G3PC_GINBI
ID G3PC_GINBI Reviewed; 340 AA.
AC Q39769;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase, cytosolic;
DE EC=1.2.1.12;
OS Ginkgo biloba (Ginkgo) (Maidenhair tree).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Ginkgoidae; Ginkgoales; Ginkgoaceae; Ginkgo.
OX NCBI_TaxID=3311;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Seed;
RX PubMed=8064871; DOI=10.1007/bf00178247;
RA Jansson S., Meyer-Gauen G., Cerff R., Martin W.;
RT "Nucleotide distribution in gymnosperm nuclear sequences suggests a model
RT for GC-content change in land-plant nuclear genomes.";
RL J. Mol. Evol. 39:34-46(1994).
CC -!- FUNCTION: Key enzyme in glycolysis that catalyzes the first step of the
CC pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-
CC phospho-D-glyceroyl phosphate. Essential for the maintenance of
CC cellular ATP levels and carbohydrate metabolism (By similarity).
CC {ECO:0000250}.
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:0000255|PROSITE-ProRule:PRU10009};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MISCELLANEOUS: Plants contain two types of GAPDH: cytosolic forms which
CC participate in glycolysis and chloroplast forms which participate in
CC photosynthesis. All the forms are encoded by distinct genes.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; L26924; AAA33352.1; -; mRNA.
DR AlphaFoldDB; Q39769; -.
DR SMR; Q39769; -.
DR PRIDE; Q39769; -.
DR UniPathway; UPA00109; UER00184.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 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 Cytoplasm; Glycolysis; NAD; Oxidoreductase.
FT CHAIN 1..340
FT /note="Glyceraldehyde-3-phosphate dehydrogenase, cytosolic"
FT /id="PRO_0000145600"
FT ACT_SITE 157
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 16..17
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 38
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 156..158
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 216..217
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 321
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 184
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 340 AA; 36769 MW; 4D450659E369CFD7 CRC64;
MSSTGKIKIG INGFGRIGRL VARVALLRDD IELVAVNDPF ISTDYMTYMF KYDSVHGQWK
KHEVKVKDSN TLLFGEKAVT VFGCRNPEEI PWGETGVEYV VESTGVFTDK EKAAAHIKGG
AKKVVITAPS KDAPMFVVGV NEHEYKPDLA IVSNASCTTN CLAPLAKVIN DRFGIVEGLM
TTVHSITATQ KTVDGPSNKD WRGGRGAGFN IIPSSTGAAK AVGKVLPALN GKLTGMAFRV
PTPDVSVVDL TVRLEKPASY DEIKAAIKEE SEGKLKGILG YTEDDVVSTD FIGDNRSSIF
DAKAGIALSD NFVKLVSWYD NEWGYSSRVI DLIVHMASTV