ID DAPB_METBF Reviewed; 263 AA. AC Q46DC3; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 04-NOV-2026, entry version 124. 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=Mbar_A1151; OS Methanosarcina barkeri (strain Fusaro / DSM 804). OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group; OC Methanomicrobia; Methanosarcinales; Methanosarcinaceae; Methanosarcina. OX NCBI_TaxID=269797; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Fusaro / DSM 804; RX PubMed=16980466; DOI=10.1128/jb.00810-06; RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S., RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.; RT "The Methanosarcina barkeri genome: comparative analysis with RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive RT rearrangement within methanosarcinal genomes."; RL J. Bacteriol. 188:7922-7931(2006). 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; CP000099; AAZ70119.1; -; Genomic_DNA. DR AlphaFoldDB; Q46DC3; -. DR SMR; Q46DC3; -. DR STRING; 269797.Mbar_A1151; -. DR PaxDb; 269797-Mbar_A1151; -. DR KEGG; mba:Mbar_A1151; -. DR eggNOG; arCOG04393; Archaea. DR HOGENOM; CLU_047479_2_1_2; -. DR OMA; AAAPCVN; -. DR OrthoDB; 195035at2157; -. DR UniPathway; UPA00034; UER00018. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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 GO; GO:0009085; P:L-lysine biosynthetic process; IEA:InterPro. DR CDD; cd02274; DHDPR_N; 1. DR FunFam; 3.30.360.10:FF:000004; 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. FT CHAIN 1..263 FT /note="4-hydroxy-tetrahydrodipicolinate reductase" FT /id="PRO_0000228407" FT ACT_SITE 157 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102" FT ACT_SITE 161 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102" FT BINDING 8..13 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102" FT BINDING 34 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" 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 158 FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate" FT /ligand_id="ChEBI:CHEBI:16845" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102" FT BINDING 167..168 FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate" FT /ligand_id="ChEBI:CHEBI:16845" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102" SQ SEQUENCE 263 AA; 28098 MW; E5C6CAB943AB4EA0 CRC64; MINVAVLGAC GRMGSLIVEN VINSKDMQLV AAFDISYFGR DAGEFARVGK LGVQISDVKN LETVLKESKA DVLIDFTAAG ATVVNAPIAA RAGVNLIIGT TGLTPEQRAV IDEAIQEGQV SAVISPNYSV GVNVFFKIIR EAAKYLADYD IEIIEAHHNQ KKDAPSGTAL RAADIISEAV GGREYVYGRE GIAPRGKEIG IHGVRAGDIT GDHIVLFAGN SERIEIKHIA HSRQIFAKGA VRAAEWVCRQ KPGIYSMDDV LGL //