GAPN_PEA
ID GAPN_PEA Reviewed; 496 AA.
AC P81406; Q53WX1;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 1.
DT 03-AUG-2022, entry version 90.
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 Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=cv. Rosakrone; TISSUE=Shoot;
RX PubMed=7545914; DOI=10.1006/jmbi.1994.1217;
RA Habenicht A., Hellman U., Cerff R.;
RT "Non-phosphorylating GAPDH of higher plants is a member of the aldehyde
RT dehydrogenase superfamily with no sequence homology to phosphorylating
RT GAPDH.";
RL J. Mol. Biol. 237:165-171(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Habenicht A., Weile H., Cerff R.;
RT "First genomic cloning and characterization of the non-phosphorylating
RT glyceraldehyde-3-phosphate dehydrogenase from higher plants.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP CHARACTERIZATION.
RX PubMed=9461340;
RA Habenicht A.;
RT "The non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase:
RT biochemistry, structure, occurrence and evolution.";
RL Biol. Chem. 378:1413-1419(1997).
RN [4]
RP FUNCTION.
RX PubMed=10338122; DOI=10.1016/s0014-5793(99)00430-5;
RA Valverde F., Losada M., Serrano A.;
RT "Engineering a central metabolic pathway: glycolysis with no net
RT phosphorylation in an Escherichia coli gap mutant complemented with a plant
RT GapN gene.";
RL FEBS Lett. 449:153-158(1999).
CC -!- FUNCTION: Important as a means of generating NADPH for biosynthetic
CC reactions. {ECO:0000269|PubMed:10338122}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; U34988; AAO38512.1; -; Genomic_DNA.
DR EMBL; X75327; CAA53076.1; -; mRNA.
DR PIR; S43832; S43832.
DR AlphaFoldDB; P81406; -.
DR SMR; P81406; -.
DR PRIDE; P81406; -.
DR EnsemblPlants; Psat4g008600.1; Psat4g008600.1.cds; Psat4g008600.
DR Gramene; Psat4g008600.1; Psat4g008600.1.cds; Psat4g008600.
DR SABIO-RK; P81406; -.
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 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; Direct protein sequencing; NADP; Oxidoreductase.
FT CHAIN 1..496
FT /note="NADP-dependent glyceraldehyde-3-phosphate
FT dehydrogenase"
FT /id="PRO_0000056578"
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 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"
SQ SEQUENCE 496 AA; 53004 MW; 52FADC2F77C613FA CRC64;
MAATGVLAEI IDGDVYKYYA DGEWKKSTSG KSVAIINPTT RKPQYKVQAC SQEEVNKVMD
SAKSAQKSWA KTPLWKRAEL LHKAAAILKE HKAAIAECLV KEIAKPAKDA VTEVVRSGDL
VSYCAEEGVR ILGEGKFLVS DSFPGNERTK YCLTSKIPLG VILAIPPFNY PVNLAVSKIA
PALIAGNSIV LKPPTQGAVA ALHMVHCFHL AGFPKGLISC VTGKGSEIGD FLTMHPGVNC
ISFTGGDTGI AISKKSGMIP LQMELGGKDA CIVLEDADLD LVAANIIKGG FSYSGQRCTA
VKVVLVMESV ADALVEKVKV KVAKLSVGPP EDDSDITPVV SESSANFIEG LVNDAKEKGA
TFCQEYKREG NLIWPLLLDN VRPDMRIAWE EPFGPVLPVI RINSVEEGIH HCNASNFGLQ
GCVFTKDINK AIMISDAMES GTVQINSAPA RGPDHFPFQG IKDSGIGSQG ITNSINMMTK
VKTTVINLPS PSYTMG
