HAMAP rule MF_00279
General rule information
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| Accession | MF_00279 |
| Dates | 1-JUN-2001 (Created)
2-SEP-2024 (Last updated, Version 32) |
| Name | PdxJ |
| Scope(s) |
Bacteria |
| Template(s) | P0A794 (PDXJ_ECOLI); [ Recover all ] |
| Triggered by |
HAMAP; MF_00279 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | PDXJ |
| Protein name | RecName: Full=Pyridoxine 5'-phosphate synthase; Short=PNP synthase; EC=2.6.99.2; |
| Gene name | Name=pdxJ; |
Comments
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| FUNCTION | Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino- 2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate. |
| CATALYTIC ACTIVITY | Reaction=3-amino-2-oxopropyl phosphate + 1-deoxy-D-xylulose 5-phosphate = pyridoxine 5'-phosphate + phosphate + 2 H2O + H(+); Xref=Rhea:RHEA:15265, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57279, ChEBI:CHEBI:57792, ChEBI:CHEBI:58589; EC=2.6.99.2; |
| PATHWAY | Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 5/5. |
| SUBUNIT | Homooctamer; tetramer of dimers. |
| SUBCELLULAR LOCATION | Cytoplasm. |
| SIMILARITY | Belongs to the PNP synthase family. |
Keywords
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Gene Ontology
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| GO:0016769; Molecular function:transferase activity, transferring nitrogenous groups |
| GO:0008615; Biological process:pyridoxine biosynthetic process |
| GO:0005737; Cellular component:cytoplasm |
Cross-references
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Features
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| From: PDXJ_ECOLI (P0A794) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 11 | 12 | /ligand="1-deoxy-D-xylulose 5-phosphate" /ligand_id="ChEBI:CHEBI:57792" |
D-H | ||||||||
| BINDING | 215 | 216 | /ligand="3-amino-2-oxopropyl phosphate" /ligand_id="ChEBI:CHEBI:57279" |
G-[HQFY] | ||||||||
| ACT_SITE | 45 | 45 | /note="Proton acceptor" | H | ||||||||
| ACT_SITE | 72 | 72 | /note="Proton acceptor" | E | ||||||||
| ACT_SITE | 193 | 193 | /note="Proton donor" | H | ||||||||
| BINDING | 9 | 9 | /ligand="3-amino-2-oxopropyl phosphate" /ligand_id="ChEBI:CHEBI:57279" |
N | ||||||||
| BINDING | 20 | 20 | /ligand="3-amino-2-oxopropyl phosphate" /ligand_id="ChEBI:CHEBI:57279" |
R | ||||||||
| BINDING | 47 | 47 | /ligand="1-deoxy-D-xylulose 5-phosphate" /ligand_id="ChEBI:CHEBI:57792" |
R | ||||||||
| BINDING | 52 | 52 | /ligand="1-deoxy-D-xylulose 5-phosphate" /ligand_id="ChEBI:CHEBI:57792" |
H | ||||||||
| BINDING | 102 | 102 | /ligand="1-deoxy-D-xylulose 5-phosphate" /ligand_id="ChEBI:CHEBI:57792" |
T | ||||||||
| BINDING | 194 | 194 | /ligand="3-amino-2-oxopropyl phosphate" /ligand_id="ChEBI:CHEBI:57279" |
[GASD] | ||||||||
| SITE | 153 | 153 | /note="Transition state stabilizer" | E | ||||||||
Additional information
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| Size range | 232-267 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |