ID A0A384LPK9_PLAKH Unreviewed; 367 AA. AC A0A384LPK9; A0A1A7VH32; B3LCF6; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 27-MAR-2024, entry version 26. DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] {ECO:0000256|RuleBase:RU361243}; DE EC=1.1.1.8 {ECO:0000256|RuleBase:RU361243}; GN ORFNames=PKNH_1435700 {ECO:0000313|EMBL:CAA9990954.1}; OS Plasmodium knowlesi (strain H). OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium). OX NCBI_TaxID=5851 {ECO:0000313|EMBL:CAA9990954.1, ECO:0000313|Proteomes:UP000031513}; RN [1] {ECO:0000313|EMBL:CAA9990954.1, ECO:0000313|Proteomes:UP000031513} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H {ECO:0000313|EMBL:CAA9990954.1, RC ECO:0000313|Proteomes:UP000031513}; RA Pain A., Boehme U., Berry A.E., Mungall K., Finn R., Jackson A.P., RA Mourier T., Mistry J., Pasini E.M., Aslett M., Balasubrammaniam S., RA Borgwardt K., Brooks K., Carret C., Carver T.J., Cherevach I., RA Chillingworth T., Clarke T.G., Galinski M.R., Hall N., Harper D., RA Harris D., Hauser H., Ivens A., Janssen C.S., Keane T., Larke N., Lapp S., RA Marti M., Moule S., Meyer I.M., Ormond D., Peters N., Sanders M., RA Sanders S., Sergeant T.J., Simmonds M., Smith F., Squares R., Thurston S., RA Tivey A.R., Walker D., White B., Zuiderwijk E., Churcher C., Quail M.A., RA Cowman A.F., Turner C.M.R., Rajandream M.A., Kocken C.H.M., Thomas A.W., RA Newbold C.I., Barrell B.G., Berriman M.; RT "The genome of Plasmodium knowlesi strain H, a zoonotic malaria parasite RT with host range from monkey to man."; RL Nature 455:799-803(2008). 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; AM910996; CAA9990954.1; -; Genomic_DNA. DR RefSeq; XP_002262237.1; XM_002262201.1. DR AlphaFoldDB; A0A384LPK9; -. DR STRING; 5851.A0A384LPK9; -. DR GeneID; 7323256; -. DR KEGG; pkn:PKNH_1435700; -. DR VEuPathDB; PlasmoDB:PKNH_1435700; -. DR InParanoid; A0A384LPK9; -. DR OMA; CVNETVG; -. DR OrthoDB; 3675564at2759; -. DR Proteomes; UP000031513; Chromosome 14. DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule. 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 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 3: Inferred from homology; 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:UP000031513}. FT DOMAIN 15..186 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF01210" FT DOMAIN 208..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; 40994 MW; 3DB2EE664BD7BC86 CRC64; MYKSLFDKLK EGPLKISILG SGNWASAISK VVGTNAKNNY LFENEVKMWV RDERVNGESI VDIINKKHEN VKYLKGVSLP HNIVAYSDLS KVINSADLLI FIIPSQYLEN ALKLIKENQS INIGKHTRAI SLTKGFIIKN NEMYLCSKYI SNLLGIPCSA LSGANIAMDV AMEEFSEATI GGNENETLLI WQRVFDLPYF KINCVNETVG VEIFGALKNI ITLAAGFCDG LNASTNSKSA IIRIGVKESF LFGKTFFNYS DVSIFFESCG LADIITSFLS GRNAKCSAEF VKCKPKKTWE QLESEILKGQ KLQGIVTLKY VYQMIKKNDL THEFPLFTIL HKISFENGDP RELLNIFMNN TVSGIAT //