ID Q7RRE2_PLAYO Unreviewed; 291 AA. AC Q7RRE2; DT 15-DEC-2003, integrated into UniProtKB/TrEMBL. DT 15-DEC-2003, sequence version 1. DT 27-MAR-2024, entry version 135. DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] {ECO:0000256|RuleBase:RU361243}; DE EC=1.1.1.8 {ECO:0000256|RuleBase:RU361243}; GN ORFNames=PY00789 {ECO:0000313|EMBL:EAA18471.1}; OS Plasmodium yoelii yoelii. OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia). OX NCBI_TaxID=73239 {ECO:0000313|EMBL:EAA18471.1, ECO:0000313|Proteomes:UP000008553}; RN [1] {ECO:0000313|EMBL:EAA18471.1, ECO:0000313|Proteomes:UP000008553} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=17XNL {ECO:0000313|EMBL:EAA18471.1, RC ECO:0000313|Proteomes:UP000008553}; RX PubMed=12368865; DOI=10.1038/nature01099; RA Carlton J.M., Angiuoli S.V., Suh B.B., Kooij T.W., Pertea M., Silva J.C., RA Ermolaeva M.D., Allen J.E., Selengut J.D., Koo H.L., Peterson J.D., Pop M., RA Kosack D.S., Shumway M.F., Bidwell S.L., Shallom S.J., van Aken S.E., RA Riedmuller S.B., Feldblyum T.V., Cho J.K., Quackenbush J., Sedegah M., RA Shoaibi A., Cummings L.M., Florens L., Yates J.R., Raine J.D., Sinden R.E., RA Harris M.A., Cunningham D.A., Preiser P.R., Bergman L.W., Vaidya A.B., RA van Lin L.H., Janse C.J., Waters A.P., Smith H.O., White O.R., RA Salzberg S.L., Venter J.C., Fraser C.M., Hoffman S.L., Gardner M.J., RA Carucci D.J.; RT "Genome sequence and comparative analysis of the model rodent malaria RT parasite Plasmodium yoelii yoelii."; RL Nature 419:512-519(2002). 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EAA18471.1}. 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; AABL01000210; EAA18471.1; -; Genomic_DNA. DR AlphaFoldDB; Q7RRE2; -. DR STRING; 73239.Q7RRE2; -. DR PaxDb; 73239-Q7RRE2; -. DR EnsemblProtists; EAA18471; EAA18471; EAA18471. DR InParanoid; Q7RRE2; -. DR OMA; YDTPPMD; -. DR Proteomes; UP000008553; Unassembled WGS sequence. DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. 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 Membrane {ECO:0000256|SAM:Phobius}; 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:UP000008553}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 5..22 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 43..213 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF01210" FT DOMAIN 233..282 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF07479" FT ACT_SITE 244 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-1" FT BINDING 48..53 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 193 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" SQ SEQUENCE 291 AA; 32637 MW; DA6D39613EC26075 CRC64; MVIRYIFYSI IFINVVLCYS GSSVNPINKN VISPTVKHNG PLKVSIIGSG SWGTVISKII SENTQRSNIF HPIVRMYVNE EIIDNEKLSD IINKTKENVK YMKGMKLPNN IVAIPDIDKV IEDADLLVFV VPHQYLETTL SEILKNKNLK STAKAISLMK GIKICDYKPM LLSNIIENML NIECSVLSGS NIASELSTES FSEATIGFEN LETAEIWREL FDRNYFKINC IQDKSGVEMC GALKNVVALG VGFSEAFKKS YNTKSAIIRI GLEEMKKFAK LFFPNVLDVS N //