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Reviewed, UniProtKB/Swiss-Prot P50362 (G3PA_CHLRE)

Last modified November 25, 2008. Version 71. 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

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
OrganismChlamydomonas reinhardtii
Taxonomic identifier3055 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas

Protein attributes

Sequence length374 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

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

Pathway

Carbohydrate biosynthesis; Calvin cycle.

Subunit structure

Homotetramer. Component of a complex that contains two dimers of PRK, two tetramers of GAPDH and CP12. CP12 associates with GAPDH, causing its conformation to change. This GAPDH/CP12 complex binds PRK to form a half-complex (one unit). This unit probably dimerizes due partially to interactions between the enzymes of each unit.

Subcellular location

Plastidchloroplast.

Miscellaneous

GAPDHB, the second subunit found in plants, is absent in algae.

Algae contain three forms of GAPDH: two cytosolic forms which participate in glycolysis and one chloroplastic form which participates in photosynthesis. These three forms are encoded by distinct genes.

Sequence similarities

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3434Chloroplast By similarity
Chain35 – 374340Glyceraldehyde-3-phosphate dehydrogenase A, chloroplastic
PRO_0000010418

Regions

Nucleotide binding47 – 482NADP By similarity
Region189 – 1913Glyceraldehyde 3-phosphate binding By similarity
Region248 – 2492Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1901Nucleophile By similarity
Binding site711NADP By similarity
Binding site1161NADP; via carbonyl oxygen By similarity
Binding site2201Glyceraldehyde 3-phosphate By similarity
Binding site2351Glyceraldehyde 3-phosphate By similarity
Binding site2711Glyceraldehyde 3-phosphate By similarity
Binding site3531NADP By similarity
Site2171Activates thiol group during catalysis By similarity

Amino acid modifications

Disulfide bond55 ↔ 325 By similarity

Secondary structure

................................................................. 374
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P50362-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 8CEB02897930D34C

FASTA37440,304
        10         20         30         40         50         60 
MAAMMQKSAF TGSAVSSKSG VRAKAARAVV DVRAEKKIRV AINGFGRIGR NFLRCWHGRQ 

        70         80         90        100        110        120 
NTLLDVVAIN DSGGVKQASH LLKYDSTLGT FAADVKIVDD SHISVDGKQI KIVSSRDPLQ 

       130        140        150        160        170        180 
LPWKEMNIDL VIEGTGVFID KVGAGKHIQA GASKVLITAP AKDKDIPTFV VGVNEGDYKH 

       190        200        210        220        230        240 
EYPIISNASC TTNCLAPFVK VLEQKFGIVK GTMTTTHSYT GDQRLLDASH RDLRRARAAA 

       250        260        270        280        290        300 
LNIVPTTTGA AKAVSLVLPS LKGKLNGIAL RVPTPTVSVV DLVVQVEKKT FAEEVNAAFR 

       310        320        330        340        350        360 
EAANGPMKGV LHVEDAPLVS IDFKCTDQST SIDASLTMVM GDDMVKVVAW YDNEWGYSQR 

       370 
VVDLAEVTAK KWVA 

« Hide

References

[1]"Five identical intron positions in ancient duplicated genes of eubacterial origin."
Kersanach R., Brinkmann H., Liaud M.-F., Zhang D.-X., Martin W., Cerff R.
Nature 367:387-389(1994) [PubMed: 8114942] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 1132.
[2]"The small protein CP12: a protein linker for supramolecular complex assembly."
Graciet E., Gans P., Wedel N., Lebreton S., Camadro J.-M., Gontero B.
Biochemistry 42:8163-8170(2003) [PubMed: 12846565] [Abstract]
Cited for: SUBUNIT, INTERACTION WITH CP12.
[3]"Characterization of native and recombinant A4 glyceraldehyde 3-phosphate dehydrogenase. Kinetic evidence for conformation changes upon association with the small protein CP12."
Graciet E., Lebreton S., Camadro J.-M., Gontero B.
Eur. J. Biochem. 270:129-136(2003) [PubMed: 12492483] [Abstract]
Cited for: INTERACTION WITH CP12.
[4]"Chlamydomonas reinhardtii NADP-linked glyceraldehyde-3-phosphate dehydrogenase contains the cysteine residues identified as potentially domain-locking in the higher plant enzyme and is light activated."
Li A.D., Stevens F.J., Huppe H.C., Kersanach R., Anderson L.E.
Photosyn. Res. 51:167-177(1997)
Cited for: 3D-STRUCTURE MODELING OF 35-374.

Cross-references

Sequence databases

L27668 Genomic DNA. Translation: AAA86855.1.
PIRT07990.
RefSeqXP_001689871.1.
UniGeneCre.2829

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1NLGmodel-A35-374[»]
1NLHmodel-A35-374[»]
SMRP50362. Positions 37-372.
ModBaseSearch...

Genome annotation databases

GeneID5715019.
KEGGcre:CHLREDRAFT_129019.

Family and domain databases

InterProIPR000173. GlycerAld_3-P_DHase.
IPR006424. Glyceraldehyde-3-P_DHase_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...

Entry information

Entry nameG3PA_CHLRE
AccessionPrimary (citable) accession number: P50362
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 25, 2008
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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