G3PA_SPIOL
ID G3PA_SPIOL Reviewed; 401 AA.
AC P19866; O20249;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase A, chloroplastic;
DE EC=1.2.1.13;
DE AltName: Full=NADP-dependent glyceraldehydephosphate dehydrogenase subunit A;
DE Flags: Precursor;
GN Name=GAPA; Synonyms=GPA1;
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8980499; DOI=10.1007/bf00019102;
RA Baalmann E., Scheibe R., Cerff R., Martin W.;
RT "Functional studies of chloroplast glyceraldehyde-3-phosphate dehydrogenase
RT subunits A and B expressed in Escherichia coli: formation of highly active
RT A4 and B4 homotetramers and evidence that aggregation of the B4 complex is
RT mediated by the B subunit carboxy terminus.";
RL Plant Mol. Biol. 32:505-513(1996).
RN [2]
RP PROTEIN SEQUENCE OF 66-401.
RX PubMed=2223845; DOI=10.1016/0167-4838(90)90119-z;
RA Ferri G., Stoppini M., Meloni M.L., Zapponi M.C., Iadarola P.;
RT "Chloroplast glyceraldehyde-3-phosphate dehydrogenase (NADP): amino acid
RT sequence of the subunits from isoenzyme I and structural relationship with
RT isoenzyme II.";
RL Biochim. Biophys. Acta 1041:36-42(1990).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 66-401 IN COMPLEX WITH NADP, AND
RP SUBUNIT.
RX PubMed=11846565; DOI=10.1006/jmbi.2001.5172;
RA Fermani S., Ripamonti A., Sabatino P., Zanotti G., Scagliarini S.,
RA Sparla F., Trost P., Pupillo P.;
RT "Crystal structure of the non-regulatory A(4) isoform of spinach
RT chloroplast glyceraldehyde-3-phosphate dehydrogenase complexed with NADP.";
RL J. Mol. Biol. 314:527-542(2001).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 66-401 IN COMPLEX WITH NAD, AND
RP SUBUNIT.
RX PubMed=12705826; DOI=10.1021/bi0272149;
RA Falini G., Fermani S., Ripamonti A., Sabatino P., Sparla F., Pupillo P.,
RA Trost P.;
RT "Dual coenzyme specificity of photosynthetic glyceraldehyde-3-phosphate
RT dehydrogenase interpreted by the crystal structure of A4 isoform complexed
RT with NAD.";
RL Biochemistry 42:4631-4639(2003).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 66-401 IN COMPLEX WITH NADP,
RP MUTAGENESIS OF THR-101 AND SER-257, AND SUBUNIT.
RX PubMed=15236965; DOI=10.1016/j.jmb.2004.06.005;
RA Sparla F., Fermani S., Falini G., Zaffagnini M., Ripamonti A., Sabatino P.,
RA Pupillo P., Trost P.;
RT "Coenzyme site-directed mutants of photosynthetic A4-GAPDH show selectively
RT reduced NADPH-dependent catalysis, similar to regulatory AB-GAPDH inhibited
RT by oxidized thioredoxin.";
RL J. Mol. Biol. 340:1025-1037(2004).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 66-401.
RX PubMed=17077485; DOI=10.1107/s174430910604200x;
RA Camara-Artigas A., Hirasawa M., Knaff D.B., Wang M., Allen J.P.;
RT "Crystallization and structural analysis of GADPH from Spinacia oleracea in
RT a new form.";
RL Acta Crystallogr. F 62:1087-1092(2006).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 66-401 IN COMPLEX WITH NADP, AND
RP SUBUNIT.
RX PubMed=17573533; DOI=10.1073/pnas.0611636104;
RA Fermani S., Sparla F., Falini G., Martelli P.L., Casadio R., Pupillo P.,
RA Ripamonti A., Trost P.;
RT "Molecular mechanism of thioredoxin regulation in photosynthetic A2B2-
RT glyceraldehyde-3-phosphate dehydrogenase.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:11109-11114(2007).
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: Tetramer of either four A chains (GAPDH 2) or two A and two B
CC chains (GAPDH 1). {ECO:0000269|PubMed:11846565,
CC ECO:0000269|PubMed:12705826, ECO:0000269|PubMed:15236965,
CC ECO:0000269|PubMed:17573533}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC -!- MISCELLANEOUS: Plants contain two types of GAPDH: cytosolic forms which
CC participate in glycolysis and chloroplast forms which participate in
CC photosynthesis. All the forms are encoded by distinct genes.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; L76552; AAD10217.1; -; mRNA.
DR PIR; T09012; T09012.
DR PDB; 1JN0; X-ray; 3.00 A; A/B/O=66-401.
DR PDB; 1NBO; X-ray; 2.60 A; A/B/O=66-401.
DR PDB; 1RM3; X-ray; 2.20 A; A/B/O=66-401.
DR PDB; 1RM4; X-ray; 2.00 A; A/B/O=66-401.
DR PDB; 1RM5; X-ray; 2.10 A; A/B/O=66-401.
DR PDB; 2HKI; X-ray; 3.00 A; A=66-401.
DR PDB; 2PKQ; X-ray; 3.60 A; P/R/S=66-401.
DR PDB; 2PKR; X-ray; 2.40 A; A/B/C/D/H/I/L/M/O/P/Q/R=66-401.
DR PDBsum; 1JN0; -.
DR PDBsum; 1NBO; -.
DR PDBsum; 1RM3; -.
DR PDBsum; 1RM4; -.
DR PDBsum; 1RM5; -.
DR PDBsum; 2HKI; -.
DR PDBsum; 2PKQ; -.
DR PDBsum; 2PKR; -.
DR AlphaFoldDB; P19866; -.
DR SMR; P19866; -.
DR DIP; DIP-60959N; -.
DR IntAct; P19866; 1.
DR PRIDE; P19866; -.
DR BRENDA; 1.2.1.12; 5812.
DR BRENDA; 1.2.1.13; 5812.
DR SABIO-RK; P19866; -.
DR UniPathway; UPA00116; -.
DR EvolutionaryTrace; P19866; -.
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 1: Evidence at protein level;
KW 3D-structure; Calvin cycle; Chloroplast; Direct protein sequencing; NADP;
KW Oxidoreductase; Plastid; Transit peptide.
FT TRANSIT 1..65
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:2223845"
FT CHAIN 66..401
FT /note="Glyceraldehyde-3-phosphate dehydrogenase A,
FT chloroplastic"
FT /id="PRO_0000010425"
FT ACT_SITE 218
FT /note="Nucleophile"
FT BINDING 76..77
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11846565,
FT ECO:0000269|PubMed:12705826, ECO:0000269|PubMed:15236965,
FT ECO:0000269|PubMed:17573533"
FT BINDING 100
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11846565,
FT ECO:0000269|PubMed:12705826, ECO:0000269|PubMed:15236965,
FT ECO:0000269|PubMed:17573533"
FT BINDING 145
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11846565,
FT ECO:0000269|PubMed:12705826, ECO:0000269|PubMed:15236965,
FT ECO:0000269|PubMed:17573533"
FT BINDING 217..219
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 276..277
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 381
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11846565,
FT ECO:0000269|PubMed:12705826, ECO:0000269|PubMed:15236965,
FT ECO:0000269|PubMed:17573533"
FT SITE 245
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250"
FT MUTAGEN 101
FT /note="T->A: Reduced affinity for NADP, and slight increase
FT of the affinity for NAD."
FT /evidence="ECO:0000269|PubMed:15236965"
FT MUTAGEN 257
FT /note="S->A: Reduced affinity for NADP, and slight increase
FT of the affinity for NAD."
FT /evidence="ECO:0000269|PubMed:15236965"
FT CONFLICT 288
FT /note="N -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="Q -> QA (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:1RM4"
FT HELIX 76..86
FT /evidence="ECO:0007829|PDB:1RM4"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:1RM3"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:1RM4"
FT HELIX 104..112
FT /evidence="ECO:0007829|PDB:1RM4"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:1RM4"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:1RM4"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:1RM4"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:1RM4"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:1RM4"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:1RM4"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:1RM4"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:1RM4"
FT HELIX 170..178
FT /evidence="ECO:0007829|PDB:1RM4"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:1RM4"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:1RM4"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:1RM4"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:1RM4"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:1RM4"
FT HELIX 218..234
FT /evidence="ECO:0007829|PDB:1RM4"
FT STRAND 236..246
FT /evidence="ECO:0007829|PDB:1RM4"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:1RM4"
FT TURN 261..264
FT /evidence="ECO:0007829|PDB:1RM4"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:1RM4"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:1RM4"
FT HELIX 278..285
FT /evidence="ECO:0007829|PDB:1RM4"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:1RM4"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:1RM4"
FT STRAND 293..301
FT /evidence="ECO:0007829|PDB:1RM4"
FT STRAND 306..316
FT /evidence="ECO:0007829|PDB:1RM4"
FT HELIX 320..331
FT /evidence="ECO:0007829|PDB:1RM4"
FT TURN 332..338
FT /evidence="ECO:0007829|PDB:1RM4"
FT STRAND 339..342
FT /evidence="ECO:0007829|PDB:1RM4"
FT HELIX 348..351
FT /evidence="ECO:0007829|PDB:1RM4"
FT STRAND 356..361
FT /evidence="ECO:0007829|PDB:1RM4"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:1RM4"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:1RM4"
FT TURN 369..371
FT /evidence="ECO:0007829|PDB:1RM4"
FT STRAND 372..379
FT /evidence="ECO:0007829|PDB:1RM4"
FT HELIX 383..398
FT /evidence="ECO:0007829|PDB:1RM4"
SQ SEQUENCE 401 AA; 43023 MW; 2A815842EA095A84 CRC64;
MASNMLSIAN PSLRVYNKGF SEFSGLHTSS LPFGRKGSDD LMAFVSFQTN AVGGKRSSQN
GVVEAKLKVA INGFGRIGRN FLRCWHGRKD SPLDVVVIND TGGVKQASHL LKYDSILGTF
DADVKTAGDS AISVDGKVIK VVSDRNPVNL PWGDMGIDLV IEGTGVFVDR DGAGKHLQAG
AKKVLITAPG KGDIPTYVVG VNEEGYTHAD TIISNASCTT NCLAPFVKVL DQKFGIIKGT
MTTTHSYTGD QRLLDASHRD LRRARAACLN IVPTSTGAAK AVALVLPNLK GKLNGIALRV
PTPNVSVVDL VVQVSKKTFA EEVNAAFRES ADNELKGILS VCDEPLVSID FRCTDVSSTI
DSSLTMVMGD DMVKVIAWYD NEWGYSQRVV DLADIVANKW Q
