ID C7BJY6_PHOAA Unreviewed; 273 AA. AC C7BJY6; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 27-MAR-2024, entry version 88. DE RecName: Full=4-hydroxy-tetrahydrodipicolinate reductase {ECO:0000256|ARBA:ARBA00038983, ECO:0000256|HAMAP-Rule:MF_00102}; DE Short=HTPA reductase {ECO:0000256|HAMAP-Rule:MF_00102}; DE EC=1.17.1.8 {ECO:0000256|ARBA:ARBA00038983, ECO:0000256|HAMAP-Rule:MF_00102}; GN Name=dapB {ECO:0000256|HAMAP-Rule:MF_00102, GN ECO:0000313|EMBL:CAQ82652.1}; GN OrderedLocusNames=PAU_00560 {ECO:0000313|EMBL:CAQ82652.1}; OS Photorhabdus asymbiotica subsp. asymbiotica (strain ATCC 43949 / 3105-77) OS (Xenorhabdus luminescens (strain 2)). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Morganellaceae; Photorhabdus. OX NCBI_TaxID=553480 {ECO:0000313|EMBL:CAQ82652.1, ECO:0000313|Proteomes:UP000002747}; RN [1] {ECO:0000313|EMBL:CAQ82652.1, ECO:0000313|Proteomes:UP000002747} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43949 / 3105-77 {ECO:0000313|Proteomes:UP000002747}; RX PubMed=19583835; DOI=10.1186/1471-2164-10-302; RA Wilkinson P., Waterfield N.R., Crossman L., Corton C., RA Sanchez-Contreras M., Vlisidou I., Barron A., Bignell A., Clark L., RA Ormond D., Mayho M., Bason N., Smith F., Simmonds M., Churcher C., RA Harris D., Thompson N.R., Quail M., Parkhill J., ffrench-Constant R.H.; RT "Comparative genomics of the emerging human pathogen Photorhabdus RT asymbiotica with the insect pathogen Photorhabdus luminescens."; RL BMC Genomics 10:302-302(2009). CC -!- FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate CC (HTPA) to tetrahydrodipicolinate. {ECO:0000256|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; CC Evidence={ECO:0000256|ARBA:ARBA00036290, ECO:0000256|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; CC Evidence={ECO:0000256|ARBA:ARBA00036097, ECO:0000256|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:0000256|ARBA:ARBA00037922, ECO:0000256|HAMAP-Rule:MF_00102}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00102}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00102}. CC -!- SIMILARITY: Belongs to the DapB family. {ECO:0000256|ARBA:ARBA00006642, CC ECO:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_00102}. 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; FM162591; CAQ82652.1; -; Genomic_DNA. DR AlphaFoldDB; C7BJY6; -. DR STRING; 291112.PAU_00560; -. DR KEGG; pay:PAU_00560; -. DR eggNOG; COG0289; Bacteria. DR UniPathway; UPA00034; UER00018. DR Proteomes; UP000002747; Chromosome. 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 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 {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP- KW Rule:MF_00102}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00102}; KW Diaminopimelate biosynthesis {ECO:0000256|ARBA:ARBA00022915, KW ECO:0000256|HAMAP-Rule:MF_00102}; KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154, ECO:0000256|HAMAP- KW Rule:MF_00102}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00102}; KW NADP {ECO:0000256|HAMAP-Rule:MF_00102}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00102, KW ECO:0000313|EMBL:CAQ82652.1}. FT DOMAIN 6..129 FT /note="Dihydrodipicolinate reductase N-terminal" FT /evidence="ECO:0000259|Pfam:PF01113" FT DOMAIN 132..268 FT /note="Dihydrodipicolinate reductase C-terminal" FT /evidence="ECO:0000259|Pfam:PF05173" FT ACT_SITE 159 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102" FT ACT_SITE 163 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102" FT BINDING 12..17 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102" FT BINDING 38 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102" FT BINDING 39 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102" FT BINDING 102..104 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102" FT BINDING 126..129 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102" FT BINDING 160 FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate" FT /ligand_id="ChEBI:CHEBI:16845" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102" FT BINDING 169..170 FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate" FT /ligand_id="ChEBI:CHEBI:16845" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102" SQ SEQUENCE 273 AA; 28957 MW; 9C657FA42BE8EEB5 CRC64; MADTDIRVAI VGAGGRMGRQ LIQAVHQLSG VVLGVALERS GSSLLGTDAG ELAGIGHIGV TVCDDLKNVV DDFDVLIDFT RPEGTLAHLE ICRRHSKAIV IGTTGFDDEG KQAIKDASAN IPIVFAANFS VGVNLVLKLL EKAAKVMGEY TDIEIIEAHH RHKVDAPSGT ALAMGESIAH ALGRDLKECA VYAREGYTGE RDPKSIGFAT IRAGDIVGEH TAMFADVGER VEITHKASSR MTFANGAVKA ALWLNGKNSG LFTMKDVLNL DLI //