ID   GAPN_NICPL              Reviewed;         496 AA.
AC   P93338;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 91.
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   Nicotiana plumbaginifolia (Leadwort-leaved tobacco) (Tex-Mex tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4092;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9370287; DOI=10.1016/s0378-1119(97)00320-x;
RA   Habenicht A., Quesada A., Cerff R.;
RT   "Sequence of the non-phosphorylating glyceraldehyde-3-phosphate
RT   dehydrogenase from Nicotiana plumbaginifolia and phylogenetic origin of the
RT   gene family.";
RL   Gene 198:237-243(1997).
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   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; U87848; AAB47571.1; -; mRNA.
DR   AlphaFoldDB; P93338; -.
DR   SMR; P93338; -.
DR   PRIDE; P93338; -.
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   2: Evidence at transcript level;
KW   Cytoplasm; NADP; Oxidoreductase.
FT   CHAIN           1..496
FT                   /note="NADP-dependent glyceraldehyde-3-phosphate
FT                   dehydrogenase"
FT                   /id="PRO_0000056577"
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"
SQ   SEQUENCE   496 AA;  53144 MW;  6F350F1688D7A108 CRC64;
     MAGNGVFVDI IEGDVFKYYS EGEWKKSASG KSVAIINPTT RKTQYKVQAC TQEEVNKVME
     VAKTAQKSWA KTPLWKRAEL LHKAAAILKE HKAPIAECLV KEIAKPAKDA VTEVVRSGDL
     VSYTAEEGVR ILGEGKFLVS DSFPGNERTK YCLTSKIPLG VILAIPPFNY PVNLAVSKIA
     PALIAGNSLV LKPPTQGAVA CLHMVHCFHL AGFPKGLISC VTGKGSEIGD FLTMHPGVHC
     ISFTGGDTGV AISKKAGMIP LQMELGGKDA CIVLEDADLD LAAGSIVKGG FSYSGQRCTA
     VKVVLVMESV ADALVEKVNA KVAKLTVGPP EDDCDITPVV SESSANFIEG LVMDAKQKNA
     TFCQQYKREG NLIWPLLLDN VRPDMRIAWE EPFGPVLPVI RINSVEEGIH HCNASNFGLQ
     GCVFTKDINK AILISDAMET GTVQINSAPA RGPDHFPFQG IKDSGIGSQG ITNSINMMTK
     VKTTVINLPT PSYTMG