ID A0A1A8WZJ6_9APIC Unreviewed; 337 AA. AC A0A1A8WZJ6; DT 05-OCT-2016, integrated into UniProtKB/TrEMBL. DT 05-OCT-2016, sequence version 1. DT 22-FEB-2023, entry version 27. 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; Sar; 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|Proteomes:UP000078546} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Naeem Raeece; RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3- CC phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12; CC Evidence={ECO:0000256|RuleBase:RU361160}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000256|RuleBase:RU361160}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU361160}. CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase CC family. {ECO:0000256|ARBA:ARBA00007406, ECO:0000256|RuleBase:RU000397}. 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 AlphaFoldDB; A0A1A8WZJ6; -. 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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. 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; IPR036291; NAD(P)-bd_dom_sf. DR PANTHER; PTHR10836; GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE; 1. DR PANTHER; PTHR10836:SF76; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE-RELATED; 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; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR TIGRFAMs; TIGR01534; GAPDH-I; 1. DR PROSITE; PS00071; GAPDH; 1. PE 3: Inferred from homology; KW Glycolysis {ECO:0000256|RuleBase:RU361160}; KW NAD {ECO:0000256|PIRSR:PIRSR000149-3, ECO:0000256|RuleBase:RU361160}; KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000149-3}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU361160}. FT DOMAIN 4..153 FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P) FT binding" FT /evidence="ECO:0000259|SMART:SM00846" FT ACT_SITE 153 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-1" FT BINDING 13..14 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3" FT BINDING 35 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3" FT BINDING 122 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3" FT BINDING 152..154 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2" FT BINDING 183 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2" FT BINDING 214..215 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2" FT BINDING 237 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2" FT BINDING 319 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3" FT SITE 180 FT /note="Activates thiol group during catalysis" FT /evidence="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 //