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Reviewed, UniProtKB/Swiss-Prot O59494 (G3P_PYRHO)

Last modified November 25, 2008. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
      Short name=GAPDH
    EC=1.2.1.59
Alternative name(s):
    NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase
Gene names
Name: gap
Ordered Locus Names: PH1830
OrganismPyrococcus horikoshii [Complete proteome] [HAMAP]
Taxonomic identifier53953 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

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Protein attributes

Sequence length334 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

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

Pathway

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

Subunit structure

Homotetramer.

Subcellular location

CytoplasmBy similarity.

Sequence similarities

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 334334Glyceraldehyde-3-phosphate dehydrogenase
PRO_0000145731

Regions

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

Sites

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

Secondary structure

1 ................................................................ 334
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
O59494-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: AEA615734718E39B

FASTA33437,264
        10         20         30         40         50         60 
MKVKVGVNGY GTIGKRVAYA VTKQDDMELI GITKTKPDFE AYRAKELGIP VYAASEEFIP 

        70         80         90        100        110        120 
RFEKEGFEVA GTLNDLLEKV DIIVDATPGG IGAKNKPLYE KAGVKAIFQG GEKADVAEVS 

       130        140        150        160        170        180 
FVAQANYEAA LGKNYVRVVS CNTTGLVRTL SAIREYADYV YAVMIRRAAD PNDTKRGPIN 

       190        200        210        220        230        240 
AIKPTVEVPS HHGPDVQTVI PINIETMAFV VPTTLMHVHS VMVELKKPLT KDDVIDIFEN 

       250        260        270        280        290        300 
TTRVLLFEKE KGFDSTAQII EFARDLHREW NNLYEIAVWK ESINIKGNRL FYIQAVHQES 

       310        320        330 
DVIPENIDAI RAMFELADKW DSIKKTNKSL GILK

« Hide

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References

« Hide 'large scale' references
[1]"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3."
Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T. expand/collapse author list , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.
DNA Res. 5:55-76(1998) [PubMed: 9679194] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OT3.
[2]"Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from Pyrococcus horikoshii ot3."
RIKEN structural genomics initiative (RSGI)
Submitted (JAN-2006) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH NAD, SUBUNIT.

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Cross-references

Sequence databases

BA000001 Genomic DNA. Translation: BAA30950.1.
PIRG71194.
RefSeqNP_143662.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2CZCX-ray2.00A/B/C/D1-334[»]
ModBaseSearch...

Genome annotation databases

GeneID1442672.
GenomeReviewsGene locus PH1830 in contig BA000001_GR.
KEGGpho:PH1830.
NMPDRfig|70601.1.peg.1786.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMO59494.

Family and domain databases

HAMAPMF_00559.
[Tree]
InterProIPR000173. GlycerAld_3-P_DHase.
IPR006436. Glyceraldehyde-3-P_DHase_2_arc.
[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.
ProDomPD007761. GAPDH_like. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01546. GAPDH-II_archae. 1 hit.
PROSITEPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameG3P_PYRHO
AccessionPrimary (citable) accession number: O59494
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: November 25, 2008
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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