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| Annotation rule MF_02086 |
General rule information
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| Accession | MF_02086 |
| Dates | 14-MAR-2017 (Created) 20-NOV-2019 (Last updated, Version 4) |
| Name | PdxA_Epsilonprot |
| Scope | Bacteria; Epsilonproteobacteria |
| Templates | Q9PN58 (PDXA_CAMJE); P19624 (PDXA_ECOLI): [Recover all] |
| Triggered by |
Propagated annotation
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Identifier, protein and gene names
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| Identifier |
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| Protein name |
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| Gene name |
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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 | RHEA:32275: 4-(phosphooxy)-L-threonine + NAD(+) = 3-amino-2-oxopropyl phosphate + CO2 + NADH
EC 1.1.1.262 |
| Cofactor | Zn(2+) Mg(2+) Co(2+) |
| 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.
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 | ||||||
| METAL | 177 | 177 | Divalent metal cation; shared with dimeric partner | H | ||||||||
| METAL | 216 | 216 | Divalent metal cation; shared with dimeric partner | H | ||||||||
| METAL | 301 | 301 | Divalent metal cation; shared with dimeric partner | H | ||||||||
| BINDING (Optional) | 148 | 148 | Substrate | H | ||||||||
| BINDING (Optional) | 149 | 149 | Substrate | T | ||||||||
| BINDING (Optional) | 309 | 309 | Substrate | K | ||||||||
| BINDING (Optional) | 318 | 318 | Substrate | N | ||||||||
| BINDING (Optional) | 327 | 327 | Substrate | R | ||||||||
Additional information
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| Size range | 296-375 amino acids |
| Related rules | None |
| Fusion | None |