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Reviewed, UniProtKB/Swiss-Prot P07487 (G3P2_DROME)

Last modified June 16, 2009. Version 91. 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 · Binary interactions · 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
ORF Names: CG8893
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length332 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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
   Coding sequence diversityPolymorphism
   LigandNAD
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processglycolysis

Inferred from expression pattern. Source: FlyBase

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentlipid particle

Inferred from direct assay. Source: FlyBase

   Molecular functionNAD or NADH binding

Inferred from electronic annotation. Source: InterPro

glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity

Inferred from direct assay. Source: FlyBase

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q9VRJ91EBI-110014,EBI-100603

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 332332Glyceraldehyde-3-phosphate dehydrogenase 2
PRO_0000145522

Regions

Nucleotide binding11 – 122NAD By similarity
Region148 – 1503Glyceraldehyde 3-phosphate binding By similarity
Region208 – 2092Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1491Nucleophile By similarity
Binding site321NAD By similarity
Binding site771NAD; via carbonyl oxygen By similarity
Binding site1791Glyceraldehyde 3-phosphate By similarity
Binding site2311Glyceraldehyde 3-phosphate By similarity
Binding site3131NAD By similarity
Site1761Activates thiol group during catalysis By similarity

Amino acid modifications

Modified residue2731Phosphotyrosine Ref.6
Modified residue2741Phosphothreonine Ref.6

Natural variations

Natural variant801A → V in strain: MA2. Ref.2

Experimental info

Sequence conflict381N → K in AAA28561. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P07487-1 [UniParc].

Last modified June 1, 2001. Version 2.
Checksum: 5D5D274B8D3B4839

FASTA33235,369
        10         20         30         40         50         60 
MSKIGINGFG RIGRLVLRAA IDKGANVVAV NDPFIDVNYM VYLFKFDSTH GRFKGTVAAE 

        70         80         90        100        110        120 
GGFLVVNGQK ITVFSERDPA NINWASAGAE YIVESTGVFT TIDKASTHLK GGAKKVIISA 

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

       190        200        210        220        230        240 
TQKTVDGPSG KLWRDGRGAA QNIIPASTGA AKAVGKVIPA LNGKLTGMAF RVPTPNVSVV 

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

       310        320        330 
NDKFVKLISW YDNEFGYSNR VIDLIKYMQS KD 

« Hide

References

« Hide 'large scale' references
[1]"Structure of two unlinked Drosophila melanogaster glyceraldehyde-3-phosphate dehydrogenase genes."
Tso J.Y., Sun X.-H., Wu R.
J. Biol. Chem. 260:8220-8228(1985) [PubMed: 2989282] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Adaptive evolution of metabolic pathways in Drosophila."
Flowers J., Sezgin E., Kumagai S., Duvernell D., Matzkin L., Schmidt P., Eanes W.
Mol. Biol. Evol. 24:1347-1354(2007) [PubMed: 17379620] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-80.
Strain: AF8, AF9, HFL1, HFL2, HFL3, HFL4, MA2, MA7, SC1, SC2, VT1, VT2, VT3, VT4, Zh23 and Zh33.
[3]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[4]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
[5]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Head.
[6]"An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
Mol. Biosyst. 3:275-286(2007) [PubMed: 17372656] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-273 AND THR-274, MASS SPECTROMETRY.

Cross-references

Sequence databases

M11255 Genomic DNA. Translation: AAA28561.1.
DQ864106 Genomic DNA. Translation: ABH06741.1.
DQ864107 Genomic DNA. Translation: ABH06742.1.
DQ864108 Genomic DNA. Translation: ABH06743.1.
DQ864109 Genomic DNA. Translation: ABH06744.1.
DQ864110 Genomic DNA. Translation: ABH06745.1.
DQ864111 Genomic DNA. Translation: ABH06746.1.
DQ864112 Genomic DNA. Translation: ABH06747.1.
DQ864113 Genomic DNA. Translation: ABH06748.1.
DQ864114 Genomic DNA. Translation: ABH06749.1.
DQ864115 Genomic DNA. Translation: ABH06750.1.
DQ864116 Genomic DNA. Translation: ABH06751.1.
DQ864117 Genomic DNA. Translation: ABH06752.1.
DQ864118 Genomic DNA. Translation: ABH06753.1.
DQ864119 Genomic DNA. Translation: ABH06754.1.
DQ864120 Genomic DNA. Translation: ABH06755.1.
DQ864121 Genomic DNA. Translation: ABH06756.1.
AE014298 Genomic DNA. Translation: AAF48531.1.
AE014298 Genomic DNA. Translation: AAN09371.1.
AY094940 mRNA. Translation: AAM11293.1.
PIRB22366.
RefSeqNP_525091.1.
NP_542445.1.
UniGeneDm.6789

3D structure databases

HSSPHSSP built from PDB template 1CRW based on UniProtKB P56649.
SMRP07487. Positions 2-332.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:17969N.
IntActP07487. 17 interactions.

Proteomic databases

PRIDEP07487.

Genome annotation databases

EnsemblFBgn0001092. Drosophila melanogaster. [Contig view]
GeneID32545.
KEGGdme:Dmel_CG8893.

Organism-specific databases

FlyBaseFBgn0001092. Gapdh2.

Phylogenomic databases

HOGENOMP07487.
OMAP07487. YLIVANE.

Enzyme and pathway databases

BioCycDMEL-XXX-02:DMEL-XXX-02-002069-MON.
DMEL-XXX-02:DMEL-XXX-02-002070-MON.
BRENDA1.2.1.12. 48.

Gene expression databases

ArrayExpressP07487.
GermOnlineCG8893. Drosophila melanogaster.

Family and domain databases

InterProIPR000173. GlycerAld_3-P_DH.
IPR006424. Glyceraldehyde-3-P_DH_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...

Other Resources

NextBio779058.

Entry information

Entry nameG3P2_DROME
AccessionPrimary (citable) accession number: P07487
Secondary accession number(s): A5XCW0, Q541C2, Q9VXM7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: June 1, 2001
Last modified: June 16, 2009
This is version 91 of the entry and version 2 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 · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents