G3PA_COEVA
ID G3PA_COEVA Reviewed; 314 AA.
AC Q8VXQ9;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase A, chloroplastic;
DE EC=1.2.1.13;
DE AltName: Full=NADP-dependent glyceraldehydephosphate dehydrogenase A;
DE Short=GAPDHA;
DE Flags: Fragment;
GN Name=GapA;
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 -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + NADP(+) + phosphate = (2R)-3-
CC phospho-glyceroyl phosphate + H(+) + NADPH; Xref=Rhea:RHEA:10296,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57604,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:59776; EC=1.2.1.13;
CC -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC -!- INDUCTION: Repressed by addition of D-galactose, D-mannose, D-glucose,
CC D-ribose or sucrose, but not by the addition of non-metabolizable sugar
CC analogs. {ECO:0000269|PubMed:15830207}.
CC -!- MISCELLANEOUS: GAPDHB, the second subunit found in plants, is absent in
CC algae.
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 glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AJ252208; CAC81011.1; -; mRNA.
DR AlphaFoldDB; Q8VXQ9; -.
DR SMR; Q8VXQ9; -.
DR PRIDE; Q8VXQ9; -.
DR UniPathway; UPA00116; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0047100; F:glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway.
DR InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43148; PTHR43148; 1.
DR Pfam; PF02800; Gp_dh_C; 1.
DR Pfam; PF00044; Gp_dh_N; 1.
DR PIRSF; PIRSF000149; GAP_DH; 1.
DR PRINTS; PR00078; G3PDHDRGNASE.
DR SMART; SM00846; Gp_dh_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR PROSITE; PS00071; GAPDH; 1.
PE 2: Evidence at transcript level;
KW Calvin cycle; Chloroplast; Disulfide bond; NADP; Oxidoreductase; Plastid.
FT CHAIN <1..>314
FT /note="Glyceraldehyde-3-phosphate dehydrogenase A,
FT chloroplastic"
FT /id="PRO_0000292345"
FT ACT_SITE 148
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 5..6
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 29
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 147..149
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 206..207
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 311
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 175
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250"
FT DISULFID 13..283
FT /evidence="ECO:0000250"
FT NON_TER 1
FT NON_TER 314
SQ SEQUENCE 314 AA; 33574 MW; F0F3CA15BDC4DB77 CRC64;
NGFGRIGRNF LRCLETRQNS LLEVIAINDS GGVKQASHLL KYDSTLGKFD ADVKIVDDGH
ISVNGKSIRV VSSRDPTKLP WGEMEIDLVI EGTGVFIDTP GASKHIEAGA KKVLITAPAK
GSDIPTYVVG VNAHDYKHSD AIISNASCTT NCLAPFVKVL DEKFGIVKGT MTNTHSYTGD
QRLLDASHRD LRRARAAALN IVPTTTGAAK AVALVLPKLK GKLNGIALRV PTPNVSVVDL
VVQVEKKTFA EEINNAFKEA AAGSLNGVLA VSDEPLVSVD FRCTDVSSTI DSSLTMVMGA
DMVKVVAWYD NEWG
