ID G3PC_MAIZE Reviewed; 337 AA. AC P08735; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 2. DT 16-JUN-2009, entry version 74. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase, cytosolic 1; DE EC=1.2.1.12; GN Name=GAPC1; Synonyms=GAPC, GPC1; OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Wisconsin 22; RX MEDLINE=90040690; PubMed=2810356; DOI=10.1016/0022-2836(89)90147-2; RA Martinez P., Martin W.F., Cerff R.; RT "Structure, evolution and anaerobic regulation of a nuclear gene RT encoding cytosolic glyceraldehyde-3-phosphate dehydrogenase from RT maize."; RL J. Mol. Biol. 208:551-565(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=88230473; PubMed=3131533; DOI=10.1007/BF02101150; RA Brinkmann H., Martinez P., Quigley F., Martin W.F., Cerff R.; RT "Endosymbiotic origin and codon bias of the nuclear gene for RT chloroplast glyceraldehyde-3-phosphate dehydrogenase from maize."; RL J. Mol. Evol. 26:320-328(1987). 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; X07156; CAA30151.1; -; mRNA. DR EMBL; X15596; CAA33620.1; -; Genomic_DNA. DR PIR; S00354; DEZMGC. DR RefSeq; NP_001105413.1; -. DR UniGene; Zm.3765; -. DR HSSP; P56649; 1DSS. DR GeneID; 542367; -. DR Gramene; P08735; -. DR MaizeGDB; 13873; -. DR BRENDA; 1.2.1.12; 289. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (p...; IEA:EC. DR GO; GO:0051287; F:NAD or NADH 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_DH. DR InterPro; IPR006424; Glyceraldehyde-3-P_DH_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 1. FT /FTId=PRO_0000145605. FT NP_BIND 13 14 NAD (By similarity). FT REGION 1 151 Binding to NAD. FT REGION 152 337 Catalytic. 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). FT CONFLICT 336 336 T -> S (in Ref. 2; CAA30151). SQ SEQUENCE 337 AA; 36523 MW; E18F580F09FDC07B CRC64; MGKIKIGING FGRIGRLVAR VALQSEDVEL VAVNDPFITT DYMTYMFKYD TVHGHWKHSD ITLKDSKTLL FGDKPVTVFG IRNPEEIPWG EAGAEYVVES TGVFTDKDKA AAHLKGGAKK VVISAPSKDA PMFVVGVNED KYTSDVNIVS NASCTTNCLA PLAKVIHDNF GIVEGLMTTV HAITATQKTV DGPSAKDWRG GRAASFNIIP SSTGAAKAVG KVLPDLNGKL TGMSFRVPTV DVSVVDLTVR IEKGASYEDI KKAIKAASEG PLKGIMGYVE EDLVSTDFLG DSRSSIFDAK AGIALNDHFV KLVSWYDNEW GYSNRVVDLI RHMFKTQ //