ID G3PC_ANTMA Reviewed; 337 AA. AC P25861; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1992, sequence version 1. DT 25-NOV-2008, entry version 57. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase, cytosolic; DE EC=1.2.1.12; GN Name=GAPC; Synonyms=GAPDH; OS Antirrhinum majus (Garden snapdragon). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Lamiales; Plantaginaceae; Antirrhineae; OC Antirrhinum. OX NCBI_TaxID=4151; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Martin W., Gierl A., Seadler H.; RT "Molecular evidence for pre-Cretaceous angiosperm origins."; RL Nature 339:46-48(1989). CC -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate + CC NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 1/5. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- MISCELLANEOUS: Plants contain three forms of GAPDH: a cytosolic CC form which participates in glycolysis and two chloroplast forms CC which participates in photosynthesis. These three forms are CC encoded by distinct genes. CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate CC dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X59517; CAA42103.1; ALT_INIT; mRNA. DR PIR; S17991; DESKG. DR HSSP; P56649; 1IHX. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (p...; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR000173; GlycerAld_3-P_DHase. DR InterPro; IPR006424; Glyceraldehyde-3-P_DHase_1. DR PANTHER; PTHR10836; GAP_DH; 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 TIGRFAMs; TIGR01534; GAPDH-I; 1. DR PROSITE; PS00071; GAPDH; 1. PE 2: Evidence at transcript level; KW Cytoplasm; Glycolysis; NAD; Oxidoreductase. FT CHAIN 1 337 Glyceraldehyde-3-phosphate dehydrogenase, FT cytosolic. FT /FTId=PRO_0000145593. FT NP_BIND 13 14 NAD (By similarity). FT REGION 153 155 Glyceraldehyde 3-phosphate binding (By FT similarity). FT REGION 213 214 Glyceraldehyde 3-phosphate binding (By FT similarity). FT ACT_SITE 154 154 Nucleophile (By similarity). FT BINDING 35 35 NAD (By similarity). FT BINDING 82 82 NAD; via carbonyl oxygen (By similarity). FT BINDING 184 184 Glyceraldehyde 3-phosphate (By FT similarity). FT BINDING 236 236 Glyceraldehyde 3-phosphate (By FT similarity). FT BINDING 318 318 NAD (By similarity). FT SITE 181 181 Activates thiol group during catalysis FT (By similarity). SQ SEQUENCE 337 AA; 36685 MW; 0E0E69F1F474F0D7 CRC64; MAPIKIGING FGRIGRLVAR VALQRDDVEL VAVNDPFIST DYMTYMFKYD SVHGAWKHHE LKVKDEKTLL FGEKPVVVFG RRNPEEIPRA STGAEYIVES TGVFTDKDKA AAHLKGGAKK VIISAPSKDA PMFVVGVNEK EYKSDLHIVS NASCTTNCLA PLAKVINDRF GIVEGLMTTV HSITATQKTV DGPSAKDWRG GRAASFNIIP SSTGAAKAVG KVLPQLNGKL TGMSFRVPTV DVSVVDLTVR LEKKATYEQI KAAIKEESEG KLKGILGYTE DDVVSTDFVG DSRSSIFDAK AGIALNDNFV KLVSWYDNEW GYSTRVVDLI VHMASVQ //