ID DAPB_SYNR3 Reviewed; 273 AA. AC A5GSL5; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 12-JUN-2007, sequence version 1. DT 02-SEP-2026, entry version 102. 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=SynRCC307_0971; OS Synechococcus sp. (strain RCC307). OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales; OC Synechococcaceae; Synechococcus. OX NCBI_TaxID=316278; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RCC307; RG Genoscope; RL Submitted (MAY-2006) 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 + 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; CT978603; CAK27874.1; -; Genomic_DNA. DR AlphaFoldDB; A5GSL5; -. DR SMR; A5GSL5; -. DR STRING; 316278.SynRCC307_0971; -. DR KEGG; syr:SynRCC307_0971; -. DR eggNOG; COG0289; Bacteria. DR HOGENOM; CLU_047479_0_0_3; -. DR OrthoDB; 9790352at2; -. DR UniPathway; UPA00034; UER00018. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. 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 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..273 FT /note="4-hydroxy-tetrahydrodipicolinate reductase" FT /id="PRO_1000008654" FT ACT_SITE 162 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102" FT ACT_SITE 166 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102" FT BINDING 11..16 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102" FT BINDING 106..108 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102" FT BINDING 163 FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate" FT /ligand_id="ChEBI:CHEBI:16845" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102" FT BINDING 172..173 FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate" FT /ligand_id="ChEBI:CHEBI:16845" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102" SQ SEQUENCE 273 AA; 28975 MW; 939C6B6AD20882D2 CRC64; MTDQIPVVVA GALGRMGAEV IKAVHTAGDC QLVGAIDTCP GREGEDVGLA LGLGELEVAL TQDFEGALCL ASQQHPGAVL VDFTHPKVVY EHTRAAIAYG VTPVIGTTGL APEQLQELAS FAAKASMGGA VIPNFSVGMV LLQQAAAAAA RFYDHAELVE LHHNRKADAP SGTCIKTAEL MEELGKQFNA QEVEEHETLE GSRGGLRPSG LRLHSIRLPG LVAHQEVQFG GAGERYVLRH DTFDRAAYMP GVLLTVRKVR QLGALVYGLE RLL //