G3PC_SINAL
ID G3PC_SINAL Reviewed; 338 AA.
AC P04796;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase, cytosolic;
DE EC=1.2.1.12;
GN Name=GAPC;
OS Sinapis alba (White mustard) (Brassica hirta).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Sinapis.
OX NCBI_TaxID=3728;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3530755; DOI=10.1111/j.1432-1033.1986.tb09871.x;
RA Martin W.F., Cerff R.;
RT "Prokaryotic features of a nucleus-encoded enzyme. cDNA sequences for
RT chloroplast and cytosolic glyceraldehyde-3-phosphate dehydrogenases from
RT mustard (Sinapis alba).";
RL Eur. J. Biochem. 159:323-331(1986).
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; X04301; CAA27844.1; -; mRNA.
DR PIR; A24796; DEIS3C.
DR AlphaFoldDB; P04796; -.
DR SMR; P04796; -.
DR PRIDE; P04796; -.
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; S-nitrosylation.
FT CHAIN 1..338
FT /note="Glyceraldehyde-3-phosphate dehydrogenase, cytosolic"
FT /id="PRO_0000145618"
FT REGION 2..153
FT /note="Binding to NAD"
FT REGION 56..75
FT /note="External loop"
FT REGION 154..338
FT /note="Catalytic"
FT REGION 183..206
FT /note="S-loop"
FT ACT_SITE 156
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 15..16
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 155..157
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 215..216
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 183
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 156
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9FX54"
FT MOD_RES 160
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9FX54"
SQ SEQUENCE 338 AA; 36924 MW; B783A86327E8F658 CRC64;
MADKKIKIGI NGFGRIGRLV ARVILQRNDV ELVAVNDPFI TTEYMTYMFK YDSVHGQWKH
NELKVKDEKT LLFGEKPVTV FGIRNPEDIP WGEAGADFVV ESTGVFTDKD KAAAHLKGGA
KKVVISAPSK DAPMFVVGVN EHEYKSDLNI VSNASCTTNC LAPLAKVIND RFGIVEGLMT
TVHSITATQK TVDGPSMKDW RGGRAASFNI IPSSTGAAKA VGKVLPQLNG KLTGMSFRVP
TVDVSVVDLT VRLEKAATYD EIKKAIKEES QGKLKGILGY TEDDVVSTDF VGDNRSSIFD
AKAGIALSDN FVKLVSWYDN EWGYSTRVVD LIIHMSKA
