ID DAPB_ANADE Reviewed; 270 AA. AC Q2IGX0; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 1. DT 16-JUN-2009, entry version 24. DE RecName: Full=Dihydrodipicolinate reductase; DE Short=DHPR; DE EC=1.3.1.26; GN Name=dapB; OrderedLocusNames=Adeh_4068; OS Anaeromyxobacter dehalogenans (strain 2CP-C). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Myxococcaceae; Anaeromyxobacter. OX NCBI_TaxID=290397; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., RA Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M., RA Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., RA Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.; RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C."; RL Submitted (JAN-2006) 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; CP000251; ABC83832.1; -; Genomic_DNA. DR RefSeq; YP_467269.1; -. DR GeneID; 3888259; -. DR GenomeReviews; CP000251_GR; Adeh_4068. DR KEGG; ade:Adeh_4068; -. DR HOGENOM; Q2IGX0; -. DR OMA; Q2IGX0; TIGFSTI. DR BioCyc; ADEH290397:ADEH_4068-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; 2. 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 1 270 Dihydrodipicolinate reductase. FT /FTId=PRO_1000008532. SQ SEQUENCE 270 AA; 27724 MW; AB021B5366761657 CRC64; MTKVVVTGAA GRMGTQIVRL VRATPGLSVS GAVERAGSPA IGKDAGTLAG GEPLGVAVVD DLAKALPGAD VVIDFTSHEA SVRHAQACAA AGVALVIGST GFTPDAKAKV AEAARKVPVV LSPNMSVGVN VVFELVRQAA RVLGDAYDVE VVEIHHKHKR DAPSGTAVRL GEVAAEALGR APADALAYSR HGILGERPPW QIGIQTLRGG DVVGEHTVFF CGEGERVEIT HRATSREQFA RGAARAAAWL PGKAPGVYDM ADVLGLRGGK //