HAMAP rule MF_00418
General rule information
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| Accession | MF_00418 |
| Dates | 19-JUN-2001 (Created)
1-JUN-2023 (Last updated, Version 46) |
| Name | DapA |
| Scope(s) |
Bacteria Archaea |
| Template(s) | P0A6L2 (DAPA_ECOLI); P9WP25 (DAPA_MYCTU); Q9X1K9 (DAPA_THEMA); Q57695 (DAPA_METJA); Q6GH13 (DAPA_STAAR); Q5HG25 (DAPA_STAAC); Q9JZR4 (DAPA_NEIMB); Q9I4W3 (DAPA_PSEAE); Q07607 (DAPA_RHIML); Q8UGL3 (DAPA_AGRFC); [ Recover all ] |
| Triggered by |
HAMAP; MF_00418 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | DAPA |
| Protein name | RecName: Full=4-hydroxy-tetrahydrodipicolinate synthase; Short=HTPA synthase; EC=4.3.3.7; |
| Gene name | Name=dapA; |
Comments
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| FUNCTION | Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). |
| CATALYTIC ACTIVITY | Reaction=L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy- 2,3,4,5-tetrahydrodipicolinate + H(+) + H2O; Xref=Rhea:RHEA:34171, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:67139, ChEBI:CHEBI:537519; EC=4.3.3.7; |
| PATHWAY | Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4. |
| case (<OC:Bacteria> or <OC:Archaea>) and not (<OC:Staphylococcus> or <OC:Pseudomonas>) | |
| SUBUNIT | Homotetramer; dimer of dimers. |
| else | |
| SUBUNIT | Homodimer. |
| end case | |
| SUBCELLULAR LOCATION | Cytoplasm. |
| SIMILARITY | Belongs to the DapA family. |
| CAUTION | Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)- dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB. |
Keywords
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| Cytoplasm |
| Amino-acid biosynthesis |
| Diaminopimelate biosynthesis |
| Lyase |
| Lysine biosynthesis |
| Schiff base |
Gene Ontology
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| GO:0008840; Molecular function:4-hydroxy-tetrahydrodipicolinate synthase activity |
| GO:0019877; Biological process:diaminopimelate biosynthetic process |
| GO:0009085; Biological process:lysine biosynthetic process |
| GO:0005737; Cellular component:cytoplasm |
Cross-references
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| Pfam | PF00701; DHDPS; 1; |
| PRINTS | PR00146; DHPICSNTHASE; 1; |
| NCBIfam | TIGR00674; DapA; 1; |
| PROSITE | PS00665; DHDPS_1; 1; |
| PROSITE | PS00666; DHDPS_2; 1; |
Features
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| From: DAPA_ECOLI (P0A6L2) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| ACT_SITE | 133 | 133 | /note="Proton donor/acceptor" | Y | ||||||||
| ACT_SITE | 161 | 161 | /note="Schiff-base intermediate with substrate" | K | ||||||||
| BINDING | 45 | 45 | /ligand="pyruvate" /ligand_id="ChEBI:CHEBI:15361" |
[TS] | ||||||||
| BINDING | 203 | 203 | /ligand="pyruvate" /ligand_id="ChEBI:CHEBI:15361" |
[IVAT] | ||||||||
| SITE | 44 | 44 | /note="Part of a proton relay during catalysis" | [TS] | ||||||||
| SITE | 107 | 107 | /note="Part of a proton relay during catalysis" | Y | ||||||||
Additional information
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| Size range | 283-311 amino acids |
| Related rules |
MF_01237 MF_00694 |
| Fusion | Nter: None Cter: None |