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   16-JUN-2009, entry version 53.
DE   RecName: Full=NADP-dependent glyceraldehyde-3-phosphate dehydrogenase;
DE            EC=1.2.1.9;
DE   AltName: Full=Non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase;
DE   AltName: Full=Glyceraldehyde-3-phosphate dehydrogenase [NADP+];
DE   AltName: Full=Triosephosphate dehydrogenase;
GN   Name=GPN1;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae;
OC   PACCAD clade; Panicoideae; Andropogoneae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. KW5330; TISSUE=Shoot;
RX   MEDLINE=94180387; 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
RT   aldehyde dehydrogenase superfamily with no sequence homology to
RT   phosphorylating GAPDH.";
RL   J. Mol. Biol. 237:165-171(1994).
CC   -!- FUNCTION: Important as a means of generating NADPH for
CC       biosynthetic reactions.
CC   -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + NADP(+) + H(2)O
CC       = 3-phospho-D-glycerate + NADPH.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
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DR   EMBL; X75326; CAA53075.1; -; mRNA.
DR   PIR; S43833; S43833.
DR   RefSeq; NP_001105589.1; -.
DR   UniGene; Zm.175; -.
DR   HSSP; Q59931; 1EUH.
DR   GeneID; 542583; -.
DR   Gramene; Q43272; -.
DR   MaizeGDB; 78926; -.
DR   BRENDA; 1.2.1.9; 289.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008886; F:glyceraldehyde-3-phosphate dehydrogenase (N...; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR016160; Ald_DH_CS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH.
DR   Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
DR   PANTHER; PTHR11699; Aldehyde_dehyd; 1.
DR   Pfam; PF00171; Aldedh; 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    498       NADP-dependent glyceraldehyde-3-phosphate
FT                                dehydrogenase.
FT                                /FTId=PRO_0000056576.
FT   NP_BIND     247    251       NAD (By similarity).
FT   REGION      171    172       Substrate binding (By similarity).
FT   REGION      299    301       Substrate binding (By similarity).
FT   ACT_SITE    266    266       Proton acceptor (By similarity).
FT   ACT_SITE    300    300       Nucleophile (By similarity).
FT   BINDING     118    118       Substrate (By similarity).
FT   BINDING     194    194       NADP (By similarity).
FT   BINDING     197    197       NADP (By similarity).
FT   BINDING     232    232       NADP (By similarity).
FT   BINDING     393    393       NADP (By similarity).
FT   BINDING     453    453       Substrate (By similarity).
FT   SITE        171    171       Transition state stabilizer (By
FT                                similarity).
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
//