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Reviewed, UniProtKB/Swiss-Prot P26519 (G3PC_PETCR)

Last modified June 16, 2009. Version 59. 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
Synonyms: GAPDH
OrganismPetroselinum crispum (Parsley) (Petroselinum hortense)
Taxonomic identifier4043 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › campanulids › Apiales › Apiaceae › Apioideae › apioid superclade › Apium clade › Petroselinum

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Protein attributes

Sequence length336 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-SubCell

   Molecular functionNAD or NADH binding

Inferred from electronic annotation. Source: InterPro

glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 336336Glyceraldehyde-3-phosphate dehydrogenase, cytosolic
PRO_0000145611

Regions

Nucleotide binding12 – 132NAD By similarity
Region152 – 1543Glyceraldehyde 3-phosphate binding By similarity
Region212 – 2132Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1531Nucleophile By similarity
Binding site341NAD By similarity
Binding site811NAD; via carbonyl oxygen By similarity
Binding site1831Glyceraldehyde 3-phosphate By similarity
Binding site2351Glyceraldehyde 3-phosphate By similarity
Binding site3171NAD By similarity
Site1801Activates thiol group during catalysis By similarity

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Sequences

Sequence LengthMass (Da)Tools
P26519-1 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 9CD52A143AFA2494

FASTA33636,372
        10         20         30         40         50         60 
MKMKIGINGF GRIGRLVARV ALMSDDIELV AVNDPFITTE YMTYMFKYDS VHGQWKKDEL 

        70         80         90        100        110        120 
KVKDSKTLLF GDKPLTVFGV RNPEEDPWGE AGAEYVVEST GVFTDKDKAA AHLKGGAKKV 

       130        140        150        160        170        180 
VISAPSGNAP MFVVGVNEKE YKKDIDIVSN ASCTTNCLAP LAKVLNDKFG IVEGLMTTVH 

       190        200        210        220        230        240 
SITATRKTVD GPSMKDWRGG RAASFNIIPS STGAAKAVGK VLPALNGKLT GMAFRVPTVD 

       250        260        270        280        290        300 
VSVVDLTARL EKAATYDEIK AAIKHESETS LKGILGYTED DVVSTDFVGD SRSSIFDAKA 

       310        320        330 
GIALNGNFVK VVSWYDNEWG YSNRVIDLIR HMASVA

« Hide

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References

[1]"Molecular evidence for pre-Cretaceous angiosperm origins."
Martin W., Gierl A., Saedler H.
Nature 339:46-48(1989)
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

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Cross-references

Sequence databases

X60344 mRNA. Translation: CAA42902.1.
PIRDEPZG. S18484.

3D structure databases

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

Enzyme and pathway databases

BRENDA1.2.1.12. 2662.

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 nameG3PC_PETCR
AccessionPrimary (citable) accession number: P26519
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: June 16, 2009
This is version 59 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