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Entry: A0A1G7IQ70_9EURY
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Original site: A0A1G7IQ70_9EURY 
ID   A0A1G7IQ70_9EURY        Unreviewed;       351 AA.
AC   A0A1G7IQ70;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Glycerol-1-phosphate dehydrogenase [NAD(P)+] {ECO:0000256|HAMAP-Rule:MF_00497};
DE            Short=G1P dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00497};
DE            Short=G1PDH {ECO:0000256|HAMAP-Rule:MF_00497};
DE            EC=1.1.1.261 {ECO:0000256|HAMAP-Rule:MF_00497};
DE   AltName: Full=Enantiomeric glycerophosphate synthase {ECO:0000256|HAMAP-Rule:MF_00497};
DE   AltName: Full=sn-glycerol-1-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00497};
GN   Name=egsA {ECO:0000256|HAMAP-Rule:MF_00497};
GN   ORFNames=SAMN05216218_10437 {ECO:0000313|EMBL:SDF14706.1};
OS   Halorientalis regularis.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Halorientalis.
OX   NCBI_TaxID=660518 {ECO:0000313|EMBL:SDF14706.1, ECO:0000313|Proteomes:UP000199076};
RN   [1] {ECO:0000313|EMBL:SDF14706.1, ECO:0000313|Proteomes:UP000199076}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBRC-M 10760 {ECO:0000313|EMBL:SDF14706.1,
RC   ECO:0000313|Proteomes:UP000199076};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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       {ECO:0000256|HAMAP-Rule:MF_00497}.
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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00497};
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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00497};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00497,
CC         ECO:0000256|PIRSR:PIRSR000112-1};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00497,
CC       ECO:0000256|PIRSR:PIRSR000112-1};
CC   -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC       {ECO:0000256|HAMAP-Rule:MF_00497}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00497}.
CC   -!- SIMILARITY: Belongs to the glycerol-1-phosphate dehydrogenase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00497}.
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DR   EMBL; FNBK01000004; SDF14706.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7IQ70; -.
DR   STRING; 660518.SAMN05216218_10437; -.
DR   OrthoDB; 8656at2157; -.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000199076; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0106357; F:glycerol-1-phosphate dehydrogenase [NAD+] activity; IEA:RHEA.
DR   GO; GO:0106358; F:glycerol-1-phosphate dehydrogenase [NADP+] activity; IEA:RHEA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd08173; Gro1PDH; 1.
DR   Gene3D; 3.40.50.1970; -; 1.
DR   Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR   HAMAP; MF_00497_A; G1P_dehydrogenase_A; 1.
DR   InterPro; IPR023002; G1P_dehydrogenase_arc.
DR   InterPro; IPR032837; G1PDH.
DR   InterPro; IPR016205; Glycerol_DH.
DR   PANTHER; PTHR43616; GLYCEROL DEHYDROGENASE; 1.
DR   PANTHER; PTHR43616:SF5; GLYCEROL DEHYDROGENASE 1; 1.
DR   Pfam; PF13685; Fe-ADH_2; 1.
DR   PIRSF; PIRSF000112; Glycerol_dehydrogenase; 1.
DR   SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00497};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW   Rule:MF_00497};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW   Rule:MF_00497};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00497};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00497};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00497};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00497};
KW   Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209,
KW   ECO:0000256|HAMAP-Rule:MF_00497};
KW   Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264, ECO:0000256|HAMAP-
KW   Rule:MF_00497};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00497}.
FT   BINDING         98..102
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00497,
FT                   ECO:0000256|PIRSR:PIRSR000112-3"
FT   BINDING         120..123
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00497,
FT                   ECO:0000256|PIRSR:PIRSR000112-3"
FT   BINDING         125
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-2"
FT   BINDING         125
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00497"
FT   BINDING         129
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00497,
FT                   ECO:0000256|PIRSR:PIRSR000112-3"
FT   BINDING         172
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00497"
FT   BINDING         172
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT   BINDING         172
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00497"
FT   BINDING         252
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00497"
FT   BINDING         252
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT   BINDING         256
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00497"
FT   BINDING         268
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00497"
FT   BINDING         268
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
SQ   SEQUENCE   351 AA;  36927 MW;  6B0E24EA5624DC51 CRC64;
     MFDKSTWIRL PRNVVVGHGV LDETVDAVAE LHLTGRPLVV TSPTPREVAG DRVVEAFGAE
     GTEPALTTVQ EASFAEVERV IETARAEEIG FLIGVGGGKV IDITKMAADE LGKGFVSVPT
     AASHDGIVSG RGSVPEGDTR HSVAAEPPLA VVADTEILAE APWRLTTAGC ADIISNYTAV
     KDWQLAHRLK NVEYSEYAGA LSQMTAEMLV ENAGSVKKGL EESAWVVVKA LVSSGVAMSI
     AGSSRPASGA EHLFSHQLDR LVPGAALHGH QVGVGSIITE YLHSGETEWR KIRDALAGIG
     APTTAEELGI DDETVIESLT TAHRIRDRYT ILGDGVSEAA AREAARATGV I
//
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