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Reviewed, UniProtKB/Swiss-Prot P34924 (G3PC_PINSY)

Last modified June 16, 2009. Version 58. 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
OrganismPinus sylvestris (Scots pine)
Taxonomic identifier3349 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Coniferopsida › Coniferales › Pinaceae › Pinus › Pinus

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Protein attributes

Sequence length340 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 – 340340Glyceraldehyde-3-phosphate dehydrogenase, cytosolic
PRO_0000145614

Regions

Nucleotide binding16 – 172NAD By similarity
Region156 – 1583Glyceraldehyde 3-phosphate binding By similarity
Region216 – 2172Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1571Nucleophile By similarity
Binding site381NAD By similarity
Binding site851NAD; via carbonyl oxygen By similarity
Binding site1871Glyceraldehyde 3-phosphate By similarity
Binding site2391Glyceraldehyde 3-phosphate By similarity
Binding site3211NAD By similarity
Site1841Activates thiol group during catalysis By similarity

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Sequences

Sequence LengthMass (Da)Tools
P34924-1 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 1E81ACA460086F01

FASTA34036,530
        10         20         30         40         50         60 
MGSTGKIKIG INGFGRIGRL VARVALTRDD IELVGVNDPF ISTDYMSYMF KYDSVHGKWK 

        70         80         90        100        110        120 
HHEVNVKDSK TLLFGEKSVA VFGCRNPEEI PWGEVGAEYV VESTGVFTDK EKASAHLKAG 

       130        140        150        160        170        180 
AKKVVISAPS KDAPMFVVGV NEHQYKSDVN IVSNASCTTN CLAPLAKVIN DKFGIVEGLM 

       190        200        210        220        230        240 
TTVHSITATQ KTVDGPSNKD WRGGRGAGFN IIPSSTGAAK AVGKVLPALN GKLTGMAFRV 

       250        260        270        280        290        300 
PTPDVSVVDL TVRLEKSATY DEIKAAIKAE SEGNLKGILG YTEDAVVSTD FIGDSRSSIF 

       310        320        330        340 
DAQAGIALSD NFVKLVSWYD NEWGYSSRVV DLIVHMAATQ

« Hide

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References

[1]"Molecular phylogenies in angiosperm evolution."
Martin W., Lydiate D., Brinkmann H., Forkmann G., Saedler H., Cerff R.
Mol. Biol. Evol. 10:140-162(1993) [PubMed: 8095691] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

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Cross-references

Sequence databases

L07501 mRNA. Translation: AAA33779.1.
PIRT09663.

3D structure databases

HSSPHSSP built from PDB template 4GPD based on UniProtKB P00357.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.2.1.12. 1355.

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.
ProDomPD007761. GAPDH_like. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01534. GAPDH-I. 1 hit.
PROSITEPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameG3PC_PINSY
AccessionPrimary (citable) accession number: P34924
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: June 16, 2009
This is version 58 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