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Reviewed, UniProtKB/Swiss-Prot P19866 (G3PA_SPIOL)

Last modified June 16, 2009. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Glyceraldehyde-3-phosphate dehydrogenase A, chloroplastic
    EC=1.2.1.13
Alternative name(s):
    NADP-dependent glyceraldehydephosphate dehydrogenase subunit A
Gene names
Name: GAPA
Synonyms: GPA1
OrganismSpinacia oleracea (Spinach)
Taxonomic identifier3562 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Amaranthaceae › Spinacia

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Protein attributes

Sequence length401 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

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

Pathway

Carbohydrate biosynthesis; Calvin cycle.

Subunit structure

Tetramer of either four A chains (GAPDH 2) or two A and two B chains (GAPDH 1). Ref.3 Ref.4

Subcellular location

Plastid › chloroplast.

Miscellaneous

Plants contain three forms of GAPDH: a cytosolic form which participates in glycolysis and two chloroplast forms which participates in photosynthesis. These three forms are encoded by distinct genes.

Sequence similarities

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6565Chloroplast Ref.2
Chain66 – 401336Glyceraldehyde-3-phosphate dehydrogenase A, chloroplastic
PRO_0000010425

Regions

Nucleotide binding76 – 772NADP
Region217 – 2193Glyceraldehyde 3-phosphate binding By similarity
Region276 – 2772Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site2181Nucleophile
Binding site1001NADP
Binding site1451NADP; via carbonyl oxygen
Binding site2481Glyceraldehyde 3-phosphate By similarity
Binding site2631Glyceraldehyde 3-phosphate By similarity
Binding site2991Glyceraldehyde 3-phosphate By similarity
Binding site3811NADP
Site2451Activates thiol group during catalysis By similarity

Experimental info

Mutagenesis1011T → A: Reduced affinity for NADP, and slight increase of the affinity for NAD. Ref.4
Mutagenesis2571S → A: Reduced affinity for NADP, and slight increase of the affinity for NAD. Ref.4
Sequence conflict2881N → Q AA sequence Ref.2
Sequence conflict4011Q → QA AA sequence Ref.2

Secondary structure

1 ....................................................................... 401
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P19866-1 [UniParc].

Last modified May 2, 2002. Version 2.
Checksum: 2A815842EA095A84

FASTA40143,023
        10         20         30         40         50         60 
MASNMLSIAN PSLRVYNKGF SEFSGLHTSS LPFGRKGSDD LMAFVSFQTN AVGGKRSSQN 

        70         80         90        100        110        120 
GVVEAKLKVA INGFGRIGRN FLRCWHGRKD SPLDVVVIND TGGVKQASHL LKYDSILGTF 

       130        140        150        160        170        180 
DADVKTAGDS AISVDGKVIK VVSDRNPVNL PWGDMGIDLV IEGTGVFVDR DGAGKHLQAG 

       190        200        210        220        230        240 
AKKVLITAPG KGDIPTYVVG VNEEGYTHAD TIISNASCTT NCLAPFVKVL DQKFGIIKGT 

       250        260        270        280        290        300 
MTTTHSYTGD QRLLDASHRD LRRARAACLN IVPTSTGAAK AVALVLPNLK GKLNGIALRV 

       310        320        330        340        350        360 
PTPNVSVVDL VVQVSKKTFA EEVNAAFRES ADNELKGILS VCDEPLVSID FRCTDVSSTI 

       370        380        390        400 
DSSLTMVMGD DMVKVIAWYD NEWGYSQRVV DLADIVANKW Q

« Hide

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References

[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: 8980499] [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: 2223845] [Abstract]
Cited for: PROTEIN SEQUENCE OF 66-401.
[3]"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: 12705826] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 66-401 IN COMPLEX WITH NAD, SUBUNIT.
[4]"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: 15236965] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 66-401 IN COMPLEX WITH NADP, MUTAGENESIS OF THR-101 AND SER-257, SUBUNIT.
+Additional computationally mapped references.

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Cross-references

Sequence databases

L76552 mRNA. Translation: AAD10217.1.
PIRT09012.

3D structure databases

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[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.2.1.13. 286.

Family and domain databases

InterProIPR000173. GlycerAld_3-P_DH.
IPR006424. Glyceraldehyde-3-P_DH_1.
[Graphical view]
PANTHERPTHR10836. GAP_DH. 1 hit.
PfamPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PIRSFPIRSF000149. GAP_DH. 1 hit.
PRINTSPR00078. G3PDHDRGNASE.
TIGRFAMsTIGR01534. GAPDH-I. 1 hit.
PROSITEPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameG3PA_SPIOL
AccessionPrimary (citable) accession number: P19866
Secondary accession number(s): O20249
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: May 2, 2002
Last modified: June 16, 2009
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents