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G1PDH_THEPD
ID   G1PDH_THEPD             Reviewed;         347 AA.
AC   A1RZJ9;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=Tpen_1231;
OS   Thermofilum pendens (strain DSM 2475 / Hrk 5).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermofilales; Thermofilaceae;
OC   Thermofilum.
OX   NCBI_TaxID=368408;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2475 / Hrk 5;
RX   PubMed=18263724; DOI=10.1128/jb.01949-07;
RA   Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E.,
RA   Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M.,
RA   Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B.,
RA   Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N.;
RT   "Genome sequence of Thermofilum pendens reveals an exceptional loss of
RT   biosynthetic pathways without genome reduction.";
RL   J. Bacteriol. 190:2957-2965(2008).
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   -!- SUBUNIT: Homodimer. {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; CP000505; ABL78629.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1RZJ9; -.
DR   SMR; A1RZJ9; -.
DR   STRING; 368408.Tpen_1231; -.
DR   PRIDE; A1RZJ9; -.
DR   EnsemblBacteria; ABL78629; ABL78629; Tpen_1231.
DR   KEGG; tpe:Tpen_1231; -.
DR   eggNOG; arCOG00982; Archaea.
DR   HOGENOM; CLU_038362_0_0_2; -.
DR   OMA; ALHGEQC; -.
DR   OrthoDB; 57545at2157; -.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000000641; 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..347
FT                   /note="Glycerol-1-phosphate dehydrogenase [NAD(P)+]"
FT                   /id="PRO_0000350663"
FT   BINDING         90..94
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT   BINDING         112..115
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT   BINDING         117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT   BINDING         121
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT   BINDING         165
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT   BINDING         165
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT   BINDING         245
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT   BINDING         249
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT   BINDING         262
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
SQ   SEQUENCE   347 AA;  36660 MW;  A06DF0E00A2C68D8 CRC64;
     MRAELPKRVV VERGALQFLP EVLRELGCSK TVVVTDSGVW SVVGSVVEGA LRGLAYEVVY
     IEAADNSNVE RARSAARRVE ACAVAGLGGG RPVDVAKYAA FMEGLPFVSV PTAISHDGFA
     SPIVALKDPE GNPLSIFTRP PAAVLVDLAV VSRAPRRLLA SGVGDIVGKV TSVADARLAQ
     RLTGEEVPEV ALRMAETAAR MVLDEVDEIA SWTERGVGVL AQAGLLAGMA MAVAGSSRPC
     SGSEHLFSHS LDKYVPWKKS LHGEQVGVGA IIASYLHGFN WRVIRDALAK VGAPTTVEGL
     GVTGEDAVRA LLKARELRKR FTILDVVELN EGLAWKVLRE TGVAPTA
 
 
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