HAMAP rule MF_00102
General rule information
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| Accession | MF_00102 |
| Dates | 1-JUN-2001 (Created)
2-SEP-2024 (Last updated, Version 42) |
| Name | DapB |
| Scope(s) |
Bacteria Archaea |
| Template(s) | P04036 (DAPB_ECOLI); P9WP23 (DAPB_MYCTU); Q9X1K8 (DAPB_THEMA); [ Recover all ] |
| Triggered by |
HAMAP; MF_00102 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | DAPB |
| Protein name | RecName: Full=4-hydroxy-tetrahydrodipicolinate reductase; Short=HTPA reductase; EC=1.17.1.8; |
| Gene name | Name=dapB; |
Comments
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| FUNCTION | Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. |
| CATALYTIC ACTIVITY | Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + NAD(+) + H2O = (2S,4S)-4- hydroxy-2,3,4,5-tetrahydrodipicolinate + NADH + H(+); Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; |
| CATALYTIC ACTIVITY | Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + NADP(+) + H2O = (2S,4S)- 4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADPH + H(+); Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; |
| 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
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| Cytoplasm |
| Amino-acid biosynthesis |
| Diaminopimelate biosynthesis |
| Lysine biosynthesis |
| Oxidoreductase |
| NAD |
| NADP |
Gene Ontology
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| 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
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| Pfam | PF05173; DapB_C; 1; |
| Pfam | PF01113; DapB_N; 1; |
| NCBIfam | TIGR00036; DapB; 1; |
| PROSITE | PS01298; DAPB; 1; |
Features
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| 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 | 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 | /note="Proton donor/acceptor" | H | ||||||||
| ACT_SITE | 163 | 163 | /note="Proton donor" | K | ||||||||
| BINDING | 38 | 38 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
[ED] | ||||||||
| BINDING | 39 | 39 | /ligand="NADP(+)" /ligand_id="ChEBI:CHEBI:58349" |
[RK] | ||||||||
| BINDING | 160 | 160 | /ligand="(S)-2,3,4,5-tetrahydrodipicolinate" /ligand_id="ChEBI:CHEBI:16845" |
[HR] | ||||||||
Additional information
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| Size range | 216-283 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: 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 |