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 02-DEC-2020, entry version 81. 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., Malfatti S., RA Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Tiedje J., Richardson P.; RT "Complete sequence of chromosome 1 of Burkholderia cenocepacia MC0-3."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate CC (HTPA) to tetrahydrodipicolinate. {ECO:0000255|HAMAP-Rule:MF_00102}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4- CC hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; CC Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00102}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)- CC 4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; CC Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={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 reductase CC (DHDPR), catalyzing the conversion of dihydrodipicolinate to CC tetrahydrodipicolinate. However, it was shown in E.coli that the CC substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) CC but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid CC (HTPA), the product released by the DapA-catalyzed reaction. CC {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 SMR; B1JVG6; -. DR EnsemblBacteria; ACA89796; ACA89796; Bcenmc03_0618. DR KEGG; bcm:Bcenmc03_0618; -. DR HOGENOM; CLU_047479_2_1_4; -. DR OMA; PNKADAP; -. DR BioCyc; BCEN406425:G1GBC-660-MONOMER; -. 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:0051287; F:NAD binding; IEA:UniProtKB-UniRule. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule. DR GO; GO:0016726; F:oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor; IEA:UniProtKB-UniRule. DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule. 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; IPR036291; NAD(P)-bd_dom_sf. 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; 1. DR TIGRFAMs; TIGR00036; dapB; 1. DR PROSITE; PS01298; DAPB; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Cytoplasm; Diaminopimelate biosynthesis; KW Lysine biosynthesis; NAD; NADP; Oxidoreductase. FT CHAIN 1..265 FT /note="4-hydroxy-tetrahydrodipicolinate reductase" FT /id="PRO_1000093947" FT NP_BIND 7..12 FT /note="NAD(P)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102" FT NP_BIND 96..98 FT /note="NAD(P)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102" FT NP_BIND 120..123 FT /note="NAD(P)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102" FT REGION 163..164 FT /note="Substrate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102" FT ACT_SITE 153 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102" FT ACT_SITE 157 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102" FT BINDING 33 FT /note="NAD" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102" FT BINDING 34 FT /note="NADP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102" FT BINDING 154 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-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 //