HAMAP rule MF_02086
General rule information
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| Accession | MF_02086 |
| Dates | 14-MAR-2017 (Created)
1-JUN-2023 (Last updated, Version 7) |
| Name | PdxA_Epsilonprot |
| Scope(s) |
Bacteria Epsilonproteobacteria |
| Template(s) | Q9PN58 (PDXA_CAMJE); P19624 (PDXA_ECOLI); [ Recover all ] |
| Triggered by |
HAMAP; MF_02086 (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; |
| COFACTOR | Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Name=Co(2+); Xref=ChEBI:CHEBI:48828; |
| 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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Gene Ontology
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| GO:0050570; Molecular function:4-hydroxythreonine-4-phosphate dehydrogenase activity |
| GO:0046872; Molecular function:metal ion binding |
| GO:0050897; Molecular function:cobalt ion binding |
| GO:0008270; Molecular function:zinc ion binding |
| GO:0000287; Molecular function:magnesium ion binding |
| GO:0042823; Biological process:pyridoxal phosphate biosynthetic process |
| GO:0008615; Biological process:pyridoxine biosynthetic process |
| GO:0005737; Cellular component:cytoplasm |
Cross-references
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Features
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| From: PDXA_CAMJE (Q9PN58) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 177 | 177 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_note="ligand shared between dimeric partners" |
H | ||||||||
| BINDING | 216 | 216 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_note="ligand shared between dimeric partners" |
H | ||||||||
| BINDING | 301 | 301 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_note="ligand shared between dimeric partners" |
H | ||||||||
| BINDING | 148 | 148 | /ligand="substrate" | H | ||||||||
| BINDING | 149 | 149 | /ligand="substrate" | T | ||||||||
| BINDING | 309 | 309 | /ligand="substrate" | K | ||||||||
| BINDING | 318 | 318 | /ligand="substrate" | N | ||||||||
| BINDING | 327 | 327 | /ligand="substrate" | R | ||||||||
Additional information
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| Size range | 296-375 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |