AC MF_00102; DC Protein; auto TR HAMAP; MF_00102; -; 1; level=0 XX Names: DapB XX ID DAPB DE RecName: Full=4-hydroxy-tetrahydrodipicolinate reductase; DE Short=HTPA reductase; DE EC=1.17.1.8; GN Name=dapB; XX CC -!- FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate CC (HTPA) to tetrahydrodipicolinate. 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 -!- 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 -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the DapB family. 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. XX DR Pfam; PF05173; DapB_C; 1; trigger=no DR Pfam; PF01113; DapB_N; 1; trigger=no DR NCBIfam; TIGR00036; DapB; 1; trigger=no DR PROSITE; PS01298; DAPB; 1; trigger=no XX KW Cytoplasm KW Amino-acid biosynthesis KW Diaminopimelate biosynthesis KW Lysine biosynthesis KW Oxidoreductase KW NAD KW NADP XX GO GO:0016726; F:oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor GO GO:0050661; F:NADP binding GO GO:0051287; F:NAD binding GO GO:0019877; P:diaminopimelate biosynthetic process GO GO:0009089; P:lysine biosynthetic process via diaminopimelate GO GO:0005737; C:cytoplasm XX FT From: DAPB_ECOLI (P04036) FT BINDING 12..17 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: G-x-x-G-x-x FT BINDING 102..104 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: [GAC]-x-[TS] FT BINDING 126..129 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Optional; Condition: [ASTGCV]-x-x-[FYMTVL] FT BINDING 169..170 FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate" FT /ligand_id="ChEBI:CHEBI:16845" FT Condition: [GA]-[TS] FT ACT_SITE 159 FT /note="Proton donor/acceptor" FT Condition: H FT ACT_SITE 163 FT /note="Proton donor" FT Condition: K FT BINDING 38 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Optional; Condition: [ED] FT BINDING 39 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT Optional; Condition: [RK] FT BINDING 160 FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate" FT /ligand_id="ChEBI:CHEBI:16845" FT Optional; Condition: [HR] XX Size: 216-283; Related: None; Template: P04036; P9WP23; Q9X1K8; Scope: Bacteria Archaea Fusion: Nter: None Cter: None Duplicate: in RHILO Plasmid: in RHIME Comments: MYCBO strain BCG seems to originate from a different bacterial species; its sequence is too divergent to that of MYCBO strain AF2122/97 and MYCTU XX # Revision 1.41 2023/06/01 //