G3PC1_MAIZE
ID G3PC1_MAIZE Reviewed; 337 AA.
AC P08735;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 1, cytosolic;
DE EC=1.2.1.12;
GN Name=GAPC1; Synonyms=GAPC, GPC1;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Wisconsin 22;
RX 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 encoding
RT cytosolic glyceraldehyde-3-phosphate dehydrogenase from maize.";
RL J. Mol. Biol. 208:551-565(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX 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 chloroplast
RT glyceraldehyde-3-phosphate dehydrogenase from maize.";
RL J. Mol. Evol. 26:320-328(1987).
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; X07156; CAA30151.1; -; mRNA.
DR EMBL; X15596; CAA33620.1; -; Genomic_DNA.
DR PIR; S00354; DEZMGC.
DR RefSeq; NP_001105413.1; NM_001111943.1.
DR AlphaFoldDB; P08735; -.
DR SMR; P08735; -.
DR STRING; 4577.GRMZM2G046804_P07; -.
DR PaxDb; P08735; -.
DR PRIDE; P08735; -.
DR ProMEX; P08735; -.
DR GeneID; 542367; -.
DR KEGG; zma:542367; -.
DR MaizeGDB; 13873; -.
DR eggNOG; KOG0657; Eukaryota.
DR OrthoDB; 945145at2759; -.
DR UniPathway; UPA00109; UER00184.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P08735; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; TAS:AgBase.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IBA:GO_Central.
DR GO; GO:0070403; F:NAD+ binding; TAS:AgBase.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0042301; F:phosphate ion binding; TAS:AgBase.
DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR GO; GO:0009416; P:response to light stimulus; TAS:AgBase.
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; Reference proteome.
FT CHAIN 1..337
FT /note="Glyceraldehyde-3-phosphate dehydrogenase 1,
FT cytosolic"
FT /id="PRO_0000145605"
FT REGION 1..151
FT /note="Binding to NAD"
FT REGION 152..337
FT /note="Catalytic"
FT ACT_SITE 154
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 13..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 35
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 153..155
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 213..214
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 318
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 181
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250"
FT CONFLICT 336
FT /note="T -> S (in Ref. 2; CAA30151)"
FT /evidence="ECO:0000305"
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
