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P07486 (G3P1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 120. 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

Names and origin

Protein namesRecommended name:
Glyceraldehyde-3-phosphate dehydrogenase 1

EC=1.2.1.12
Alternative name(s):
Glyceraldehyde-3-phosphate dehydrogenase I
Short name=GAPDH I
Gene names
Name:Gapdh1
Synonyms:Gadph-1
ORF Names:CG12055
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length332 AA.
Sequence statusComplete.
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.

Developmental stage

Expressed during adult stages. Ref.1

Sequence similarities

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from expression pattern PubMed 3149711. Source: FlyBase

   Cellular_componentM band

Inferred from direct assay PubMed 12756285. Source: FlyBase

Z disc

Inferred from direct assay PubMed 12756285. Source: FlyBase

lipid particle

Inferred from direct assay PubMed 16979555. Source: FlyBase

   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 direct assay PubMed 3149711. Source: FlyBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 332332Glyceraldehyde-3-phosphate dehydrogenase 1
PRO_0000145521

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

Natural variations

Natural variant2841F → L in strain: HFL23, HFL5, VT10, VT6 and HFL2. Ref.1 Ref.2
Natural variant2841F → V in strain: VT37, HFL15 and HFL3. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P07486 [UniParc].

Last modified June 21, 2005. Version 2.
Checksum: 3FB529173DFC6E42

FASTA33235,350
        10         20         30         40         50         60 
MSKIGINGFG RIGRLVLRAA IDKGASVVAV NDPFIDVNYM VYLFKFDSTH GRFKGTVAAE 

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

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

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

       250        260        270        280        290        300 
DLTVRLGKGA TYDEIKAKVE EASKGPLKGI LGYTDEEVVS TDFFSDTHSS 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE, VARIANT LEU-284.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-284 AND VAL-284.
Strain: HFL15, HFL2, HFL23, HFL3, HFL5, VT1, VT10, VT11, VT37, VT44, VT6 and VT9.
[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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[6]Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. expand/collapse author list , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M11254 Genomic DNA. Translation: AAA28560.1.
DQ864083 Genomic DNA. Translation: ABH06718.1.
DQ864084 Genomic DNA. Translation: ABH06719.1.
DQ864085 Genomic DNA. Translation: ABH06720.1.
DQ864086 Genomic DNA. Translation: ABH06721.1.
DQ864087 Genomic DNA. Translation: ABH06722.1.
DQ864088 Genomic DNA. Translation: ABH06723.1.
DQ864089 Genomic DNA. Translation: ABH06724.1.
DQ864090 Genomic DNA. Translation: ABH06725.1.
DQ864091 Genomic DNA. Translation: ABH06726.1.
DQ864092 Genomic DNA. Translation: ABH06727.1.
DQ864093 Genomic DNA. Translation: ABH06728.1.
DQ864094 Genomic DNA. Translation: ABH06729.1.
AE013599 Genomic DNA. Translation: AAF59192.2.
AE013599 Genomic DNA. Translation: ABC66066.1.
AY089643 mRNA. Translation: AAL90381.1.
BT004485 mRNA. Translation: AAO42649.1.
PIRA22366.
RefSeqNP_001033936.1. NM_001038847.1.
NP_525108.2. NM_080369.2.
UniGeneDm.23224.

3D structure databases

ProteinModelPortalP07486.
SMRP07486. Positions 2-332.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-1572825.
STRING7227.FBpp0087977.

Proteomic databases

PaxDbP07486.
PRIDEP07486.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0088903; FBpp0087977; FBgn0001091.
FBtr0100479; FBpp0099914; FBgn0001091.
GeneID35728.
KEGGdme:Dmel_CG12055.

Organism-specific databases

CTD35728.
FlyBaseFBgn0001091. Gapdh1.

Phylogenomic databases

eggNOGCOG0057.
GeneTreeENSGT00690000101860.
InParanoidP07486.
KOK00134.
OMAAKIHLES.
OrthoDBEOG4QRFKR.
PhylomeDBP07486.

Enzyme and pathway databases

UniPathwayUPA00109; UER00184.

Gene expression databases

BgeeP07486.
GermOnlineCG12055. Drosophila melanogaster.

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

GenomeRNAi35728.
NextBio794917.

Entry information

Entry nameG3P1_DROME
AccessionPrimary (citable) accession number: P07486
Secondary accession number(s): A4UZ75 expand/collapse secondary AC list , A5XCT3, A5XCT7, Q8SXG8, Q9V318
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: June 21, 2005
Last modified: April 3, 2013
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila 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