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Reviewed, UniProtKB/Swiss-Prot P32636 (G3P2_AGABI)

Last modified June 16, 2009. Version 57. 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 2
      Short name=GAPDH 2
    EC=1.2.1.12
Gene names
Name: gpd2
OrganismAgaricus bisporus (Common mushroom)
Taxonomic identifier5341 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Homobasidiomycetes › Agaricomycetidae › Agaricales › Agaricaceae › Agaricus

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Protein attributes

Sequence length338 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

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 – 338338Glyceraldehyde-3-phosphate dehydrogenase 2
PRO_0000145534

Regions

Nucleotide binding11 – 122NAD By similarity
Region149 – 1513Glyceraldehyde 3-phosphate binding By similarity
Region209 – 2102Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1501Nucleophile By similarity
Binding site331NAD By similarity
Binding site781NAD; via carbonyl oxygen By similarity
Binding site1801Glyceraldehyde 3-phosphate By similarity
Binding site2321Glyceraldehyde 3-phosphate By similarity
Binding site3141NAD By similarity
Site1771Activates thiol group during catalysis By similarity

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Sequences

Sequence LengthMass (Da)Tools
P32636-1 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 3381DBBF73B84469

FASTA33836,570
        10         20         30         40         50         60 
MVKVGINGFG RIGRIVLRNA LQFQDIEVVA VNDPFIDLEY MAYMFKYDSV HGRFKGTVEV 

        70         80         90        100        110        120 
KNGSFVVDGR PMKVFAERDP AAIPWGSVGA DYVVESTGVF TTIDKASAHL KGGAKKVVIS 

       130        140        150        160        170        180 
APSADAPMYV CGVNLDKYNP KDTIISNASC TTNCLATLAK VIHDNFGIVE GLMTTVHATT 

       190        200        210        220        230        240 
ATQKTVDGPS HKDWRGGRGV GNNIIPSSTG AAKAVGKVIP SLNGKLTGLS MRVPTQDVSV 

       250        260        270        280        290        300 
VDLVVRLEKP ASYEQIKEVM RKAAEGEYKG IIAYTDEDVV STDFISDNNS CVFDAKAGIQ 

       310        320        330 
LSPNFVKLIA WYDNEWGYSR RVCNLLQYVA KEDAKAGI

« Hide

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References

[1]"Sequence analysis of the glyceraldehyde-3-phosphate dehydrogenase genes from the basidiomycetes Schizophyllum commune, Phanerochaete chrysosporium and Agaricus bisporus."
Harmsen M.C., Schuren F.H.J., Moukha S.M., van Zuilen C.M., Punt P.J., Wessels J.G.H.
Curr. Genet. 22:447-454(1992) [PubMed: 1473176] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Horst U3.

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Cross-references

Sequence databases

M81728 Genomic DNA. Translation: AAA32634.1.
PIRS26976.

3D structure databases

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

Enzyme and pathway databases

BRENDA1.2.1.12. 984.

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 nameG3P2_AGABI
AccessionPrimary (citable) accession number: P32636
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 16, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal 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