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HAMAP rule MF_00102

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General rule information [?]

Accession MF_00102
Dates 1-JUN-2001 (Created)
1-JUN-2023 (Last updated, Version 41)
Name DapB
Templates P04036 (DAPB_ECOLI); P9WP23 (DAPB_MYCTU); Q9X1K8 (DAPB_THEMA): [Recover all]

Propagated annotation [?]

Identifier, protein and gene names [?]

Protein name
RecName: Full=4-hydroxy-tetrahydrodipicolinate reductase;
Short=HTPA reductase;
Gene name

Comments [?]

Function Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic activity RHEA:35323: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH
RHEA:35331: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH
Pathway Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.
Subunit Homotetramer.
Subcellular location Cytoplasm.
Similarity Belongs to the DapB family.
Caution Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction.

Keywords [?]

Gene Ontology [?]

GO:0016726; Molecular function: oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor.
GO:0050661; Molecular function: NADP binding.
GO:0051287; Molecular function: NAD binding.
GO:0019877; Biological process: diaminopimelate biosynthetic process.
GO:0009089; Biological process: lysine biosynthetic process via diaminopimelate.
GO:0005737; Cellular component: cytoplasm.

Cross-references [?]

Pfam PF05173; DapB_C; 1;
PF01113; DapB_N; 1;
NCBIfam TIGR00036; DapB; 1;

Features [?]

From: DAPB_ECOLI (P04036)
Key     From     To       Description   Tag   Condition   FTGroup
BINDING     12     17       /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540     G-x-x-G-x-x  
BINDING     102     104       /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540     [GAC]-x-[TS]  
BINDING (Optional)     126     129       /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540     [ASTGCV]-x-x-[FYMTVL]  
BINDING     169     170       /ligand="(S)-2,3,4,5-tetrahydrodipicolinate" /ligand_id="ChEBI:CHEBI:16845     [GA]-[TS]  
ACT_SITE     159     159       Proton donor/acceptor     H  
ACT_SITE     163     163       Proton donor     K  
BINDING (Optional)     38     38       /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540     [ED]  
BINDING (Optional)     39     39       /ligand="NADP(+)" /ligand_id="ChEBI:CHEBI:58349     [RK]  
BINDING (Optional)     160     160       /ligand="(S)-2,3,4,5-tetrahydrodipicolinate" /ligand_id="ChEBI:CHEBI:16845     [HR]  

Additional information [?]

Size range 216-283 amino acids
Related rules None
Fusion None
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