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Protein

Glyceraldehyde-3-phosphate dehydrogenase A, chloroplastic

Gene

GAPA

Organism
Spinacia oleracea (Spinach)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

D-glyceraldehyde 3-phosphate + phosphate + NADP+ = 3-phospho-D-glyceroyl phosphate + NADPH.

Pathwayi: Calvin cycle

This protein is involved in the pathway Calvin cycle, which is part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the pathway Calvin cycle and in Carbohydrate biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei100 – 1001NADP4 Publications
Binding sitei145 – 1451NADP; via carbonyl oxygen4 Publications
Active sitei218 – 2181Nucleophile
Sitei245 – 2451Activates thiol group during catalysisBy similarity
Binding sitei248 – 2481Glyceraldehyde 3-phosphateBy similarity
Binding sitei263 – 2631Glyceraldehyde 3-phosphateBy similarity
Binding sitei299 – 2991Glyceraldehyde 3-phosphateBy similarity
Binding sitei381 – 3811NADP4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi76 – 772NADP4 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Calvin cycle

Keywords - Ligandi

NADP

Enzyme and pathway databases

BRENDAi1.2.1.13. 5812.
SABIO-RKP19866.
UniPathwayiUPA00116.

Names & Taxonomyi

Protein namesi
Recommended name:
Glyceraldehyde-3-phosphate dehydrogenase A, chloroplastic (EC:1.2.1.13)
Alternative name(s):
NADP-dependent glyceraldehydephosphate dehydrogenase subunit A
Gene namesi
Name:GAPA
Synonyms:GPA1
OrganismiSpinacia oleracea (Spinach)
Taxonomic identifieri3562 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesChenopodiaceaeChenopodioideaeAnserineaeSpinacia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi101 – 1011T → A: Reduced affinity for NADP, and slight increase of the affinity for NAD. 1 Publication
Mutagenesisi257 – 2571S → A: Reduced affinity for NADP, and slight increase of the affinity for NAD. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6565Chloroplast1 PublicationAdd
BLAST
Chaini66 – 401336Glyceraldehyde-3-phosphate dehydrogenase A, chloroplasticPRO_0000010425Add
BLAST

Proteomic databases

PRIDEiP19866.

Interactioni

Subunit structurei

Tetramer of either four A chains (GAPDH 2) or two A and two B chains (GAPDH 1).4 Publications

Protein-protein interaction databases

DIPiDIP-60959N.

Structurei

Secondary structure

1
401
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi67 – 726Combined sources
Helixi76 – 8611Combined sources
Beta strandi88 – 903Combined sources
Beta strandi92 – 998Combined sources
Helixi104 – 1129Combined sources
Turni115 – 1173Combined sources
Beta strandi124 – 1263Combined sources
Beta strandi130 – 1345Combined sources
Beta strandi137 – 1426Combined sources
Helixi147 – 1493Combined sources
Helixi152 – 1554Combined sources
Beta strandi159 – 1624Combined sources
Beta strandi164 – 1663Combined sources
Helixi170 – 1789Combined sources
Beta strandi182 – 1887Combined sources
Beta strandi191 – 1933Combined sources
Turni199 – 2013Combined sources
Helixi203 – 2053Combined sources
Beta strandi211 – 2144Combined sources
Helixi218 – 23417Combined sources
Beta strandi236 – 24611Combined sources
Beta strandi253 – 2553Combined sources
Turni261 – 2644Combined sources
Turni267 – 2693Combined sources
Beta strandi272 – 2743Combined sources
Helixi278 – 2858Combined sources
Helixi287 – 2893Combined sources
Turni290 – 2923Combined sources
Beta strandi293 – 3019Combined sources
Beta strandi306 – 31611Combined sources
Helixi320 – 33112Combined sources
Turni332 – 3387Combined sources
Beta strandi339 – 3424Combined sources
Helixi348 – 3514Combined sources
Beta strandi356 – 3616Combined sources
Helixi362 – 3643Combined sources
Beta strandi366 – 3683Combined sources
Turni369 – 3713Combined sources
Beta strandi372 – 3798Combined sources
Helixi383 – 39816Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JN0X-ray3.00A/B/O66-401[»]
1NBOX-ray2.60A/B/O66-401[»]
1RM3X-ray2.20A/B/O66-401[»]
1RM4X-ray2.00A/B/O66-401[»]
1RM5X-ray2.10A/B/O66-401[»]
2HKIX-ray3.00A66-401[»]
2PKQX-ray3.60P/R/S66-401[»]
2PKRX-ray2.40A/B/C/D/H/I/L/M/O/P/Q/R66-401[»]
ProteinModelPortaliP19866.
SMRiP19866. Positions 66-401.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19866.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni217 – 2193Glyceraldehyde 3-phosphate bindingBy similarity
Regioni276 – 2772Glyceraldehyde 3-phosphate bindingBy similarity

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR020831. GlycerAld/Erythrose_P_DH.
IPR020830. GlycerAld_3-P_DH_AS.
IPR020829. GlycerAld_3-P_DH_cat.
IPR020828. GlycerAld_3-P_DH_NAD(P)-bd.
IPR006424. Glyceraldehyde-3-P_DH_1.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR10836. PTHR10836. 1 hit.
PfamiPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000149. GAP_DH. 1 hit.
PRINTSiPR00078. G3PDHDRGNASE.
SMARTiSM00846. Gp_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01534. GAPDH-I. 1 hit.
PROSITEiPS00071. GAPDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P19866-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASNMLSIAN PSLRVYNKGF SEFSGLHTSS LPFGRKGSDD LMAFVSFQTN
60 70 80 90 100
AVGGKRSSQN GVVEAKLKVA INGFGRIGRN FLRCWHGRKD SPLDVVVIND
110 120 130 140 150
TGGVKQASHL LKYDSILGTF DADVKTAGDS AISVDGKVIK VVSDRNPVNL
160 170 180 190 200
PWGDMGIDLV IEGTGVFVDR DGAGKHLQAG AKKVLITAPG KGDIPTYVVG
210 220 230 240 250
VNEEGYTHAD TIISNASCTT NCLAPFVKVL DQKFGIIKGT MTTTHSYTGD
260 270 280 290 300
QRLLDASHRD LRRARAACLN IVPTSTGAAK AVALVLPNLK GKLNGIALRV
310 320 330 340 350
PTPNVSVVDL VVQVSKKTFA EEVNAAFRES ADNELKGILS VCDEPLVSID
360 370 380 390 400
FRCTDVSSTI DSSLTMVMGD DMVKVIAWYD NEWGYSQRVV DLADIVANKW

Q
Length:401
Mass (Da):43,023
Last modified:May 2, 2002 - v2
Checksum:i2A815842EA095A84
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti288 – 2881N → Q AA sequence (PubMed:2223845).Curated
Sequence conflicti401 – 4011Q → QA AA sequence (PubMed:2223845).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L76552 mRNA. Translation: AAD10217.1.
PIRiT09012.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L76552 mRNA. Translation: AAD10217.1.
PIRiT09012.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JN0X-ray3.00A/B/O66-401[»]
1NBOX-ray2.60A/B/O66-401[»]
1RM3X-ray2.20A/B/O66-401[»]
1RM4X-ray2.00A/B/O66-401[»]
1RM5X-ray2.10A/B/O66-401[»]
2HKIX-ray3.00A66-401[»]
2PKQX-ray3.60P/R/S66-401[»]
2PKRX-ray2.40A/B/C/D/H/I/L/M/O/P/Q/R66-401[»]
ProteinModelPortaliP19866.
SMRiP19866. Positions 66-401.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60959N.

Proteomic databases

PRIDEiP19866.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00116.
BRENDAi1.2.1.13. 5812.
SABIO-RKP19866.

Miscellaneous databases

EvolutionaryTraceiP19866.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR020831. GlycerAld/Erythrose_P_DH.
IPR020830. GlycerAld_3-P_DH_AS.
IPR020829. GlycerAld_3-P_DH_cat.
IPR020828. GlycerAld_3-P_DH_NAD(P)-bd.
IPR006424. Glyceraldehyde-3-P_DH_1.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR10836. PTHR10836. 1 hit.
PfamiPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000149. GAP_DH. 1 hit.
PRINTSiPR00078. G3PDHDRGNASE.
SMARTiSM00846. Gp_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01534. GAPDH-I. 1 hit.
PROSITEiPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Functional studies of chloroplast glyceraldehyde-3-phosphate dehydrogenase subunits A and B expressed in Escherichia coli: formation of highly active A4 and B4 homotetramers and evidence that aggregation of the B4 complex is mediated by the B subunit carboxy terminus."
    Baalmann E., Scheibe R., Cerff R., Martin W.
    Plant Mol. Biol. 32:505-513(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Chloroplast glyceraldehyde-3-phosphate dehydrogenase (NADP): amino acid sequence of the subunits from isoenzyme I and structural relationship with isoenzyme II."
    Ferri G., Stoppini M., Meloni M.L., Zapponi M.C., Iadarola P.
    Biochim. Biophys. Acta 1041:36-42(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 66-401.
  3. "Crystal structure of the non-regulatory A(4) isoform of spinach chloroplast glyceraldehyde-3-phosphate dehydrogenase complexed with NADP."
    Fermani S., Ripamonti A., Sabatino P., Zanotti G., Scagliarini S., Sparla F., Trost P., Pupillo P.
    J. Mol. Biol. 314:527-542(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 66-401 IN COMPLEX WITH NADP, SUBUNIT.
  4. "Dual coenzyme specificity of photosynthetic glyceraldehyde-3-phosphate dehydrogenase interpreted by the crystal structure of A4 isoform complexed with NAD."
    Falini G., Fermani S., Ripamonti A., Sabatino P., Sparla F., Pupillo P., Trost P.
    Biochemistry 42:4631-4639(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 66-401 IN COMPLEX WITH NAD, SUBUNIT.
  5. "Coenzyme site-directed mutants of photosynthetic A4-GAPDH show selectively reduced NADPH-dependent catalysis, similar to regulatory AB-GAPDH inhibited by oxidized thioredoxin."
    Sparla F., Fermani S., Falini G., Zaffagnini M., Ripamonti A., Sabatino P., Pupillo P., Trost P.
    J. Mol. Biol. 340:1025-1037(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 66-401 IN COMPLEX WITH NADP, MUTAGENESIS OF THR-101 AND SER-257, SUBUNIT.
  6. "Crystallization and structural analysis of GADPH from Spinacia oleracea in a new form."
    Camara-Artigas A., Hirasawa M., Knaff D.B., Wang M., Allen J.P.
    Acta Crystallogr. F 62:1087-1092(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 66-401.
  7. "Molecular mechanism of thioredoxin regulation in photosynthetic A2B2-glyceraldehyde-3-phosphate dehydrogenase."
    Fermani S., Sparla F., Falini G., Martelli P.L., Casadio R., Pupillo P., Ripamonti A., Trost P.
    Proc. Natl. Acad. Sci. U.S.A. 104:11109-11114(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 66-401 IN COMPLEX WITH NADP, SUBUNIT.

Entry informationi

Entry nameiG3PA_SPIOL
AccessioniPrimary (citable) accession number: P19866
Secondary accession number(s): O20249
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: May 2, 2002
Last modified: July 6, 2016
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Plants contain two types of GAPDH: cytosolic forms which participate in glycolysis and chloroplast forms which participate in photosynthesis. All the forms are encoded by distinct genes.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.