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HAMAP rule MF_00536
General rule information
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| Accession | MF_00536 |
| Dates | 30-JAN-2002 (Created)
1-JUN-2023 (Last updated, Version 36) |
| Name | PdxA |
| Scope(s) |
Bacteria |
| Template(s) | P19624 (PDXA_ECOLI); P58717 (PDXA_SALTY); Q9I5U4 (PDXA_PSEAE); [ Recover all ] |
| Triggered by |
HAMAP; MF_00536 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | PDXA |
| Protein name | RecName: Full=4-hydroxythreonine-4-phosphate dehydrogenase; EC=1.1.1.262; AltName: Full=4-(phosphohydroxy)-L-threonine dehydrogenase; |
| Gene name | Name=pdxA; |
Comments
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| FUNCTION | Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L- threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP). |
| CATALYTIC ACTIVITY | Reaction=4-(phosphooxy)-L-threonine + NAD(+) = 3-amino-2-oxopropyl phosphate + CO2 + NADH; Xref=Rhea:RHEA:32275, ChEBI:CHEBI:16526, ChEBI:CHEBI:57279, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58452; EC=1.1.1.262; |
| case <OC:Pseudomonadota> | |
| COFACTOR | Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Note=Binds 1 divalent metal cation per subunit. Can use ions such as Zn(2+), Mg(2+) or Co(2+).; |
| else | |
| COFACTOR | Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Note=Binds 1 divalent metal cation per subunit.; |
| end case | |
| PATHWAY | Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5. |
| SUBUNIT | Homodimer. |
| SUBCELLULAR LOCATION | Cytoplasm. |
| MISCELLANEOUS | The active site is located at the dimer interface. |
| SIMILARITY | Belongs to the PdxA family. |
Keywords
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| Cytoplasm | |
| Pyridoxine biosynthesis | |
| Oxidoreductase | |
| NAD | |
| NADP | |
| Metal-binding | |
| case <OC:Pseudomonadota> | |
| Cobalt | |
| Magnesium | |
| Zinc | |
| end case | |
Gene Ontology
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| GO:0050570; Molecular function:4-hydroxythreonine-4-phosphate dehydrogenase activity | |
| GO:0046872; Molecular function:metal ion binding | |
| GO:0042823; Biological process:pyridoxal phosphate biosynthetic process | |
| GO:0008615; Biological process:pyridoxine biosynthetic process | |
| case <OCellular component:Pseudomonadota> | |
| GO:0050897; Molecular function:cobalt ion binding | |
| GO:0008270; Molecular function:zinc ion binding | |
| GO:0000287; Molecular function:magnesium ion binding | |
| end case | |
| GO:0005737; Cellular component:cytoplasm | |
Cross-references
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Features
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| From: PDXA_ECOLI (P19624) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 166 | 166 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_note="ligand shared between dimeric partners" |
H | ||||||||
| BINDING | 211 | 211 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_note="ligand shared between dimeric partners" |
H | ||||||||
| BINDING | 266 | 266 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_note="ligand shared between dimeric partners" |
H | ||||||||
| BINDING | 136 | 136 | /ligand="substrate" | H | ||||||||
| BINDING | 137 | 137 | /ligand="substrate" | [TS] | ||||||||
| BINDING | 274 | 274 | /ligand="substrate" | K | ||||||||
| BINDING | 283 | 283 | /ligand="substrate" | N | ||||||||
| BINDING | 292 | 292 | /ligand="substrate" | R | ||||||||
Additional information
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| Size range | 307-364 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |
| Comments | MF_00536 signature has been revised (March 2017) to avoid wrong annotation of DUF1537-linked PdxA2, which are paralogs of PdxA and are involved in carbon source metabolism rather than PLP biosynthesis. |