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 22-FEB-2023, entry version 94.
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 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 CDD; cd07082; ALDH_F11_NP-GAPDH; 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 PANTHER; PTHR42991; ALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR42991:SF1; ALDEHYDE DEHYDROGENASE; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 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
//
