacteria."; RL Science 296:2376-2379(2002). 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; AE013218; AAM67707.1; -; Genomic_DNA. DR RefSeq; NP_660496.1; -. DR HSSP; P04036; 1DRW. DR GeneID; 1005956; -. DR GenomeReviews; AE013218_GR; BUsg_139. DR KEGG; bas:BUsg139; -. DR HOGENOM; Q8K9Z5; -. DR BioCyc; BAPH198804:BUSG139-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:HAMAP. 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. 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 1 273 Dihydrodipicolinate reductase. FT /FTId=PRO_0000141420. SQ SEQUENCE 273 AA; 30674 MW; E49AD0EADB67042F CRC64; MKKKITRIAI TGAMGRMGQV LIKEIQKNKN TVLTAALVKN NHPLIGQNIG EKIGIGKTSV SISSDINIEK NDFDVLIDFT KPSGTFYFLE QCYEFKKNMI IGTTGFSEKE IKTINSYAKK IALIKASNFS IGINLLYQLI QKTTKILGNT SDIDIIEYHH RNKIDIPSGT ALSIGENISK VMNWELNKHS LYYTKGITKK IRETKKIGFS SIRSGNIIGK HTVLFSSSDE EIKITHSAFN RESFAKGAIE AAVWIHEKKH GLFNMNDILK DKF //