ID   GAPN_COEVA              Reviewed;         233 AA.
AC   Q8VXQ7;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=NADP-dependent glyceraldehyde-3-phosphate dehydrogenase;
DE            EC=1.2.1.9;
DE   AltName: Full=Glyceraldehyde-3-phosphate dehydrogenase [NADP(+)];
DE            Short=GAPDHN;
DE   AltName: Full=Non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase;
DE   AltName: Full=Triosephosphate dehydrogenase;
DE   Flags: Fragment;
GN   Name=GapN;
OS   Coelastrella vacuolata (Green alga) (Chlorella fusca var. vacuolata).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Sphaeropleales; Scenedesmaceae; Scenedesmus.
OX   NCBI_TaxID=77546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC   STRAIN=SAG 211-8b;
RX   PubMed=15830207; DOI=10.1007/s00425-005-1501-0;
RA   Valverde F., Ortega J.M., Losada M., Serrano A.;
RT   "Sugar-mediated transcriptional regulation of the Gap gene system and
RT   concerted photosystem II functional modulation in the microalga Scenedesmus
RT   vacuolatus.";
RL   Planta 221:937-952(2005).
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   -!- INDUCTION: Induced by sugar addition. {ECO:0000269|PubMed:15830207}.
CC   -!- MISCELLANEOUS: Algae contain three forms of GAPDH: two cytosolic forms
CC       which participate in glycolysis and one chloroplastic form which
CC       participates in photosynthesis. These three forms are encoded by
CC       distinct genes.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ252211; CAC81014.1; -; mRNA.
DR   AlphaFoldDB; Q8VXQ7; -.
DR   SMR; Q8VXQ7; -.
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..>233
FT                   /note="NADP-dependent glyceraldehyde-3-phosphate
FT                   dehydrogenase"
FT                   /id="PRO_0000291764"
FT   ACT_SITE        102
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   ACT_SITE        136
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   BINDING         7..8
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         30
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         33
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         83..87
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         135..137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         180
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   BINDING         229
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   SITE            7
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         233
SQ   SEQUENCE   233 AA;  24436 MW;  F198D939BB96FD69 CRC64;
     LAIPPFNYPV NLAVSKLAPA LMAGNTVVLK PPSQGVVAGI HMIKCFQAAG LPAGTVNLVT
     GKGSEIGDFL TTHPAVNCIS FTGGDTGIAI SRKAGMVPLQ MELGGKDACI VCSDADLDLA
     ATHIIKGGFS YSGQRCTAVK VVLVMQDIAD ELVRKVHAGV QKLKVGRPED NADITAVVSE
     GSANFIQGLV EDAKAKGATF LTDWKREGNL LWPVLLDNVT ADMRIAWEEP FGP