ID A0A1Q7LLG5_9CREN Unreviewed; 354 AA.
AC A0A1Q7LLG5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=AUJ07_11775 {ECO:0000313|EMBL:OLD01233.1};
OS Crenarchaeota archaeon 13_1_40CM_3_53_5.
OC Archaea; Thermoproteota.
OX NCBI_TaxID=1805098 {ECO:0000313|EMBL:OLD01233.1, ECO:0000313|Proteomes:UP000186658};
RN [1] {ECO:0000313|EMBL:OLD01233.1, ECO:0000313|Proteomes:UP000186658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OLD01233.1}.
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DR EMBL; MNGL01000082; OLD01233.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7LLG5; -.
DR STRING; 1805098.AUJ07_11775; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000186658; 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 100..104
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 122..125
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 127
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-2"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00497"
FT BINDING 131
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 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00497"
FT BINDING 174
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00497"
FT BINDING 254
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00497"
FT BINDING 254
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT BINDING 258
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00497"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00497"
FT BINDING 270
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
SQ SEQUENCE 354 AA; 37426 MW; 79BC6834D7BD6192 CRC64;
MDSDESQHYT QLPREVIVGK DVISHVGDVC HRLGFRGNAL VVSGPITYPL AGERVAKSIA
KAGLRVDHVI VKEASESILE EVITKVRQSE ANLVLGVGGG KDIDLAKLSS ARAAVQFMSI
PTAASHDGIA SPYASIKGSS KPYSIRGQAP IAILADIGIL AQSPYQLLAA GCGDIVAKYT
AVKDWQLAHK LKNEYYGDYA AELALMSAEL VSKNSRDITQ RKLEGVRTVV EALISCGVAM
SIAGSSRPCS GAEHLFSHAL DIVAGETSLH GERTGVGAIL CAYLQGSNWE SIRDFLREIG
APSSAKELKV SPSQIVKALT MAHSLRPERY TILGETGVAG PAAERVAKAT GVIE
//
