ID DAPB_BACA2 Reviewed; 267 AA. AC A7Z600; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 1. DT 16-JUN-2009, entry version 14. DE RecName: Full=Dihydrodipicolinate reductase; DE Short=DHPR; DE EC=1.3.1.26; GN Name=dapB; OrderedLocusNames=RBAM_020640; OS Bacillus amyloliquefaciens (strain FZB42). OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=326423; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17704766; DOI=10.1038/nbt1325; RA Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K., RA Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H., RA Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H., RA Strittmatter A., Gottschalk G., Borriss R.; RT "Comparative analysis of the complete genome sequence of the plant RT growth-promoting bacterium Bacillus amyloliquefaciens FZB42."; RL Nat. Biotechnol. 25:1007-1014(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; CP000560; ABS74426.1; -; Genomic_DNA. DR RefSeq; YP_001421657.1; -. DR GeneID; 5461680; -. DR GenomeReviews; CP000560_GR; RBAM_020640. DR KEGG; bay:RBAM_020640; -. DR OMA; A7Z600; VLMMKFA. 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 1 267 Dihydrodipicolinate reductase. FT /FTId=PRO_1000008534. SQ SEQUENCE 267 AA; 29375 MW; 17245042C649E9D8 CRC64; MSNETIKVVI AGPRGRMGQE AVKLAVRTPH FELVGAIDHT YDQQTLREVM SADSDALIYT DIRACFQETK PDVLIDLTTP EIGKKHTKAA LEHGVRPVVG TTGFSEADLE ELQALTEEKG IGAIIAPNFA LGAVLMMKFS QMAANYFEDV EIIELHHDQK LDAPSGTALK TAEMISSVRT EKQQGHPDEK EILPGARGAE LNGIRLHSVR LPGLIAHQEV MFGMDGQTLK LRHDSYNRAS FMSGVKLSVE QVMKIDQLVY GLENIID //