ID DAPB_HELPY Reviewed; 254 AA. AC P94844; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 02-SEP-2026, entry version 147. 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=HP_0510; OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori). OC Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria; OC Campylobacterales; Helicobacteraceae; Helicobacter. OX NCBI_TaxID=85962; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=DSM 4867 / CCUG 17874 / NCTC 11638; RA Clairoux N., Boissinot M.; RT "Sequence of the dihydrodipicolinate reductase gene (dapB) from RT Helicobacter pylori and complementation in Escherichia coli."; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700392 / 26695; RX PubMed=9252185; DOI=10.1038/41483; RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A., RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.; RT "The complete genome sequence of the gastric pathogen Helicobacter RT pylori."; RL Nature 388:539-547(1997). 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 -!- INTERACTION: CC P94844; O25114: HP_0347; NbExp=3; IntAct=EBI-7497752, EBI-7497815; 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; U75328; AAB39718.1; -; Genomic_DNA. DR EMBL; AE000511; AAD07574.1; -; Genomic_DNA. DR PIR; F64583; F64583. DR RefSeq; WP_000690507.1; NC_018939.1. DR AlphaFoldDB; P94844; -. DR SMR; P94844; -. DR DIP; DIP-3440N; -. DR FunCoup; P94844; 365. DR IntAct; P94844; 1. DR MINT; P94844; -. DR STRING; 85962.HP_0510; -. DR PaxDb; 85962-HP_0510; -. DR EnsemblBacteria; AAD07574; AAD07574; HP_0510. DR KEGG; heo:C694_02620; -. DR KEGG; hpy:HP_0510; -. DR PATRIC; fig|85962.47.peg.548; -. DR eggNOG; COG0289; Bacteria. DR InParanoid; P94844; -. DR OrthoDB; 9790352at2; -. DR PhylomeDB; P94844; -. DR UniPathway; UPA00034; UER00018. DR Proteomes; UP000000429; 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 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 1: Evidence at protein level; KW Amino-acid biosynthesis; Cytoplasm; Diaminopimelate biosynthesis; KW Lysine biosynthesis; NAD; NADP; Oxidoreductase; Reference proteome. FT CHAIN 1..254 FT /note="4-hydroxy-tetrahydrodipicolinate reductase" FT /id="PRO_0000141445" FT ACT_SITE 147 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102" FT ACT_SITE 151 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102" FT BINDING 7..12 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102" FT BINDING 35 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102" FT BINDING 91..93 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102" FT BINDING 115..118 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102" FT BINDING 148 FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate" FT /ligand_id="ChEBI:CHEBI:16845" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102" FT BINDING 157..158 FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate" FT /ligand_id="ChEBI:CHEBI:16845" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102" FT CONFLICT 22 FT /note="G -> E (in Ref. 1; AAB39718)" FT /evidence="ECO:0000305" FT CONFLICT 28 FT /note="A -> V (in Ref. 1; AAB39718)" FT /evidence="ECO:0000305" FT CONFLICT 44 FT /note="S -> A (in Ref. 1; AAB39718)" FT /evidence="ECO:0000305" FT CONFLICT 76 FT /note="N -> H (in Ref. 1; AAB39718)" FT /evidence="ECO:0000305" FT CONFLICT 80 FT /note="A -> T (in Ref. 1; AAB39718)" FT /evidence="ECO:0000305" FT CONFLICT 104 FT /note="Q -> K (in Ref. 1; AAB39718)" FT /evidence="ECO:0000305" FT CONFLICT 115 FT /note="A -> V (in Ref. 1; AAB39718)" FT /evidence="ECO:0000305" FT CONFLICT 120 FT /note="I -> L (in Ref. 1; AAB39718)" FT /evidence="ECO:0000305" FT CONFLICT 132 FT /note="T -> A (in Ref. 1; AAB39718)" FT /evidence="ECO:0000305" FT CONFLICT 144 FT /note="I -> V (in Ref. 1; AAB39718)" FT /evidence="ECO:0000305" FT CONFLICT 154 FT /note="I -> A (in Ref. 1; AAB39718)" FT /evidence="ECO:0000305" FT CONFLICT 179 FT /note="I -> T (in Ref. 1; AAB39718)" FT /evidence="ECO:0000305" SQ SEQUENCE 254 AA; 27827 MW; 96DBC96B76C5BE3D CRC64; MKIGVYGASG RIGKLLLEEL KGGYKGLALS SVFVRQKCET DFSSFSHAPL VTNDLKAFVR ACECVIDFSL PKGVDNLLEA LLECPKILVS GTTGLEKETL EKMQQLALKA PLLHAHNMSI GIMMLNQLAF LTSLKLKDAD IEIIETHHNL KKDIPSGTAL SLYETCAKAR GYDEKNALIT HREGLRSKES IGIAALRGGD VAGKHTIGFY LEGEYIELSH TATNRSIFAK GALEVALWLK DKAAKKYEIN EMFG //