Skip Header

Contribute Send feedback
Read comments (?) or add your own

O59494 (G3P_PYRHO) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
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
Ordered Locus Names:PH1830
OrganismPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]
Taxonomic identifier70601 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

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

General annotation (Comments)

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. Ref.2

Subcellular location

Cytoplasm By similarity HAMAP MF_00559.

Sequence similarities

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandNAD
NADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
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_0000145731

Regions

Nucleotide binding12 – 132NAD HAMAP MF_00559
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...

Sequences

Sequence LengthMass (Da)Tools
O59494 [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

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: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000001 Genomic DNA. Translation: BAA30950.1.
PIRG71194.
RefSeqNP_143662.1. NC_000961.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CZCX-ray2.00A/B/C/D1-334[»]
ProteinModelPortalO59494.
SMRO59494. Positions 1-334.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBPYRT00000001355; EBPYRP00000001355; EBPYRG00000001355.
GeneID1442672.
GenomeReviewsGene locus PH1830 in contig BA000001_GR.
KEGGpho:PH1830.
NMPDRfig|70601.1.peg.1786.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000022490.
HOGENOMHBG392099.
OMAVPSHHGP.
ProtClustDBPRK04207.

Enzyme and pathway databases

BioCycPHOR70601:PH1830-MONOMER.

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.
KOK00150.
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_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 16, 2011
This is version 89 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents