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Reviewed, UniProtKB/Swiss-Prot Q42671 (G3PC_CRAPL)

Last modified November 25, 2008. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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, cytosolic
    EC=1.2.1.12
Gene names
Name: GAPC
OrganismCraterostigma plantagineum
Taxonomic identifier4153 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Lamiales › Linderniaceae › Craterostigma

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Protein attributes

Sequence length337 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Catalytic activity

D-glyceraldehyde 3-phosphate + phosphate + NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH.

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm.

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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Ontologies

Keywords

   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase

Gene Ontology (GO)

   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionNAD binding

Inferred from electronic annotation. Source: InterPro

glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 337337Glyceraldehyde-3-phosphate dehydrogenase, cytosolic
PRO_0000145598

Regions

Nucleotide binding13 – 142NAD By similarity
Region153 – 1553Glyceraldehyde 3-phosphate binding By similarity
Region213 – 2142Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1541Nucleophile By similarity
Binding site351NAD By similarity
Binding site821NAD; via carbonyl oxygen By similarity
Binding site1841Glyceraldehyde 3-phosphate By similarity
Binding site2361Glyceraldehyde 3-phosphate By similarity
Binding site3181NAD By similarity
Site1811Activates thiol group during catalysis By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q42671-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: BF73D81E417580E5

FASTA33736,477
        10         20         30         40         50         60 
MAKVKIGING FGRIGRLVAR VALVRDDVEL VAVNDPFITV DYMAYMFKYD TVHGQYKHHE 

        70         80         90        100        110        120 
LKVKDEKTLL FGDKPVAVFG LRNPEEIPWA ETGAEYVVES TGVFTEKEKA AAHLKGGAKK 

       130        140        150        160        170        180 
VIISAPSKDA PMFVVGVNEK TYTPDIDVVS NASCTTNCLA PLAKVIHDRF GIVEGLMTTV 

       190        200        210        220        230        240 
HSITATQKTV DGPSSKDWRG GRAASFNIIP SSTGAAKAVG KVLPDLNGKL TGMAFRVPTV 

       250        260        270        280        290        300 
DVSVVDLTVT LAKEASYDEI KAAIKEESEG KLKGILGYTE EDVVSSDFVG DSRSSIFDAK 

       310        320        330 
AGIALSKKFV KIVAWYDNEW GYSSRVVDLI RHMAAAK

« Hide

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References

[1]"Dehydration and ABA increase mRNA levels and enzyme activity of cytosolic GAPDH in the resurrection plant Craterostigma plantagineum."
Velasco R., Salamini F., Bartels D.
Plant Mol. Biol. 26:541-546(1994) [PubMed: 7948905] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Leaf.

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Cross-references

Sequence databases

X78307 mRNA. Translation: CAA55116.1.
PIRS42479.

3D structure databases

HSSPHSSP built from PDB template 1IHX based on UniProtKB P56649.
ModBaseSearch...

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...

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Entry information

Entry nameG3PC_CRAPL
AccessionPrimary (citable) accession number: Q42671
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: November 25, 2008
This is version 53 of the entry and version 1 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

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