ID G3PC_PHYPA Reviewed; 342 AA. AC P34923; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 25-NOV-2008, entry version 54. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase, cytosolic; DE EC=1.2.1.12; GN Name=GAPC; OS Physcomitrella patens (Moss). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta; OC Moss Superclass V; Bryopsida; Funariidae; Funariales; Funariaceae; OC Physcomitrella. OX NCBI_TaxID=3218; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=93196483; PubMed=8095691; RA Martin W., Lydiate D., Brinkmann H., Forkmann G., Saedler H., RA Cerff R.; RT "Molecular phylogenies in angiosperm evolution."; RL Mol. Biol. Evol. 10:140-162(1993). 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 -!- 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; X72381; CAA51071.1; -; mRNA. DR HSSP; P56649; 1DSS. 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 1 342 Glyceraldehyde-3-phosphate dehydrogenase, FT cytosolic. FT /FTId=PRO_0000145613. FT NP_BIND 16 17 NAD (By similarity). FT REGION 155 157 Glyceraldehyde 3-phosphate binding (By FT similarity). FT REGION 215 216 Glyceraldehyde 3-phosphate binding (By FT similarity). FT ACT_SITE 156 156 Nucleophile (By similarity). FT BINDING 38 38 NAD (By similarity). FT BINDING 85 85 NAD; via carbonyl oxygen (By similarity). FT BINDING 186 186 Glyceraldehyde 3-phosphate (By FT similarity). FT BINDING 238 238 Glyceraldehyde 3-phosphate (By FT similarity). FT BINDING 320 320 NAD (By similarity). FT SITE 183 183 Activates thiol group during catalysis FT (By similarity). SQ SEQUENCE 342 AA; 36762 MW; F15CD336F1E4CFCA CRC64; MVGSAKIKVG INGFGRIGRL VARVALERDD IELVAINDPF ITPEYMTYMF KYDSTHGQWK KTEVTLHSEG HLTFGGNPVA VYACRDPSEI PWGKHGADFV VESTGVFTDK DKAAAHLKGG AKKVVISAPS KDAPMFVMGV NENKYSDEDI VSNASCTTNC LAPLAKVIND KFGILEGLMT TVHATTATQK TVDGPSSKDW RGGRSAATNI IPSATGAAKA VGKVLPELNG KLTGMAFRVP TTDVSVVDLT VRLEKPASYD AIKTAIKEAS EGQMKGILGY TEDDVVSTDF ITDSRSSIFD AKAGIALSDT FVKLVAWYDN EWGYSNRVVD LIVHMAKQGT SQ //