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HAMAP rule MF_00497
General rule information
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| Accession | MF_00497 |
| Dates | 4-DEC-2001 (Created)
15-FEB-2024 (Last updated, Version 32) |
| Name | G1P_dehydrogenase |
| Scope(s) |
Bacteria Bacillales Archaea |
| Template(s) | P72010 (G1PDH_METTH); Q9YER2 (G1PDH_AERPE); P94527 (G1PDH_BACSU); [ Recover all ] |
| Triggered by |
case c? <OC:Bacteria>
HAMAP; MF_00497_B (Get profile general information and statistics) end case
case c? <OC:Archaea>
HAMAP; MF_00497_A (Get profile general information and statistics) end case
|
Propagated annotation
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Identifier, protein and gene names
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| Identifier | G1PDH |
| 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; |
| Gene name | Name=egsA; |
Comments
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| 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. |
| CATALYTIC ACTIVITY | Reaction=NAD(+) + sn-glycerol 1-phosphate = dihydroxyacetone phosphate + H(+) + NADH; Xref=Rhea:RHEA:21412, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57642, ChEBI:CHEBI:57685, ChEBI:CHEBI:57945; EC=1.1.1.261; |
| CATALYTIC ACTIVITY | Reaction=NADP(+) + sn-glycerol 1-phosphate = dihydroxyacetone phosphate + H(+) + NADPH; Xref=Rhea:RHEA:21416, ChEBI:CHEBI:15378, ChEBI:CHEBI:57642, ChEBI:CHEBI:57685, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.261; |
| COFACTOR | Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.; |
| PATHWAY | Membrane lipid metabolism; glycerophospholipid metabolism. |
| end case | |
| case <OC:Methanobacteria> | |
| SUBUNIT | Homooctamer. |
| end case | |
| case <OC:Thermoprotei> | |
| SUBUNIT | Homodimer. |
| 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. |
| CATALYTIC ACTIVITY | Reaction=NAD(+) + sn-glycerol 1-phosphate = dihydroxyacetone phosphate + H(+) + NADH; Xref=Rhea:RHEA:21412, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57642, ChEBI:CHEBI:57685, ChEBI:CHEBI:57945; EC=1.1.1.261; |
| CATALYTIC ACTIVITY | Reaction=NADP(+) + sn-glycerol 1-phosphate = dihydroxyacetone phosphate + H(+) + NADPH; Xref=Rhea:RHEA:21416, ChEBI:CHEBI:15378, ChEBI:CHEBI:57642, ChEBI:CHEBI:57685, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.261; |
| COFACTOR | Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Note=Binds 1 nickel ion per subunit.; |
| SUBUNIT | Homodimer. |
| end case | |
| SUBCELLULAR LOCATION | Cytoplasm. |
| SIMILARITY | Belongs to the glycerol-1-phosphate dehydrogenase family. |
Keywords
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| Cytoplasm | |
| Lipid biosynthesis | |
| Lipid metabolism | |
| Metal-binding | |
| NAD | |
| NADP | |
| case <OC:Bacillales> | |
| Nickel | |
| end case | |
| Oxidoreductase | |
| Phospholipid biosynthesis | |
| Phospholipid metabolism | |
| case <OC:Archaea> | |
| Zinc | |
| end case | |
Gene Ontology
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| GO:0050492; Molecular function:glycerol-1-phosphate dehydrogenase [NAD(P)+] activity |
| GO:0006650; Biological process:glycerophospholipid metabolic process |
| GO:0005737; Cellular component:cytoplasm |
Cross-references
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| Pfam | PF01761; DHQ_synthase; 1; |
Features
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| From: G1PDH_METTH (P72010) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| case <OC:Archaea> | ||||||||||||
| BINDING | 94 | 98 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
G-x-x-x-D | ||||||||
| BINDING | 116 | 119 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
T-x-x-S | ||||||||
| BINDING | 168 | 168 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_note="catalytic" |
[DE] | ||||||||
| BINDING | 248 | 248 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_note="catalytic" |
H | ||||||||
| BINDING | 264 | 264 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_note="catalytic" |
H | ||||||||
| BINDING | 121 | 121 | /ligand="substrate" | D | ||||||||
| BINDING | 125 | 125 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
S | ||||||||
| BINDING | 168 | 168 | /ligand="substrate" | [DE] | ||||||||
| BINDING | 252 | 252 | /ligand="substrate" | H | ||||||||
| end case | ||||||||||||
| From: G1PDH_BACSU (P94527) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| case <OC:Bacillales> | ||||||||||||
| BINDING | 116 | 120 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
G-x-x-x-D | ||||||||
| BINDING | 138 | 141 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
T-x-x-S | ||||||||
| BINDING | 190 | 190 | /ligand="Ni(2+)" /ligand_id="ChEBI:CHEBI:49786" /ligand_note="catalytic" |
D | ||||||||
| BINDING | 270 | 270 | /ligand="Ni(2+)" /ligand_id="ChEBI:CHEBI:49786" /ligand_note="catalytic" |
H | ||||||||
| BINDING | 290 | 290 | /ligand="Ni(2+)" /ligand_id="ChEBI:CHEBI:49786" /ligand_note="catalytic" |
H | ||||||||
| BINDING | 54 | 54 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
D | ||||||||
| BINDING | 143 | 143 | /ligand="substrate" | D | ||||||||
| BINDING | 147 | 147 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
S | ||||||||
| BINDING | 190 | 190 | /ligand="substrate" | D | ||||||||
| BINDING | 274 | 274 | /ligand="substrate" | H | ||||||||
| end case | ||||||||||||
Additional information
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| Size range | 314-360 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |