Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glyceraldehyde-3-phosphate dehydrogenase 2

Gene

Gapdh2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH.PROSITE-ProRule annotation

Pathwayi: glycolysis

This protein is involved in step 1 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase 1 (Gapdh1), Glyceraldehyde-3-phosphate dehydrogenase 2 (Gapdh2), Glyceraldehyde-3-phosphate dehydrogenase (Gapdh2), Glyceraldehyde-3-phosphate dehydrogenase (CG9010)
  2. Phosphoglycerate kinase (Pgk)
  3. no protein annotated in this organism
  4. Enolase (Eno)
  5. Pyruvate kinase (CG7069), Pyruvate kinase (CG7069), Pyruvate kinase (CG7362), Pyruvate kinase (PyK), Pyruvate kinase (CG2964), Pyruvate kinase (CG2964)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei32 – 321NADBy similarity
Binding sitei77 – 771NAD; via carbonyl oxygenBy similarity
Active sitei149 – 1491NucleophilePROSITE-ProRule annotation
Sitei176 – 1761Activates thiol group during catalysisBy similarity
Binding sitei179 – 1791Glyceraldehyde 3-phosphateBy similarity
Binding sitei231 – 2311Glyceraldehyde 3-phosphateBy similarity
Binding sitei313 – 3131NADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 122NADBy similarity

GO - Molecular functioni

GO - Biological processi

  • glucose metabolic process Source: InterPro
  • glycolytic process Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

NAD

Enzyme and pathway databases

ReactomeiR-DME-70171. Glycolysis.
R-DME-70263. Gluconeogenesis.
UniPathwayiUPA00109; UER00184.

Names & Taxonomyi

Protein namesi
Recommended name:
Glyceraldehyde-3-phosphate dehydrogenase 2 (EC:1.2.1.12)
Alternative name(s):
Glyceraldehyde-3-phosphate dehydrogenase II
Short name:
GAPDH II
Gene namesi
Name:Gapdh2
ORF Names:CG8893
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0001092. Gapdh2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: FlyBase
  • lipid particle Source: FlyBase
  • microtubule associated complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 332332Glyceraldehyde-3-phosphate dehydrogenase 2PRO_0000145522Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei273 – 2731Phosphotyrosine1 Publication
Modified residuei274 – 2741Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP07487.
PRIDEiP07487.

PTM databases

iPTMnetiP07487.

Expressioni

Gene expression databases

BgeeiP07487.
ExpressionAtlasiP07487. differential.
GenevisibleiP07487. DM.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi58893. 33 interactions.
DIPiDIP-17969N.
IntActiP07487. 2 interactions.
MINTiMINT-934462.
STRINGi7227.FBpp0073922.

Structurei

3D structure databases

ProteinModelPortaliP07487.
SMRiP07487. Positions 2-332.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni148 – 1503Glyceraldehyde 3-phosphate bindingBy similarity
Regioni208 – 2092Glyceraldehyde 3-phosphate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0657. Eukaryota.
COG0057. LUCA.
GeneTreeiENSGT00760000119172.
InParanoidiP07487.
KOiK00134.
OMAiSTDFIHD.
OrthoDBiEOG7Q5HDF.
PhylomeDBiP07487.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR020831. 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]
PANTHERiPTHR10836. PTHR10836. 1 hit.
PfamiPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000149. GAP_DH. 1 hit.
PRINTSiPR00078. G3PDHDRGNASE.
SMARTiSM00846. Gp_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01534. GAPDH-I. 1 hit.
PROSITEiPS00071. GAPDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P07487-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKIGINGFG RIGRLVLRAA IDKGANVVAV NDPFIDVNYM VYLFKFDSTH
60 70 80 90 100
GRFKGTVAAE GGFLVVNGQK ITVFSERDPA NINWASAGAE YIVESTGVFT
110 120 130 140 150
TIDKASTHLK GGAKKVIISA PSADAPMFVC GVNLDAYKPD MKVVSNASCT
160 170 180 190 200
TNCLAPLAKV INDNFEIVEG LMTTVHATTA TQKTVDGPSG KLWRDGRGAA
210 220 230 240 250
QNIIPASTGA AKAVGKVIPA LNGKLTGMAF RVPTPNVSVV DLTVRLGKGA
260 270 280 290 300
SYDEIKAKVQ EAANGPLKGI LGYTDEEVVS TDFLSDTHSS VFDAKAGISL
310 320 330
NDKFVKLISW YDNEFGYSNR VIDLIKYMQS KD
Length:332
Mass (Da):35,369
Last modified:June 1, 2001 - v2
Checksum:i5D5D274B8D3B4839
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 381N → K in AAA28561 (PubMed:2989282).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti80 – 801A → V in strain: MA2. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
AY094940 mRNA. Translation: AAM11293.1.
PIRiB22366.
RefSeqiNP_001259584.1. NM_001272655.1.
NP_542445.1. NM_080714.4.
UniGeneiDm.6789.

Genome annotation databases

EnsemblMetazoaiFBtr0074112; FBpp0073922; FBgn0001092.
FBtr0332618; FBpp0304864; FBgn0001092.
GeneIDi32545.
KEGGidme:Dmel_CG8893.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
AY094940 mRNA. Translation: AAM11293.1.
PIRiB22366.
RefSeqiNP_001259584.1. NM_001272655.1.
NP_542445.1. NM_080714.4.
UniGeneiDm.6789.

3D structure databases

ProteinModelPortaliP07487.
SMRiP07487. Positions 2-332.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi58893. 33 interactions.
DIPiDIP-17969N.
IntActiP07487. 2 interactions.
MINTiMINT-934462.
STRINGi7227.FBpp0073922.

PTM databases

iPTMnetiP07487.

Proteomic databases

PaxDbiP07487.
PRIDEiP07487.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0074112; FBpp0073922; FBgn0001092.
FBtr0332618; FBpp0304864; FBgn0001092.
GeneIDi32545.
KEGGidme:Dmel_CG8893.

Organism-specific databases

CTDi32545.
FlyBaseiFBgn0001092. Gapdh2.

Phylogenomic databases

eggNOGiKOG0657. Eukaryota.
COG0057. LUCA.
GeneTreeiENSGT00760000119172.
InParanoidiP07487.
KOiK00134.
OMAiSTDFIHD.
OrthoDBiEOG7Q5HDF.
PhylomeDBiP07487.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00184.
ReactomeiR-DME-70171. Glycolysis.
R-DME-70263. Gluconeogenesis.

Miscellaneous databases

ChiTaRSiGapdh2. fly.
GenomeRNAii32545.
NextBioi779058.
PROiP07487.

Gene expression databases

BgeeiP07487.
ExpressionAtlasiP07487. differential.
GenevisibleiP07487. DM.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR020831. 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]
PANTHERiPTHR10836. PTHR10836. 1 hit.
PfamiPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000149. GAP_DH. 1 hit.
PRINTSiPR00078. G3PDHDRGNASE.
SMARTiSM00846. Gp_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01534. GAPDH-I. 1 hit.
PROSITEiPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. 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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. 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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-273 AND THR-274, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiG3P2_DROME
AccessioniPrimary (citable) accession number: P07487
Secondary accession number(s): A5XCW0, Q541C2, Q9VXM7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: June 1, 2001
Last modified: May 11, 2016
This is version 158 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.