ID GPDA_RICPR Reviewed; 316 AA. AC Q9ZDA0; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 27-MAR-2024, entry version 140. 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)H-dependent glycerol-3-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00394}; GN Name=gpsA {ECO:0000255|HAMAP-Rule:MF_00394}; OrderedLocusNames=RP442; OS Rickettsia prowazekii (strain Madrid E). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group. OX NCBI_TaxID=272947; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Madrid E; RX PubMed=9823893; DOI=10.1038/24094; RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., RA Kurland C.G.; RT "The genome sequence of Rickettsia prowazekii and the origin of RT mitochondria."; RL Nature 396:133-140(1998). CC -!- CATALYTIC ACTIVITY: CC Reaction=NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate CC + H(+) + NADH; 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 -!- CATALYTIC ACTIVITY: CC Reaction=NADP(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate CC + H(+) + NADPH; 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 -!- 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 --------------------------------------------------------------------------- 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; AJ235271; CAA14899.1; -; Genomic_DNA. DR PIR; A71703; A71703. DR RefSeq; NP_220823.1; NC_000963.1. DR RefSeq; WP_004599474.1; NC_000963.1. DR AlphaFoldDB; Q9ZDA0; -. DR SMR; Q9ZDA0; -. DR STRING; 272947.gene:17555522; -. DR EnsemblBacteria; CAA14899; CAA14899; CAA14899. DR GeneID; 57569567; -. DR KEGG; rpr:RP442; -. DR PATRIC; fig|272947.5.peg.455; -. DR eggNOG; COG0240; Bacteria. DR HOGENOM; CLU_033449_0_0_5; -. DR OrthoDB; 9812273at2; -. DR BRENDA; 1.1.1.94; 5447. DR UniPathway; UPA00940; -. DR Proteomes; UP000002480; Chromosome. DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro. DR GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-UniRule. 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:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. 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 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; 1. DR PIRSF; PIRSF000114; Glycerol-3-P_dh; 1. DR PRINTS; PR00077; GPDHDRGNASE. 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; Oxidoreductase; KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome. FT CHAIN 1..316 FT /note="Glycerol-3-phosphate dehydrogenase [NAD(P)+]" FT /id="PRO_0000138017" FT ACT_SITE 192 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394" FT BINDING 11..16 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394" FT BINDING 109 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394" FT BINDING 109 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394" FT BINDING 141 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394" FT BINDING 259..260 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394" FT BINDING 259 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394" FT BINDING 285 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394" SQ SEQUENCE 316 AA; 34487 MW; EBA9E84E19874D42 CRC64; MNKFKNIAVY GGGSFGTSLA SLVARNCNNV TLFLRDEIIL KEILYKKTNA QYLGDIELPT NLQATTNLSV IKDFELIIIA VPSYAFDDSI KLLKTYGISK EHTILVATKG LADNPTELFS DRLNTLLPDN PIGFLSGPNL AKELAKNLPA SASIASLDID IANKIAYNFS SKTFSTNTTI DIVTLQIAGA LKNIFAIKSG IDLAREQGAN SRATLIVGAL KEITTLSKVL GGMQKNSDIL LEAGVLGDLV LTCYSLGSRN TKFGYEFEIS RDKKKFLCEY KELVEGREAL KLVLDLIKKY NLHMPIVAEV ASLILI //