ID A0A1A8WZJ6_9APIC Unreviewed; 337 AA. AC A0A1A8WZJ6; DT 05-OCT-2016, integrated into UniProtKB/TrEMBL. DT 05-OCT-2016, sequence version 1. DT 07-JUN-2017, entry version 6. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160}; DE EC=1.2.1.12 {ECO:0000256|RuleBase:RU361160}; GN ORFNames=POVCU1_034250 {ECO:0000313|EMBL:SBS96851.1}; OS Plasmodium ovale curtisi. OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium). OX NCBI_TaxID=864141 {ECO:0000313|EMBL:SBS96851.1, ECO:0000313|Proteomes:UP000078546}; RN [1] {ECO:0000313|EMBL:SBS96851.1, ECO:0000313|Proteomes:UP000078546} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lavstsen T., Jespersen J.S.; RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate + CC NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH. CC {ECO:0000256|RuleBase:RU361160}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 1/5. CC {ECO:0000256|RuleBase:RU361160}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU361160}. CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate CC dehydrogenase family. {ECO:0000256|RuleBase:RU361160}. 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; FLQV01000632; SBS96851.1; -; Genomic_DNA. DR EnsemblProtists; SBS96851; SBS96851; POVCU1_034250. DR UniPathway; UPA00109; UER00184. DR Proteomes; UP000078546; Unassembled WGS sequence. DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-UniRule. DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR020831; GlycerAld/Erythrose_P_DH. DR InterPro; IPR020830; GlycerAld_3-P_DH_AS. DR InterPro; IPR020829; GlycerAld_3-P_DH_cat. DR InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd. DR InterPro; IPR006424; Glyceraldehyde-3-P_DH_1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR10836; PTHR10836; 1. DR Pfam; PF02800; Gp_dh_C; 1. DR Pfam; PF00044; Gp_dh_N; 1. DR PIRSF; PIRSF000149; GAP_DH; 1. DR PRINTS; PR00078; G3PDHDRGNASE. DR SMART; SM00846; Gp_dh_N; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01534; GAPDH-I; 1. DR PROSITE; PS00071; GAPDH; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000078546}; KW Glycolysis {ECO:0000256|RuleBase:RU361160}; KW NAD {ECO:0000256|RuleBase:RU361160}; KW Oxidoreductase {ECO:0000256|RuleBase:RU361160}. FT DOMAIN 4 153 Gp_dh_N. {ECO:0000259|SMART:SM00846}. FT ACT_SITE 153 153 Nucleophile. {ECO:0000256|PIRSR: FT PIRSR000149-1}. FT SITE 180 180 Activates thiol group during catalysis. FT {ECO:0000256|PIRSR:PIRSR000149-4}. SQ SEQUENCE 337 AA; 36587 MW; FAA2CE8AB6763AB2 CRC64; MTVTKVGING FGRIGRLVFR AAYERSDIEV VAINDPFMDI KHLCYLLKYD SVHGKFPCEV TPGEGMFTVG DKKIYVHSEK DPAQIPWGKY AIDVVCESTG VFLTKELAGA HLKGGAKKVI MSAPPKDDTP IYVMGINHQK YDGKQLIVSN ASCTTNCLAP IAKVLNDNFG IVEGLMTTVH ASTANQLVVD GPSKGGKDWR AGRCALQNII PASTGAAKAV GKVLPELNGK LTGVAFRVPI GTVSVVDLVC RLEKPAKYEE VAAQIKKAAD GPLKGILGYT EDEVVSQDFV HDNRSSIFDL KAGLALNDNF FKIVSWYDNE WGYSNRVLDL AVHITKN //