G1PDH_THEKO
ID G1PDH_THEKO Reviewed; 351 AA.
AC Q5JH91;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Glycerol-1-phosphate dehydrogenase [NAD(P)+] {ECO:0000255|HAMAP-Rule:MF_00497};
DE Short=G1P dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00497};
DE Short=G1PDH {ECO:0000255|HAMAP-Rule:MF_00497};
DE EC=1.1.1.261 {ECO:0000255|HAMAP-Rule:MF_00497};
DE AltName: Full=Enantiomeric glycerophosphate synthase {ECO:0000255|HAMAP-Rule:MF_00497};
DE AltName: Full=sn-glycerol-1-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00497};
GN Name=egsA {ECO:0000255|HAMAP-Rule:MF_00497}; OrderedLocusNames=TK0789;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
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:0000255|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:0000255|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:0000255|HAMAP-
CC Rule:MF_00497};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00497};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00497};
CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_00497}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00497}.
CC -!- SIMILARITY: Belongs to the glycerol-1-phosphate dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_00497}.
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DR EMBL; AP006878; BAD84978.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5JH91; -.
DR SMR; Q5JH91; -.
DR STRING; 69014.TK0789; -.
DR PRIDE; Q5JH91; -.
DR EnsemblBacteria; BAD84978; BAD84978; TK0789.
DR KEGG; tko:TK0789; -.
DR PATRIC; fig|69014.16.peg.769; -.
DR eggNOG; arCOG00982; Archaea.
DR HOGENOM; CLU_038362_0_0_2; -.
DR InParanoid; Q5JH91; -.
DR OMA; ALHGEQC; -.
DR PhylomeDB; Q5JH91; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000000536; Chromosome.
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 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; PTHR43616; 1.
DR Pfam; PF13685; Fe-ADH_2; 1.
DR PIRSF; PIRSF000112; Glycerol_dehydrogenase; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Lipid biosynthesis; Lipid metabolism; Metal-binding; NAD; NADP;
KW Oxidoreductase; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Zinc.
FT CHAIN 1..351
FT /note="Glycerol-1-phosphate dehydrogenase [NAD(P)+]"
FT /id="PRO_0000157351"
FT BINDING 98..102
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 120..123
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 129
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
SQ SEQUENCE 351 AA; 37756 MW; 67A8EC4FEA4F15F0 CRC64;
MERRIHLMQL PREVLLGENL TGEVVSVAKR IGLTGKALVI YGPKTKEIAG RDVEDAIKSA
YEVSSLTIRK GATMEEVERT IEKIKDEGIG WVIAVGGGSI IDVAKLSSFK TGVPFISFPT
TASHDGIASA NASIKDLGSK TSVKAVPPVA VIADVKVIKT APYRYLAAGV GDTISNLTAV
RDWQLAHRIK GEYYSEYAAS LSLMSAKMVM RNADIIRLGN EESVRKVIKA LISTGVAMSI
AGSSRPASGA EHLFSHALDM LLDKPALHGE QTGLGTIIMA YLHGMKWERV RETLKRVGAP
TNAYELGIDP EVIIEALTIA HTIRPERYTI LGKDGLTREA AEKAAKITGV I
