ID S0B4C5_ENTIV Unreviewed; 334 AA. AC S0B4C5; DT 18-SEP-2013, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 1. DT 29-MAY-2024, entry version 45. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160}; DE EC=1.2.1.12 {ECO:0000256|RuleBase:RU361160}; OS Entamoeba invadens. OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae; OC Entamoeba. OX NCBI_TaxID=33085 {ECO:0000313|EMBL:BAN42079.1}; RN [1] {ECO:0000313|EMBL:BAN42079.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IP1 {ECO:0000313|EMBL:BAN42079.1}; RA Hiranuka K., Kumagai M., Wakaguri H., Suzuki Y., Sugano S., Watanabe J., RA Makioka A.; RT "Short 5' UTR of Entamoeba genes."; RL Submitted (JUN-2012) 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; AK423680; BAN42079.1; -; mRNA. DR AlphaFoldDB; S0B4C5; -. DR UniPathway; UPA00109; UER00184. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. 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 NCBIfam; TIGR01534; GAPDH-I; 1. 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 PROSITE; PS00071; GAPDH; 1. PE 2: Evidence at transcript level; KW Glycolysis {ECO:0000256|RuleBase:RU361160}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000149-3}; KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000149-3}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU361160}. FT DOMAIN 3..151 FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P) FT binding" FT /evidence="ECO:0000259|SMART:SM00846" FT ACT_SITE 151 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-1" FT BINDING 12..13 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3" FT BINDING 34 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3" FT BINDING 79 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3" FT BINDING 121 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3" FT BINDING 150..152 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2" FT BINDING 181 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2" FT BINDING 210..211 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2" FT BINDING 233 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2" FT BINDING 315 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3" FT SITE 178 FT /note="Activates thiol group during catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-4" SQ SEQUENCE 334 AA; 35925 MW; AA7851CA3D1ABFEB CRC64; MAIKVGINGF GRIGRLVARV IPSRPEFELV ALNDPFMDPK YMEYMLKYDT VHGKFPGTVA VEEGNLVVDG HKIIVKAERD PAQIGWGTLG ADYVVESTGV FTTIPKCEAH IKGGAKKVII SAPSADAPMF VVGVNTEAYK PEMNVLSNAS CTTNCLAPLA KIINNEFGII EGLMTTIHST TATQKTVDGP SGKDWRAGRC AACNIIPAST GAAKAVGKVI PSLNGKLTGM SFRVGTPDVS CVDLTVRTEK EVSVEAINAA ITKYAEGELK GIMGITHDLV VSSDFIHDNR SSIFDAAATI ILNPHFCKLV SWYDNEWGYS TRLVDLIQII NKVH //