ID R4J9F1_9HEMI Unreviewed; 332 AA. AC R4J9F1; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 08-JUN-2016, entry version 15. 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; OC Pterygota; Neoptera; Paraneoptera; Hemiptera; Euhemiptera; OC Membracoidea; 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 RT challenged by phytoplasma infection."; RL Submitted (JUL-2012) 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; JX273237; AGJ71762.1; -; mRNA. DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-EC. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. 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; -; 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; 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 2: Evidence at transcript level; KW Glycolysis {ECO:0000256|RuleBase:RU361160}; KW NAD {ECO:0000256|RuleBase:RU361160}; KW Oxidoreductase {ECO:0000256|RuleBase:RU361160}. FT DOMAIN 2 149 Gp_dh_N. {ECO:0000259|SMART:SM00846}. FT ACT_SITE 149 149 Nucleophile. {ECO:0000256|PIRSR: FT PIRSR000149-1}. FT SITE 176 176 Activates thiol group during catalysis. FT {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 //