ID B0BWB9_RICRO Unreviewed; 285 AA. AC B0BWB9; DT 26-FEB-2008, integrated into UniProtKB/TrEMBL. DT 26-FEB-2008, sequence version 1. DT 27-MAR-2024, entry version 105. 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 OrderedLocusNames=RrIowa_0233 {ECO:0000313|EMBL:ABY72145.1}; OS Rickettsia rickettsii (strain Iowa). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=452659 {ECO:0000313|EMBL:ABY72145.1, ECO:0000313|Proteomes:UP000000796}; RN [1] {ECO:0000313|EMBL:ABY72145.1, ECO:0000313|Proteomes:UP000000796} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Iowa {ECO:0000313|EMBL:ABY72145.1, RC ECO:0000313|Proteomes:UP000000796}; RX PubMed=18025092; DOI=10.1128/IAI.00952-07; RA Ellison D.W., Clark T.R., Sturdevant D.E., Virtaneva K., Porcella S.F., RA Hackstadt T.; RT "Genomic comparison of virulent Rickettsia rickettsii Sheila Smith and RT avirulent Rickettsia rickettsii Iowa."; RL Infect. Immun. 76:542-550(2008). 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: Lacks conserved residue(s) required for the propagation of CC feature annotation. {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; CP000766; ABY72145.1; -; Genomic_DNA. DR AlphaFoldDB; B0BWB9; -. DR KEGG; rrj:RrIowa_0233; -. DR eggNOG; COG0289; Bacteria. DR HOGENOM; CLU_047479_2_2_5; -. DR UniPathway; UPA00034; UER00018. DR Proteomes; UP000000796; 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:ABY72145.1}. FT DOMAIN 49..151 FT /note="Dihydrodipicolinate reductase N-terminal" FT /evidence="ECO:0000259|Pfam:PF01113" FT DOMAIN 154..282 FT /note="Dihydrodipicolinate reductase C-terminal" FT /evidence="ECO:0000259|Pfam:PF05173" FT ACT_SITE 180 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102" FT ACT_SITE 184 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102" FT BINDING 54..59 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102" FT BINDING 124..126 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102" FT BINDING 148..151 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102" FT BINDING 181 FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate" FT /ligand_id="ChEBI:CHEBI:16845" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102" FT BINDING 190..191 FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate" FT /ligand_id="ChEBI:CHEBI:16845" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102" SQ SEQUENCE 285 AA; 31820 MW; 549827E6CE4F0EA0 CRC64; MASYNKICGS NYIKYTLRSK DFRRLALVQI KLRLLTVHLL GVYIANMLNI GLSGSTGKMG ETILERIDKF KDCKIAAKFN STNNLDDLDN FCKNSDVIID FSTPEILEKL INYALKHNTK LVIGTTGLQP QHFKLLEKAA QTLPVLYSAN MSIGANLLSY LAKEVTKILD DYDVEILETH HRNKKDSPSG TAVMLAETIA SKKGLNITFN RGNRLRSEKE IGISSLRGGN VHGIHEISFL GDDEIITLKH EALNKNSFSI GAIKAAIWLQ DKPSALYSMQ DIYKI //