ID DAPB_BACCR Reviewed; 266 AA. AC Q81FP4; DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 02-SEP-2026, entry version 127. 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=BC_1532; OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Bacillus; Bacillus cereus group. OX NCBI_TaxID=226900; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB RC 9373 / NCTC 2599 / NRRL B-3711; RX PubMed=12721630; DOI=10.1038/nature01582; RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G., RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.; RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus RT anthracis."; RL Nature 423:87-91(2003). 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 + NAD(+) + H2O = (2S,4S)-4- CC hydroxy-2,3,4,5-tetrahydrodipicolinate + NADH + H(+); 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 + NADP(+) + H2O = (2S,4S)- CC 4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADPH + H(+); 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; AE016877; AAP08512.1; -; Genomic_DNA. DR RefSeq; WP_000658813.1; NC_004722.1. DR AlphaFoldDB; Q81FP4; -. DR SMR; Q81FP4; -. DR STRING; 226900.BC_1532; -. DR GeneID; 50192310; -. DR KEGG; bce:BC1532; -. DR PATRIC; fig|226900.8.peg.1509; -. DR HOGENOM; CLU_047479_0_1_9; -. DR OrthoDB; 9790352at2; -. DR UniPathway; UPA00034; UER00018. DR Proteomes; UP000001417; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase activity; IEA:UniProtKB-EC. DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule. DR CDD; cd02274; DHDPR_N; 1. DR FunFam; 3.30.360.10:FF:000009; 4-hydroxy-tetrahydrodipicolinate reductase; 1. DR FunFam; 3.40.50.720:FF:000180; 4-hydroxy-tetrahydrodipicolinate reductase; 1. DR Gene3D; 3.30.360.10; Dihydrodipicolinate Reductase, domain 2; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. 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 NCBIfam; TIGR00036; dapB; 1. DR PANTHER; PTHR20836:SF0; 4-HYDROXY-TETRAHYDRODIPICOLINATE REDUCTASE 1, CHLOROPLASTIC-RELATED; 1. DR PANTHER; PTHR20836; DIHYDRODIPICOLINATE REDUCTASE; 1. DR Pfam; PF05173; DapB_C; 1. DR Pfam; PF01113; DapB_N; 1. DR PIRSF; PIRSF000161; DHPR; 1. DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS01298; DAPB; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Cytoplasm; Diaminopimelate biosynthesis; KW Lysine biosynthesis; NAD; NADP; Oxidoreductase; Reference proteome. FT CHAIN 1..266 FT /note="4-hydroxy-tetrahydrodipicolinate reductase" FT /id="PRO_0000141409" FT ACT_SITE 155 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102" FT ACT_SITE 159 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102" FT BINDING 10..15 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102" FT BINDING 38 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102" FT BINDING 99..101 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102" FT BINDING 125..128 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102" FT BINDING 156 FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate" FT /ligand_id="ChEBI:CHEBI:16845" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102" FT BINDING 165..166 FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate" FT /ligand_id="ChEBI:CHEBI:16845" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102" SQ SEQUENCE 266 AA; 29197 MW; C945C50657245F8F CRC64; MKEIKVIIAG PRGRMGHEAV LLMERTEHFN LVAAVDYKHG GEKISDLPGM PALHAPIYAD LHTCLDEVEA DVLLDLTTPE VGKQHVTLAV ERGLRSVIGT TGFTEEELTR LTENAKEKAV GTIIAPNFAI GAVLMMKFSQ MAAKYFQDVE VIELHHDQKL DAPSGTAVKT VELIRQNRES KQQGHPNEVE QLAGARGANV DGIHIHSVRL PGLIAHQEVM FGGDGQMLTV RHDSFNRASF MSGVKLSIET VMNLDHLVYG LENIID //