ID R4J9F1_9HEMI Unreviewed; 332 AA. AC R4J9F1; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-AUG-2020, entry version 35. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160}; DE EC=1.2.1.12 {ECO:0000256|RuleBase:RU361160}; OS Macrosteles quadripunctulatus. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Paraneoptera; Hemiptera; Auchenorrhyncha; Membracoidea; OC Cicadellidae; Deltocephalinae; Macrosteles. OX NCBI_TaxID=1128428 {ECO:0000313|EMBL:AGJ71762.1}; RN [1] {ECO:0000313|EMBL:AGJ71762.1} RP NUCLEOTIDE SEQUENCE. RA Galetto L., Marzachi C., Bosco D.; RT "Determining housekeeping genes in two leafhopper vector species challenged RT by phytoplasma infection."; RL Submitted (JUL-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|ARBA:ARBA00004869, CC 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; JX273237; AGJ71762.1; -; mRNA. DR UniPathway; UPA00109; UER00184. 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; IPR036291; NAD(P)-bd_dom_sf. 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 2: Evidence at transcript level; 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 2..149 FT /note="Gp_dh_N" FT /evidence="ECO:0000259|SMART:SM00846" FT NP_BIND 11..12 FT /note="NAD" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3" FT REGION 148..150 FT /note="Glyceraldehyde 3-phosphate binding" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2" FT REGION 208..209 FT /note="Glyceraldehyde 3-phosphate binding" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2" FT ACT_SITE 149 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-1" FT BINDING 32 FT /note="NAD" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3" FT BINDING 77 FT /note="NAD; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3" FT BINDING 119 FT /note="NAD" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3" FT BINDING 179 FT /note="Glyceraldehyde 3-phosphate" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2" FT BINDING 231 FT /note="Glyceraldehyde 3-phosphate" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2" FT BINDING 313 FT /note="NAD" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3" FT SITE 176 FT /note="Activates thiol group during catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-4" SQ SEQUENCE 332 AA; 35511 MW; 4EB990DBEFA68EEE CRC64; MWKIGINGFG RIGRLVLRAS LERGGQVVAI NDPFIGLDYM VYMFKHDSTH GRFKGEVKAE GDFLVVNGNK IAVFSERDPK AIPWGKAGAE YVVESTGVFT TIDKASAHLE GGAKKVIISA PSADAPMFVV GVNLDAYDPS YKVVSNASCT TNCLAPLAKV VHDNFEIVEG LMTTVHATTA TQKTVDGPSG KLWRDGRGAQ QNIIPAATGA AKAVGKVIPA LNGKLTGMAF RVPVPNVSVV DLTVXLGKEA SYDDIKAKVK EAAEGPLKGI LGYTEDDVVS SDFVGDNHSS IFDAKAGIPL NGKFVKLISW YDNEFGYSSR VIDLIKYIQS KD //