ID DAPB_ACICJ Reviewed; 247 AA. AC A5FXD9; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 12-JUN-2007, sequence version 1. DT 16-JUN-2009, entry version 15. DE RecName: Full=Dihydrodipicolinate reductase; DE Short=DHPR; DE EC=1.3.1.26; GN Name=dapB; OrderedLocusNames=Acry_1055; OS Acidiphilium cryptum (strain JF-5). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acidiphilium. OX NCBI_TaxID=349163; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Sims D., Brettin T., Bruce D., Han C., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Magnuson T., RA Richardson P.; RT "Complete sequence of chromosome of Acidiphilium cryptum JF-5."; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. 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; CP000697; ABQ30271.1; -; Genomic_DNA. DR RefSeq; YP_001234190.1; -. DR GeneID; 5162498; -. DR GenomeReviews; CP000697_GR; Acry_1055. DR KEGG; acr:Acry_1055; -. DR OMA; A5FXD9; 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 1 247 Dihydrodipicolinate reductase. FT /FTId=PRO_1000008529. SQ SEQUENCE 247 AA; 25070 MW; CB148C8846410468 CRC64; MNGADLRIGI AGITGRMGKL LAEAVPLAGA TLAGGIGRDG DLAALARESD VVIDFTVAAT VSRHAGILAA AGTPWVLGTT GFDPAAEADI ADAAARIPVF QAANFAPGVN LVIALAERLG ATLAAETHDA EILEMHHRQK IDAPSGTALA IGAAVARGRG VDLAAVKDSG RDGHTGKRET GAIGFAALRG GQIVGSHSAI FTSAVEQITL THHALDRRIF AEGAVRAALW LAGRAPGRYG MRDLLGL //