ID   GAPN_MAIZE              Reviewed;         498 AA.
AC   Q43272;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 113.
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=GPN1;
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 [MRNA].
RC   STRAIN=cv. KW5330; 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).
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; X75326; CAA53075.1; -; mRNA.
DR   PIR; S43833; S43833.
DR   RefSeq; NP_001105589.1; NM_001112119.1.
DR   AlphaFoldDB; Q43272; -.
DR   SMR; Q43272; -.
DR   STRING; 4577.GRMZM2G035268_P01; -.
DR   PaxDb; Q43272; -.
DR   PRIDE; Q43272; -.
DR   GeneID; 542583; -.
DR   KEGG; zma:542583; -.
DR   MaizeGDB; 78926; -.
DR   eggNOG; KOG2450; Eukaryota.
DR   OrthoDB; 692580at2759; -.
DR   SABIO-RK; Q43272; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; Q43272; 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   2: Evidence at transcript level;
KW   Cytoplasm; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..498
FT                   /note="NADP-dependent glyceraldehyde-3-phosphate
FT                   dehydrogenase"
FT                   /id="PRO_0000056576"
FT   ACT_SITE        266
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   ACT_SITE        300
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   BINDING         118
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         171..172
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         194
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         197
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         232
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         247..251
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         299..301
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         393
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         453
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            171
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   498 AA;  53146 MW;  7AF1C0DACAB4EE39 CRC64;
     MALAGTGVFA EILDGEVYRY YADGEWRTSA SGKSVAIVNP TTRKTQYRVQ ACTQEEVNKA
     MDAAKVAQKA WARTPLWKRA DVLHKAAAIL KEHKAPIAEC LVKEIAKPAK DAVSEVVRSG
     DLVSYTAEEG VRILGEGKLV VSDSFPGNER NKYCLSSKIP LGVVLAIPPF NYPANLAGSK
     IGPALIAGNA LVLKPPTQGA VAALHMVHCF HLAGFPKGLI SCVTGKGSEI GDFLTMHPGV
     NCISFTGGDT GIAISKKAGM VPLQMELGGK DACIVLEDAD LDLVSANIVK GGFSYSGQRC
     TAVKVVLIME SIADAVVQKV NAKLAKLKVG PPEDDSDITP VVTESSANFI EGLVMDAKEK
     GATFCQEYRR EGNLIWPLLL DHVRPDMRIA WEEPFGPVLP VIRINSVEEG IHHCNASNFG
     LQGCIFTRDI NKAILISDAM ETGTVQINSA PARGPDHFSF QGLKDSGIGS QGITNSINMM
     TKVKSTVINL PSPSYTMG