AC   MF_00497;
DC   Protein; auto
c?   <OC:Bacteria>
TR   HAMAP; MF_00497_B; -; 1; level=0
c?   <OC:Archaea>
TR   HAMAP; MF_00497_A; -; 1; level=0
XX
Names: G1P_dehydrogenase
XX
ID   G1PDH
DE   RecName: Full=Glycerol-1-phosphate dehydrogenase [NAD(P)+];
DE            Short=G1P dehydrogenase;
DE            Short=G1PDH;
DE            EC=1.1.1.261;
DE   AltName: Full=Enantiomeric glycerophosphate synthase;
DE   AltName: Full=sn-glycerol-1-phosphate dehydrogenase;
GN   Name=egsA;
XX
case <OC:Archaea>
CC   -!- FUNCTION: Catalyzes the NAD(P)H-dependent reduction of
CC       dihydroxyacetonephosphate (DHAP or glycerone phosphate) to glycerol 1-
CC       phosphate (G1P). The G1P thus generated is used as the glycerophosphate
CC       backbone of phospholipids in the cellular membranes of Archaea.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + sn-glycerol 1-phosphate = dihydroxyacetone phosphate
CC         + H(+) + NADH; Xref=Rhea:RHEA:21412, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57642, ChEBI:CHEBI:57685,
CC         ChEBI:CHEBI:57945; EC=1.1.1.261;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + sn-glycerol 1-phosphate = dihydroxyacetone phosphate
CC         + H(+) + NADPH; Xref=Rhea:RHEA:21416, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57642, ChEBI:CHEBI:57685, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.1.1.261;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 1 zinc ion per subunit.;
CC   -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
end case
case <OC:Methanobacteria>
CC   -!- SUBUNIT: Homooctamer.
end case
case <OC:Thermoprotei>
CC   -!- SUBUNIT: Homodimer.
end case
case <OC:Bacillales>
CC   -!- FUNCTION: Catalyzes the NAD(P)H-dependent reduction of
CC       dihydroxyacetonephosphate (DHAP or glycerone phosphate) to glycerol 1-
CC       phosphate (G1P). The G1P thus generated is probably used for the
CC       synthesis of phosphoglycerolipids in Gram-positive bacterial species.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + sn-glycerol 1-phosphate = dihydroxyacetone phosphate
CC         + H(+) + NADH; Xref=Rhea:RHEA:21412, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57642, ChEBI:CHEBI:57685,
CC         ChEBI:CHEBI:57945; EC=1.1.1.261;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + sn-glycerol 1-phosphate = dihydroxyacetone phosphate
CC         + H(+) + NADPH; Xref=Rhea:RHEA:21416, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57642, ChEBI:CHEBI:57685, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.1.1.261;
CC   -!- COFACTOR:
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC       Note=Binds 1 nickel ion per subunit.;
CC   -!- SUBUNIT: Homodimer.
end case
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the glycerol-1-phosphate dehydrogenase family.
XX
DR   Pfam; PF01761; DHQ_synthase; 1; trigger=no
XX
KW   Cytoplasm
KW   Lipid biosynthesis
KW   Lipid metabolism
KW   Metal-binding
KW   NAD
KW   NADP
case <OC:Bacillales>
KW   Nickel
end case
KW   Oxidoreductase
KW   Phospholipid biosynthesis
KW   Phospholipid metabolism
case <OC:Archaea>
KW   Zinc
end case
XX
GO   GO:0050492; F:glycerol-1-phosphate dehydrogenase [NAD(P)+] activity
GO   GO:0008654; P:phospholipid biosynthetic process
GO   GO:0005737; C:cytoplasm
XX
FT   From: G1PDH_METTH (P72010)
case <OC:Archaea>
FT   BINDING         94..98
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: G-x-x-x-D
FT   BINDING         116..119
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: T-x-x-S
FT   BINDING         168
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT   Condition: [DE]
FT   BINDING         248
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT   Condition: H
FT   BINDING         264
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT   Condition: H
FT   BINDING         121
FT                   /ligand="substrate"
FT   Condition: D
FT   BINDING         125
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: S
FT   BINDING         168
FT                   /ligand="substrate"
FT   Condition: [DE]
FT   BINDING         252
FT                   /ligand="substrate"
FT   Condition: H
end case
FT   From: G1PDH_BACSU (P94527)
case <OC:Bacillales>
FT   BINDING         116..120
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: G-x-x-x-D
FT   BINDING         138..141
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: T-x-x-S
FT   BINDING         190
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_note="catalytic"
FT   Condition: D
FT   BINDING         270
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_note="catalytic"
FT   Condition: H
FT   BINDING         290
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_note="catalytic"
FT   Condition: H
FT   BINDING         54
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: D
FT   BINDING         143
FT                   /ligand="substrate"
FT   Condition: D
FT   BINDING         147
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: S
FT   BINDING         190
FT                   /ligand="substrate"
FT   Condition: D
FT   BINDING         274
FT                   /ligand="substrate"
FT   Condition: H
end case
XX
case <OC:Bacteria>
Size: 394-404;
end case
case <OC:Archaea>
Size: 314-360;
end case
Related: None;
Template: P72010; Q9YER2; P94527;
Scope:
 Bacteria; Bacillales
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.31 2022/11/19
//