ID Q8I5P5_PLAF7 Unreviewed; 367 AA. AC Q8I5P5; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 162. DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] {ECO:0000256|RuleBase:RU361243}; DE EC=1.1.1.8 {ECO:0000256|RuleBase:RU361243}; GN ORFNames=PF3D7_1216200 {ECO:0000313|EMBL:CZT99323.1}; OS Plasmodium falciparum (isolate 3D7). OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Laverania). OX NCBI_TaxID=36329 {ECO:0000313|EMBL:CZT99323.1, ECO:0000313|Proteomes:UP000001450}; RN [1] {ECO:0000313|EMBL:CZT99323.1, ECO:0000313|Proteomes:UP000001450} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Isolate 3D7 {ECO:0000313|Proteomes:UP000001450}; RX PubMed=12368864; DOI=10.1038/nature01097; RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W., RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K., RA Eisen J.A., Rutherford K., Salzberg S.L., Craig A., Kyes S., Chan M.S., RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M., RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M., RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I., RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J., RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.; RT "Genome sequence of the human malaria parasite Plasmodium falciparum."; RL Nature 419:498-511(2002). RN [2] {ECO:0007829|PDB:1YJ8} RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS). RA Robien M.A., Hol W.G.J., RA Medical Structural Genomics of Pathogenic Protozoa.; RT "Initial structural analysis of Plasmodium falciparum Glycerol-3-phosphate RT dehydrogenase."; RL Submitted (JAN-2005) to the PDB data bank. 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=1.1.1.8; CC Evidence={ECO:0000256|ARBA:ARBA00001662, CC ECO:0000256|RuleBase:RU361243}; CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00011009, CC ECO:0000256|RuleBase:RU000437}. 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; LN999947; CZT99323.1; -; Genomic_DNA. DR RefSeq; XP_001350565.1; XM_001350529.2. DR PDB; 1YJ8; X-ray; 2.85 A; A/B/C=1-367. DR PDBsum; 1YJ8; -. DR AlphaFoldDB; Q8I5P5; -. DR SMR; Q8I5P5; -. DR STRING; 36329.Q8I5P5; -. DR PaxDb; 5833-PFL0780w; -. DR EnsemblProtists; CZT99323; CZT99323; PF3D7_1216200. DR GeneID; 811209; -. DR KEGG; pfa:PF3D7_1216200; -. DR VEuPathDB; PlasmoDB:PF3D7_1216200; -. DR HOGENOM; CLU_033449_2_2_1; -. DR InParanoid; Q8I5P5; -. DR OMA; CVNETVG; -. DR OrthoDB; 3675564at2759; -. DR PhylomeDB; Q8I5P5; -. DR Reactome; R-PFA-1483166; Synthesis of PA. DR EvolutionaryTrace; Q8I5P5; -. DR Proteomes; UP000001450; Chromosome 12. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; ISS:GeneDB. DR GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-UniRule. DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule. DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; ISS:GeneDB. DR GO; GO:0006116; P:NADH oxidation; IBA:GO_Central. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR017751; G3P_DH_NAD-dep_euk. DR InterPro; IPR011128; G3P_DH_NAD-dep_N. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR03376; glycerol3P_DH; 1. DR PANTHER; PTHR11728; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1. DR PANTHER; PTHR11728:SF8; GLYCEROL-3-PHOSPHATE DEHYDROGENASE [NAD(+)]-RELATED; 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. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:1YJ8}; KW NAD {ECO:0000256|PIRSR:PIRSR000114-3, ECO:0000256|RuleBase:RU000437}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU000437}; KW Reference proteome {ECO:0000313|Proteomes:UP000001450}. FT DOMAIN 15..186 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF01210" FT DOMAIN 209..354 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF07479" FT ACT_SITE 218 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-1" FT BINDING 134 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 167 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 282..283 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 282 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 311 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 313 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" SQ SEQUENCE 367 AA; 41234 MW; 20936A730B93B907 CRC64; MYRNLFDKLK DGPLKISILG SGNWASAISK VVGTNAKNNY LFENEVRMWI RDEFVNGERM VDIINNKHEN TKYLKGVPLP HNIVAHSDLA SVINDADLLI FIVPCQYLES VLASIKESES IKIASHAKAI SLTKGFIVKK NQMKLCSNYI SDFLNIPCSA LSGANIAMDV AMENFSEATI GGNDKDSLVI WQRVFDLPYF KINCVNETIE VEICGALKNI ITLACGFCDG LNLPTNSKSA IIRNGINEMI LFGKVFFQKF NENILLESCG FADIITSFLA GRNAKCSAEF IKSTPKKTWE ELENEILKGQ KLQGTVTLKY VYHMIKEKNM TNEFPLFTVL HKISFENEDP SSLLKTFMNN KINQLNL //