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P61880 (G3P_PYRWO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glyceraldehyde-3-phosphate dehydrogenase

Short name=GAPDH
EC=1.2.1.59
Alternative name(s):
NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase
Gene names
Name:gap
Synonyms:gapDH
OrganismPyrococcus woesei
Taxonomic identifier2262 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length334 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Active in the presence of NAD and NADP. HAMAP MF_00559

Catalytic activity

D-glyceraldehyde 3-phosphate + phosphate + NAD(P)+ = 3-phospho-D-glyceroyl phosphate + NAD(P)H. HAMAP MF_00559

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5. HAMAP MF_00559

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm HAMAP MF_00559.

Sequence similarities

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Biophysicochemical properties

Temperature dependence:

Thermostable. Has a 44 minutes half-life at 100 degrees Celsius. HAMAP MF_00559

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandNAD
NADP
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNAD binding

Inferred from electronic annotation. Source: InterPro

NADP binding

Inferred from electronic annotation. Source: InterPro

glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 334334Glyceraldehyde-3-phosphate dehydrogenase HAMAP MF_00559
PRO_0000145733

Regions

Nucleotide binding12 – 132NAD By similarity
Region140 – 1423Glyceraldehyde 3-phosphate binding By similarity
Region192 – 1932Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1411Nucleophile By similarity
Binding site1111NAD; via amide nitrogen By similarity
Binding site1671NAD By similarity
Binding site2981NAD; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
P61880 [UniParc].

Last modified June 7, 2004. Version 1.
Checksum: 224E0626923AFC66

FASTA33437,436
        10         20         30         40         50         60 
MKIKVGINGY GTIGKRVAYA VTKQDDMELI GVTKTKPDFE AYRAKELGIP VYAASEEFLP 

        70         80         90        100        110        120 
RFEKAGFEVE GTLNDLLEKV DIIVDATPGG MGEKNKQLYE KAGVKAIFQG GEKAEVAQVS 

       130        140        150        160        170        180 
FVAQANYEAA LGKDYVRVVS CNTTGLVRTL NAIKDYVDYV YAVMIRRAAD PNDIKRGPIN 

       190        200        210        220        230        240 
AIKPSVTIPS HHGPDVQTVI PINIETSAFV VPTTIMHVHS IMVELKKPLT REDVIDIFEN 

       250        260        270        280        290        300 
TTRVLLFEKE KGFESTAQLI EFARDLHREW NNLYEIAVWK ESINVKGNRL FYIQAVHQES 

       310        320        330 
DVIPENIDAI RAMFEIAEKW ESIKKTNKSL GILK 

« Hide

References

[1]"Glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaebacterium Pyrococcus woesei: characterization of the enzyme, cloning and sequencing of the gene, and expression in Escherichia coli."
Zwickl P., Fabry S., Bogedain C., Haas A., Hensel R.
J. Bacteriol. 172:4329-4338(1990) [PubMed: 2165475] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-14, CHARACTERIZATION.
Strain: DSM 3773.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M83988 Genomic DNA. Translation: AAA73180.1.
PIRDEQYG. S10653.

3D structure databases

ProteinModelPortalP61880.
SMRP61880. Positions 1-334.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

HAMAPMF_00559. G3P_dehdrog_arch.
[Tree]
InterProIPR020831. GlycerAld/Erythrose_P_DH.
IPR020830. GlycerAld_3-P_DH_AS.
IPR020829. GlycerAld_3-P_DH_cat.
IPR020828. GlycerAld_3-P_DH_NAD(P)-bd.
IPR006436. Glyceraldehyde-3-P_DH_2_arc.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PfamPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PIRSFPIRSF000149. GAP_DH. 1 hit.
SMARTSM00846. Gp_dh_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR01546. GAPDH-II_archae. 1 hit.
PROSITEPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameG3P_PYRWO
AccessionPrimary (citable) accession number: P61880
Secondary accession number(s): P20286
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: June 28, 2011
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families