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Annotation rule MF_02086 |
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 |
Identifier |
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Protein name |
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Gene name |
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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. |
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 |
Size range | 296-375 amino acids |
Related rules | None |
Fusion | None |