Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot O44105 (G3P2_DROSU)

Last modified November 25, 2008. Version 46. 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

Names and origin

Protein namesRecommended name:
    Glyceraldehyde-3-phosphate dehydrogenase 2
    EC=1.2.1.12
Alternative name(s):
    Glyceraldehyde-3-phosphate dehydrogenase II
      Short name=GAPDH II
Gene names
Name: Gapdh2
OrganismDrosophila subobscura (Fruit fly)
Taxonomic identifier7241 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length304 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript 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

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-KW

   Molecular functionNAD binding

Inferred from electronic annotation. Source: InterPro

glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›304›304Glyceraldehyde-3-phosphate dehydrogenase 2
PRO_0000145525

Regions

Nucleotide binding1 – 22NAD By similarity
Region138 – 1403Glyceraldehyde 3-phosphate binding By similarity
Region198 – 1992Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1391Nucleophile By similarity
Binding site221NAD By similarity
Binding site671NAD; via carbonyl oxygen By similarity
Binding site1691Glyceraldehyde 3-phosphate By similarity
Binding site2211Glyceraldehyde 3-phosphate By similarity
Binding site3031NAD By similarity
Site1661Activates thiol group during catalysis By similarity

Experimental info

Non-terminal residue11
Non-terminal residue3041

Sequences

Sequence LengthMass (Da)Tools
O44105-1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 9BE9C70576089D1C

FASTA30432,176
        10         20         30         40         50         60 
RIGRLVLRAA IDKGASVVAV NDPFIDVNYM VYLFKFDSTH GRFKGTVVAE GGFLVVNGQK 

        70         80         90        100        110        120 
ITVFSERDPA NINWASAGAE YVVESTGVFT TIEKASTHLK GGAKKVVISA PSADAPMFVC 

       130        140        150        160        170        180 
GVNLDAYKPD MKVVSNASCT TNCLAPLAKV INDNFEIVEG LMTTVHATTA TQKTVDGPSG 

       190        200        210        220        230        240 
KLWRDGRGAA QNIIPAATGA AKAVGKVIPA LNGKLTGMAF RVPTPNVSVV DLTVRLGKGA 

       250        260        270        280        290        300 
SYDEIKAKVQ EAANGPLKGI LGYTDEEVVS TDFLSDTHSS VFDAKAGISL NDKFVKLISW 


YDNE 

« Hide

References

[1]"The molecular clock revisited: the rate of synonymous vs. replacement change in Drosophila."
Zeng L.-W., Comeron J.M., Chen B., Kreitman M.
Genetica 102:369-382(1998) [PubMed: 9720289] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

AF025810 mRNA. Translation: AAB87895.1.

3D structure databases

HSSPHSSP built from PDB template 1DSS based on UniProtKB P56649.
SMRO44105. Positions 1-304.
ModBaseSearch...

Organism-specific databases

FlyBaseFBgn0012937. Dsub\Gapdh2.

Family and domain databases

InterProIPR000173. GlycerAld_3-P_DHase.
IPR006424. Glyceraldehyde-3-P_DHase_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...

Entry information

Entry nameG3P2_DROSU
AccessionPrimary (citable) accession number: O44105
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: June 1, 1998
Last modified: November 25, 2008
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

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