ID DAPB_BURCC Reviewed; 265 AA. AC B1JVG6; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2008, sequence version 1. DT 10-MAY-2017, entry version 68. DE RecName: Full=4-hydroxy-tetrahydrodipicolinate reductase {ECO:0000255|HAMAP-Rule:MF_00102}; DE Short=HTPA reductase {ECO:0000255|HAMAP-Rule:MF_00102}; DE EC=1.17.1.8 {ECO:0000255|HAMAP-Rule:MF_00102}; GN Name=dapB {ECO:0000255|HAMAP-Rule:MF_00102}; GN OrderedLocusNames=Bcenmc03_0618; OS Burkholderia cenocepacia (strain MC0-3). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=406425; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC0-3; RA Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L., RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Tiedje J., Richardson P.; RT "Complete sequence of chromosome 1 of Burkholderia cenocepacia MC0- RT 3."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the conversion of 4-hydroxy- CC tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. CC {ECO:0000255|HAMAP-Rule:MF_00102}. CC -!- CATALYTIC ACTIVITY: (S)-2,3,4,5-tetrahydropyridine-2,6- CC dicarboxylate + NAD(P)(+) + H(2)O = (2S,4S)-4-hydroxy-2,3,4,5- CC tetrahydrodipicolinate + NAD(P)H. {ECO:0000255|HAMAP- CC Rule:MF_00102}. CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. CC {ECO:0000255|HAMAP-Rule:MF_00102}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00102}. CC -!- SIMILARITY: Belongs to the DapB family. {ECO:0000255|HAMAP- CC Rule:MF_00102}. CC -!- CAUTION: Was originally thought to be a dihydrodipicolinate CC reductase (DHDPR), catalyzing the conversion of CC dihydrodipicolinate to tetrahydrodipicolinate. However, it was CC shown in E.coli that the substrate of the enzymatic reaction is CC not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy- CC 2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by CC the DapA-catalyzed reaction. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000958; ACA89796.1; -; Genomic_DNA. DR RefSeq; WP_006476927.1; NC_010508.1. DR ProteinModelPortal; B1JVG6; -. DR SMR; B1JVG6; -. DR EnsemblBacteria; ACA89796; ACA89796; Bcenmc03_0618. DR KEGG; bcm:Bcenmc03_0618; -. DR PATRIC; 19088196; VBIBurCen61509_0634. DR HOGENOM; HOG000227153; -. DR KO; K00215; -. DR OMA; YAREGHT; -. DR OrthoDB; POG091H01P6; -. DR UniPathway; UPA00034; UER00018. DR Proteomes; UP000002169; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase; IEA:UniProtKB-EC. DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway. DR HAMAP; MF_00102; DapB; 1. DR InterPro; IPR022663; DapB_C. DR InterPro; IPR000846; DapB_N. DR InterPro; IPR022664; DapB_N_CS. DR InterPro; IPR023940; DHDPR_bac. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR20836; PTHR20836; 1. DR Pfam; PF05173; DapB_C; 1. DR Pfam; PF01113; DapB_N; 1. DR PIRSF; PIRSF000161; DHPR; 1. DR SUPFAM; SSF51735; SSF51735; 2. 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; NAD; NADP; KW Oxidoreductase; Reference proteome. FT CHAIN 1 265 4-hydroxy-tetrahydrodipicolinate FT reductase. FT /FTId=PRO_1000093947. FT NP_BIND 7 12 NAD(P). {ECO:0000255|HAMAP- FT Rule:MF_00102}. FT NP_BIND 96 98 NAD(P). {ECO:0000255|HAMAP- FT Rule:MF_00102}. FT NP_BIND 120 123 NAD(P). {ECO:0000255|HAMAP- FT Rule:MF_00102}. FT REGION 163 164 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00102}. FT ACT_SITE 153 153 Proton donor/acceptor. FT {ECO:0000255|HAMAP-Rule:MF_00102}. FT ACT_SITE 157 157 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00102}. FT BINDING 33 33 NAD. {ECO:0000255|HAMAP-Rule:MF_00102}. FT BINDING 34 34 NADP. {ECO:0000255|HAMAP-Rule:MF_00102}. FT BINDING 154 154 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00102}. SQ SEQUENCE 265 AA; 27829 MW; C0C01AD9E3E60038 CRC64; MKIAIAGASG RMGRMLIEAV LNDADAQLVG ALDRAGSPFL GQDAGAFLGK DTGVKLTDDL DAVFAQAEYL IDFTRPEGTM AHVEAALRHD VKLVIGTTGF TAEQKADLQA AAARIGIVFA ANMSVGVNVT LKLLEFAAKH FSHGYDIEII EAHHRHKVDA PSGTALMMGE AVAGALGRSL DDCAVYGRHG VTGERDPSSI GFAAVRGGDI VGDHTVLFAG IGERIEITHK SSSRVSYAQG ALRAVRFLSA RGAGLFDMQD VLGLR //