ID GPDA_SYNY3 Reviewed; 317 AA. AC P73033; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 2. DT 02-SEP-2026, entry version 163. DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(P)+] {ECO:0000255|HAMAP-Rule:MF_00394}; DE EC=1.1.1.94 {ECO:0000255|HAMAP-Rule:MF_00394}; DE AltName: Full=NAD(P)(+)-dependent glycerol-3-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00394}; DE AltName: Full=NAD(P)H-dependent dihydroxyacetone-phosphate reductase {ECO:0000255|HAMAP-Rule:MF_00394}; GN Name=gpsA {ECO:0000255|HAMAP-Rule:MF_00394}; GN OrderedLocusNames=slr1755; OS Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa). OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales; OC Merismopediaceae; Synechocystis. OX NCBI_TaxID=1111708; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27184 / PCC 6803 / Kazusa; RX PubMed=8905231; DOI=10.1093/dnares/3.3.109; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S., RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire RT genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). CC -!- FUNCTION: Catalyzes the reduction of the glycolytic intermediate CC dihydroxyacetone phosphate (DHAP) to sn-glycerol 3-phosphate (G3P), the CC key precursor for phospholipid synthesis. {ECO:0000255|HAMAP- CC Rule:MF_00394}. CC -!- CATALYTIC ACTIVITY: CC Reaction=sn-glycerol 3-phosphate + NAD(+) = dihydroxyacetone phosphate CC + NADH + H(+); Xref=Rhea:RHEA:11092, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, CC ChEBI:CHEBI:57945; EC=1.1.1.94; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00394}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11094; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00394}; CC -!- CATALYTIC ACTIVITY: CC Reaction=sn-glycerol 3-phosphate + NADP(+) = dihydroxyacetone phosphate CC + NADPH + H(+); Xref=Rhea:RHEA:11096, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349; EC=1.1.1.94; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00394}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11098; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00394}; CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism. CC {ECO:0000255|HAMAP-Rule:MF_00394}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00394}. CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate CC dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_00394}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA17053.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BA000022; BAA17053.1; ALT_INIT; Genomic_DNA. DR PIR; S75139; S75139. DR AlphaFoldDB; P73033; -. DR SMR; P73033; -. DR FunCoup; P73033; 388. DR IntAct; P73033; 1. DR STRING; 1148.gene:10497914; -. DR PaxDb; 1148-gene:10497914; -. DR EnsemblBacteria; BAA17053; BAA17053; BAA17053. DR KEGG; syn:slr1755; -. DR eggNOG; COG0240; Bacteria. DR InParanoid; P73033; -. DR PhylomeDB; P73033; -. DR BioCyc; MetaCyc:MONOMER-20261; -. DR UniPathway; UPA00940; -. DR Proteomes; UP000001425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0141152; F:glycerol-3-phosphate dehydrogenase (NAD+) activity; IEA:RHEA. DR GO; GO:0141153; F:glycerol-3-phosphate dehydrogenase (NADP+) activity; IEA:RHEA. DR GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] activity; IBA:GO_Central. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0046167; P:glycerol-3-phosphate biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro. DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IBA:GO_Central. DR GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniRule. DR FunFam; 1.10.1040.10:FF:000001; Glycerol-3-phosphate dehydrogenase [NAD(P)+]; 1. DR FunFam; 3.40.50.720:FF:001174; Glycerol-3-phosphate dehydrogenase [NAD(P)+]; 1. DR Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2. DR HAMAP; MF_00394; NAD_Glyc3P_dehydrog; 1. DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf. DR InterPro; IPR013328; 6PGD_dom2. DR InterPro; IPR006168; G3P_DH_NAD-dep. DR InterPro; IPR006109; G3P_DH_NAD-dep_C. DR InterPro; IPR011128; G3P_DH_NAD-dep_N. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; NF000940; PRK00094.1-2; 1. DR NCBIfam; NF000942; PRK00094.1-4; 1. DR NCBIfam; NF011212; PRK14619.1; 1. DR PANTHER; PTHR11728; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1. DR PANTHER; PTHR11728:SF1; GLYCEROL-3-PHOSPHATE DEHYDROGENASE [NAD(+)] 2, CHLOROPLASTIC; 1. DR Pfam; PF07479; NAD_Gly3P_dh_C; 1. DR Pfam; PF01210; NAD_Gly3P_dh_N; 2. DR PIRSF; PIRSF000114; Glycerol-3-P_dh; 1. DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00957; NAD_G3PDH; 1. PE 3: Inferred from homology; KW Cytoplasm; Lipid biosynthesis; Lipid metabolism; NAD; NADP; KW Nucleotide-binding; Oxidoreductase; Phospholipid biosynthesis; KW Phospholipid metabolism; Reference proteome. FT CHAIN 1..317 FT /note="Glycerol-3-phosphate dehydrogenase [NAD(P)+]" FT /id="PRO_0000138047" FT ACT_SITE 171 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394" FT BINDING 20 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394" FT BINDING 40 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394" FT BINDING 41 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394" FT BINDING 88 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394" FT BINDING 88 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394" FT BINDING 116 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394" FT BINDING 120 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394" FT BINDING 171 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394" FT BINDING 224 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394" FT BINDING 234 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394" FT BINDING 235 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394" FT BINDING 235 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394" FT BINDING 236 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394" FT BINDING 261 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394" SQ SEQUENCE 317 AA; 33511 MW; 1335A86E1B6E0935 CRC64; MSFANADTPP QVVVLGAGAW GSSLAYVLNN NDIPTQVWSR RSPQSLESMV AGADVIVSAV SIKGVPSVAA RLEAMDLQRR TILVTATKGL DPETMTTPSQ IWQAALPSQP IAVLSGPNLS KEIDQGLPAA TVVASSDQAA AEEIQTIFAA DNFRVYTNND PLGTELGGTL KNVMAIAVGV CEGLGLGTNA KSALITRALP EITRVGLHFG AQPDTFWGLA GLGDLLATCS SMLSRNYRVG YGLSKGQSLE EILANLGGTA EGVNTTDVLI KIANREKIAV PITRQVYRLL HGKITPPQAV EALMERELKA EFEDFDL //