GAPN_WHEAT
ID GAPN_WHEAT Reviewed; 496 AA.
AC Q8LK61; Q8L5J9;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=NADP-dependent glyceraldehyde-3-phosphate dehydrogenase;
DE EC=1.2.1.9;
DE AltName: Full=Glyceraldehyde-3-phosphate dehydrogenase [NADP(+)];
DE AltName: Full=Non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase;
DE AltName: Full=Triosephosphate dehydrogenase;
GN Name=GAPN;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], BIOPHYSICOCHEMICAL PROPERTIES, AND
RP PHOSPHORYLATION.
RC TISSUE=Endosperm, and Leaf;
RX PubMed=12387887; DOI=10.1016/s0014-5793(02)03455-5;
RA Bustos D.M., Iglesias A.A.;
RT "Non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase is post-
RT translationally phosphorylated in heterotrophic cells of wheat (Triticum
RT aestivum).";
RL FEBS Lett. 530:169-173(2002).
RN [2]
RP SEQUENCE REVISION.
RC TISSUE=Leaf;
RA Piattoni C.V., Guerrero S.A., Bustos D.M., Iglesias A.A.;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH 14-3-3 PROTEIN, SUBCELLULAR LOCATION, AND ACTIVITY
RP REGULATION.
RX PubMed=14681537; DOI=10.1104/pp.103.030981;
RA Bustos D.M., Iglesias A.A.;
RT "Phosphorylated non-phosphorylating glyceraldehyde-3-phosphate
RT dehydrogenase from heterotrophic cells of wheat interacts with 14-3-3
RT proteins.";
RL Plant Physiol. 133:2081-2088(2003).
RN [4]
RP 3D-STRUCTURE MODELING.
RX PubMed=15896993; DOI=10.1016/j.jmgm.2005.03.002;
RA Bustos D.M., Iglesias A.A.;
RT "A model for the interaction between plant GAPN and 14-3-3zeta using
RT protein-protein docking calculations, electrostatic potentials and
RT kinetics.";
RL J. Mol. Graph. Model. 23:490-502(2005).
CC -!- FUNCTION: Important as a means of generating NADPH for biosynthetic
CC reactions.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + H2O + NADP(+) = (2R)-3-
CC phosphoglycerate + 2 H(+) + NADPH; Xref=Rhea:RHEA:14669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58272, ChEBI:CHEBI:58349, ChEBI:CHEBI:59776; EC=1.2.1.9;
CC -!- ACTIVITY REGULATION: Insensitive to magnesium or calcium when
CC dephosphorylated. When phosphorylated, 3-fold activation by magnesium
CC or calcium, 2-fold activation by potassium, inhibited by ADP and AMP
CC and insensitive to ATP or PPi. {ECO:0000269|PubMed:14681537}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=40 uM for NADP {ECO:0000269|PubMed:12387887};
CC KM=118 uM for D-glyceraldehyde-3-phosphate
CC {ECO:0000269|PubMed:12387887};
CC Note=When the protein is phosphorylated, the affinity for substrates
CC is similar but the Vmax is lowered.;
CC -!- SUBUNIT: Interacts with 14-3-3 protein when phosphorylated. This
CC interaction is released by divalent cations.
CC {ECO:0000269|PubMed:14681537}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14681537}.
CC -!- PTM: Phosphorylated in shoots and non-photosynthetic tissues, but not
CC in leaves. {ECO:0000269|PubMed:12387887}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
CC -!- CAUTION: Sequences of mRNA encoded by the same gene but extracted from
CC leaves (AF521191) or from endosperm (AF521190) differ at several
CC prositions due to sequencing uncertainties. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM77678.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF521190; AAM77678.1; ALT_FRAME; mRNA.
DR EMBL; AF521191; AAM77679.2; -; mRNA.
DR AlphaFoldDB; Q8LK61; -.
DR SMR; Q8LK61; -.
DR STRING; 4565.Traes_2DS_22500FA4F.1; -.
DR PRIDE; Q8LK61; -.
DR eggNOG; KOG2450; Eukaryota.
DR BRENDA; 1.2.1.9; 6500.
DR SABIO-RK; Q8LK61; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; Q8LK61; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008886; F:glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0008911; F:lactaldehyde dehydrogenase activity; IBA:GO_Central.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; NADP; Oxidoreductase; Phosphoprotein; Reference proteome.
FT CHAIN 1..496
FT /note="NADP-dependent glyceraldehyde-3-phosphate
FT dehydrogenase"
FT /id="PRO_0000291765"
FT ACT_SITE 264
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 298
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 169..170
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 245..249
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 297..299
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 391
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 451
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 169
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 404
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT CONFLICT 98
FT /note="S -> C (in Ref. 1; AAM77678)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="V -> I (in Ref. 1; AAM77678)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="V -> A (in Ref. 1; AAM77678)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="V -> G (in Ref. 1; AAM77678)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="S -> A (in Ref. 1; AAM77678)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="E -> Z (in Ref. 1; AAM77678)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 496 AA; 53047 MW; F37AB38E8561A287 CRC64;
MAGTGVFADV LDGEVYKYYA DGEWRASASG KTVAIVNPTT RQTQYRVQAC TQEEVNKVMD
AAKVAQKSWA RTPLWKRAEL LHKAAAILKE HKTPIAESLV KEIAKPAKDA VSEVVRSGDL
VSYTAEEGVR ILGEGKLLVS DSFPGNERNK YCLSSKVPLG VVLAIPPFNY PVNLAVSKIG
PALIAGNSLV LKPPTQGAVA ALHMVHCFHL AGFPKGLISC VTGKGSEIGD FLTMHPGVNC
ISFTGGDTGI AISKKAGMVP LQMELGGKDA CIVLEDADLD LVAANIVKGG FSYSGQRCTA
VKVVLIMEAV ADTVVEKVNA KLAKLKVGPP EDDSDITPVV TESSANFIEG LVMDAKEKGA
TFCQEYRREG NLIWPLLLDH VRPDMRIAWE EPFGPVLPVI RINSVEEGIH HCNASNFGLQ
GCVFTRDINK AIMISDAMES GTVQINSAPA RGPDHFPFQG LKDSGIGSQG ITNSINMMTK
VKSTVINLPS PSYTMG
