G1PDH_METMA
ID G1PDH_METMA Reviewed; 356 AA.
AC Q8PZA4;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 130.
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=MM_0590;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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; AE008384; AAM30286.1; -; Genomic_DNA.
DR RefSeq; WP_011032541.1; NC_003901.1.
DR AlphaFoldDB; Q8PZA4; -.
DR SMR; Q8PZA4; -.
DR STRING; 192952.MM_0590; -.
DR EnsemblBacteria; AAM30286; AAM30286; MM_0590.
DR GeneID; 44086199; -.
DR GeneID; 66134246; -.
DR KEGG; mma:MM_0590; -.
DR PATRIC; fig|192952.21.peg.694; -.
DR eggNOG; arCOG00982; Archaea.
DR HOGENOM; CLU_038362_0_0_2; -.
DR OMA; ALHGEQC; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000000595; 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..356
FT /note="Glycerol-1-phosphate dehydrogenase [NAD(P)+]"
FT /id="PRO_0000157344"
FT BINDING 103..107
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 125..128
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 134
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 273
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
SQ SEQUENCE 356 AA; 38065 MW; 4AC98A82E6AC2F31 CRC64;
MKLTINKNSA KWMQLPRDVL VGHGVLEEVG DVCRDLKLKG NALIVTGSTT QDVAGKRVSR
LLEDAGNSTE TVLTCRATME EVDKLMEKAL NTEATFLLGV GSGRSIDLAK LASTRLEIPF
ISVPTAASHD GIASSRASVI DNGKNASIQA QAPLAVIADT EIISAAPYRF LAAGCGDIIS
NYTAVLDWEL ASRLRNEYFG EYAAALSRMA ARVVIENADS IKPDHETSAR LVVKALVSNG
VAMSIAGSSR PASGSEHMFS HALDRIAPKA ALHGEQCGVG TIMMMYLHGG NWQEIRDALK
KIGAPTNAEE LGIEDKYIIE ALLQAHSIRP DRYTILGNGL TLSAAEKVAR ITKVIN
