| Accession |
MF_00497 |
| Dates |
4-DEC-2001 (Created) 17-AUG-2010 (Last updated, Version 23) |
case <OC:Bacteria>
end case
case <OC:Archaea>
end case
| Protein name |
| RecName: |
Full=Glycerol-1-phosphate dehydrogenase [NAD(P)+]; Short=G1P dehydrogenase; Short=G1PDH; EC=1.1.1.261; |
| AltName: |
Full=Enantiomeric glycerophosphate synthase; |
| AltName: |
Full=sn-glycerol-1-phosphate dehydrogenase; |
|
case <OC:Archaea>
FUNCTION: Catalyzes the NAD(P)H-dependent reduction of dihydroxyacetonephosphate (DHAP or glycerone phosphate) to glycerol-1-phosphate (G1P). The G1P thus generated is used as the glycerophosphate backbone of phospholipids in the cellular membranes of Archaea (By similarity).
CATALYTIC ACTIVITY: sn-glycerol-1-phosphate + NAD(P)(+) = glycerone phosphate + NAD(P)H.
COFACTOR: Binds 1 zinc ion per subunit (By similarity).
PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
end case
case <OC:Methanobacteria>
SUBUNIT: Homooctamer (By similarity).
end case
case <OC:Thermoprotei>
SUBUNIT: Homodimer (By similarity).
end case
case <OC:Bacillales>
FUNCTION: Catalyzes the NAD(P)H-dependent reduction of dihydroxyacetonephosphate (DHAP or glycerone phosphate) to glycerol-1-phosphate (G1P). The G1P thus generated is probably used for the synthesis of phosphoglycerolipids in Gram-positive bacterial species (By similarity).
CATALYTIC ACTIVITY: sn-glycerol-1-phosphate + NAD(P)(+) = glycerone phosphate + NAD(P)H.
COFACTOR: Binds 1 nickel ion per subunit (By similarity).
SUBUNIT: Homodimer (By similarity).
end case
SUBCELLULAR LOCATION: Cytoplasm (Potential).
SIMILARITY: Belongs to the glycerol-1-phosphate dehydrogenase family.
case <OC:Bacillales>
end case
case <OC:Archaea>
end case
GO:0050492; Molecular function: glycerol-1-phosphate dehydrogenase [NAD(P)+] activity.
GO:0008654; Biological process: phospholipid biosynthetic process.
GO:0005737; Cellular component: cytoplasm.
case <OC:Archaea>
| From: G1PDH_METTH (P72010) |
| Key |
|
From |
|
To |
|
Description |
|
Condition |
|
FTGroup |
| NP_BIND |
|
94 |
|
98 |
|
NAD (By similarity) |
|
G-x-x-x-D |
|
|
| NP_BIND |
|
116 |
|
119 |
|
NAD (By similarity) |
|
T-x-x-S |
|
|
| METAL |
|
168 |
|
168 |
|
Zinc; catalytic (By similarity) |
|
[DE] |
|
|
| METAL |
|
248 |
|
248 |
|
Zinc; catalytic (By similarity) |
|
H |
|
|
| METAL |
|
264 |
|
264 |
|
Zinc; catalytic (By similarity) |
|
H |
|
|
| BINDING |
|
121 |
|
121 |
|
Substrate (By similarity) |
|
D |
|
|
| BINDING |
|
125 |
|
125 |
|
NAD (By similarity) |
|
S |
|
|
| BINDING |
|
168 |
|
168 |
|
Substrate (By similarity) |
|
[DE] |
|
|
| BINDING |
|
252 |
|
252 |
|
Substrate (By similarity) |
|
H |
|
|
end case
case <OC:Bacillales>
| From: G1PDH_BACSU (P94527) |
| Key |
|
From |
|
To |
|
Description |
|
Condition |
|
FTGroup |
| NP_BIND |
|
116 |
|
120 |
|
NAD (By similarity) |
|
G-x-x-x-D |
|
|
| NP_BIND |
|
138 |
|
141 |
|
NAD (By similarity) |
|
T-x-x-S |
|
|
| METAL |
|
190 |
|
190 |
|
Nickel; catalytic (By similarity) |
|
D |
|
|
| METAL |
|
270 |
|
270 |
|
Nickel; catalytic (By similarity) |
|
H |
|
|
| METAL |
|
290 |
|
290 |
|
Nickel; catalytic (By similarity) |
|
H |
|
|
| BINDING |
|
54 |
|
54 |
|
NAD (By similarity) |
|
D |
|
|
| BINDING |
|
143 |
|
143 |
|
Substrate (By similarity) |
|
D |
|
|
| BINDING |
|
147 |
|
147 |
|
NAD (By similarity) |
|
S |
|
|
| BINDING |
|
190 |
|
190 |
|
Substrate (By similarity) |
|
D |
|
|
| BINDING |
|
274 |
|
274 |
|
Substrate (By similarity) |
|
H |
|
|
end case
case <OC:Bacteria>
| Size range: |
394-404 amino acids |
end case
case <OC:Archaea>
| Size range: |
314-360 amino acids |
end case
| Related UniRules: |
None |
| Template: |
P72010 (G1PDH_METTH); Q9YER2 (G1PDH_AERPE); P94527 (G1PDH_BACSU): [Recover all] |
| Scope: |
Bacteria; Bacillales
Archaea |
| Fusion: |
Nter: None; Cter: None |
| Duplicate: |
None |
| Plasmid encoded: |
None |
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