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P56649 (G3P_PANVR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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=1.2.1.12
OrganismPanulirus versicolor (Spiny blue lobster) (Palinurus versicolor)
Taxonomic identifier150436 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Ecdysozoa › Arthropoda › Crustacea › Malacostraca › Eumalacostraca › Eucarida › Decapoda › Pleocyemata › Achelata › Palinuroidea › Palinuridae › Panulirus

Protein attributes

Sequence length333 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   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+) (phosphorylating) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 333333Glyceraldehyde-3-phosphate dehydrogenase
PRO_0000145506

Regions

Nucleotide binding10 – 112NAD
Region147 – 1493Glyceraldehyde 3-phosphate binding By similarity
Region207 – 2082Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1481Nucleophile
Binding site311NAD
Binding site761NAD; via carbonyl oxygen By similarity
Binding site1781Glyceraldehyde 3-phosphate By similarity
Binding site2301Glyceraldehyde 3-phosphate By similarity
Binding site3121NAD
Site1751Activates thiol group during catalysis

Amino acid modifications

Modified residue11N-acetylserine

Secondary structure

1 ............................................................................ 333
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P56649 [UniParc].

Last modified July 15, 1999. Version 1.
Checksum: 818572106E294C19

FASTA33335,724
        10         20         30         40         50         60 
SKIGINGFGR IGRLVLRAAL EMGAQVVAVN DPFIALEYMV YMFKYDSTHG MFKGEVKAED 

        70         80         90        100        110        120 
GALVVDGKKI TVFNEMKPEN IPWSKAGAEY IVESTGVFTT IEKASAHFKG GAKKVIISAP 

       130        140        150        160        170        180 
SADAPMFVCG VNLEKYSKDM KVVSNASCTT NCLAPVAKVL HENFEIVEGL MTTVHAVTAT 

       190        200        210        220        230        240 
QKTVDGPSAK DWRGGRGAAQ NIIPSSTGAA KAVGKVIPEL DGKLTGMAFR VPTPNVSVVD 

       250        260        270        280        290        300 
LTVRLGKECS YDDIKAAMKA ASEGPLQGVL GYTEDDVVSC DFTGDNRSSI FDAKAGIQLS 

       310        320        330 
KTFVKVVSWY DNEFGYSQRV IDLIKHMQKV DSA

« Hide

References

[1]"Structure of D-glyceraldehyde-3-phosphate dehydrogenase from Palinurus versicolor carrying the fluorescent NAD derivatives at 2.7-A resolution."
Lin Z.J., Li J., Zhang F.M., Song S.Y., Yang J., Liang S.J., Tsou C.L.
Arch. Biochem. Biophys. 302:161-166(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
[2]"Structure of holo-glyceraldehyde-3-phosphate dehydrogenase from Palinurus versicolor refined at 2-A resolution."
Song S.Y., Li J., Lin Z.J.
Acta Crystallogr. D 54:558-569(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) IN COMPLEX WITH NAD.
Tissue: Muscle.
+Additional computationally mapped references.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CRWX-ray2.00G/R1-333[»]
1DSSX-ray1.88G/R1-333[»]
1IHXX-ray2.80A/B/C/D1-333[»]
1IHYX-ray3.00A/B/C/D1-333[»]
1SZJX-ray2.00G/R1-333[»]
ProteinModelPortalP56649.
SMRP56649. Positions 1-333.
ModBaseSearch...

Proteomic databases

PRIDEP56649.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP56649.
UniPathwayUPA00109; UER00184.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
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.
IPR006424. Glyceraldehyde-3-P_DH_1.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR10836. PTHR10836. 1 hit.
PfamPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PIRSFPIRSF000149. GAP_DH. 1 hit.
PRINTSPR00078. G3PDHDRGNASE.
SMARTSM00846. Gp_dh_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR01534. GAPDH-I. 1 hit.
PROSITEPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP56649.

Entry information

Entry nameG3P_PANVR
AccessionPrimary (citable) accession number: P56649
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 15, 1999
Last modified: April 3, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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

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