| Accession |
MF_00536 |
| Dates |
30-JAN-2002 (Created) 25-NOV-2009 (Last updated, Version 23) |
| Protein name |
| RecName: |
Full=4-hydroxythreonine-4-phosphate dehydrogenase; EC=1.1.1.262; |
| AltName: |
Full=4-(phosphohydroxy)-L-threonine dehydrogenase; |
|
FUNCTION: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphohydroxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphohydroxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP) (By similarity).
CATALYTIC ACTIVITY: 4-(phosphonooxy)-L-threonine + NAD(+) = (2S)-2-amino-3-oxo-4-phosphonooxybutanoate + NADH.
case <OC:Proteobacteria>
COFACTOR: Binds 1 divalent metal cation per subunit. Can use ions such as zinc, magnesium or cobalt (By similarity).
else
COFACTOR: Binds 1 divalent metal cation per subunit (By similarity).
end case
PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5.
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
MISCELLANEOUS: The active site is located at the dimer interface (By similarity).
SIMILARITY: Belongs to the pdxA family.
case <OC:Proteobacteria>
end case
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 <OC:Proteobacteria>
GO:0050897; Molecular function: cobalt ion binding.
GO:0008270; Molecular function: zinc ion binding.
GO:0000287; Molecular function: magnesium ion binding.
end case
| From: PDXA_ECOLI (P19624) |
| Key |
|
From |
|
To |
|
Description |
|
Condition |
|
FTGroup |
| METAL |
|
166 |
|
166 |
|
Divalent metal cation; shared with dimeric partner (By similarity) |
|
H |
|
|
| METAL |
|
211 |
|
211 |
|
Divalent metal cation; shared with dimeric partner (By similarity) |
|
H |
|
|
| METAL |
|
266 |
|
266 |
|
Divalent metal cation; shared with dimeric partner (By similarity) |
|
H |
|
|
| BINDING (Optional) |
|
136 |
|
136 |
|
Substrate (By similarity) |
|
H |
|
|
| BINDING (Optional) |
|
137 |
|
137 |
|
Substrate (By similarity) |
|
[TS] |
|
|
| BINDING |
|
274 |
|
274 |
|
Substrate (By similarity) |
|
K |
|
|
| BINDING (Optional) |
|
283 |
|
283 |
|
Substrate (By similarity) |
|
N |
|
|
| BINDING (Optional) |
|
292 |
|
292 |
|
Substrate (By similarity) |
|
R |
|
|
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