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UniProtKB/Swiss-Prot entry P07486


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name G3P1_DROME
Primary accession number P07486
Secondary accession numbers A4UZ75 A5XCT3 A5XCT7 Q8SXG8 Q9V318
Integrated into Swiss-Prot on April 1, 1988
Sequence was last modified on June 21, 2005 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 80)
Name and origin of the protein
Protein name Glyceraldehyde-3-phosphate dehydrogenase 1
Synonyms EC 1.2.1.12
Glyceraldehyde-3-phosphate dehydrogenase I
GAPDH I
Gene name
Name: Gapdh1
Synonyms: Gadph-1
ORFNames: CG12055
From
Drosophila melanogaster (Fruit fly) [TaxID: 7227] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE, AND VARIANT LEU-284.
PubMed=2989282 [NCBI, ExPASy, EBI, Israel, Japan]
Tso J.Y., Sun X.-H., Wu R.;
"Structure of two unlinked Drosophila melanogaster glyceraldehyde-3-phosphate dehydrogenase genes.";
J. Biol. Chem. 260:8220-8228(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-284 AND VAL-284.
STRAIN=HFL15, HFL2, HFL23, HFL3, HFL5, VT1, VT10, VT11, VT37, VT44, VT6, and VT9;
DOI=10.1093/molbev/msm057; PubMed=17379620 [NCBI, ExPASy, EBI, Israel, Japan]
Flowers J., Sezgin E., Kumagai S., Duvernell D., Matzkin L., Schmidt P., Eanes W.;
"Adaptive evolution of metabolic pathways in Drosophila.";
Mol. Biol. Evol. 24:1347-1354(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
DOI=10.1126/science.287.5461.2185; PubMed=10731132 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION.
PubMed=12537572 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley;
TISSUE=Embryo;
PubMed=12537569 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley;
TISSUE=Embryo;
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., 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.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M11254; AAA28560.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ864083; ABH06718.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ864084; ABH06719.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ864085; ABH06720.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ864086; ABH06721.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ864087; ABH06722.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ864088; ABH06723.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ864089; ABH06724.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ864090; ABH06725.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ864091; ABH06726.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ864092; ABH06727.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ864093; ABH06728.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ864094; ABH06729.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE013599; AAF59192.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE013599; ABC66066.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY089643; AAL90381.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT004485; AAO42649.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A22366; A22366.
RefSeq NP_001033936.1; -.
NP_525108.2; -.
UniGene Dm.23224
3D structure databases
HSSP P56649; 1DSS. [HSSP ENTRY / PDB]
SMR P07486; 2-332.
ModBase P07486.
Protein-protein interaction databases
IntAct P07486; -.
Organism-specific databases
FlyBase FBgn0001091; Gapdh1.
Gene expression databases
ArrayExpress P07486; -.
GermOnline CG12055; Drosophila melanogaster.
Ontologies
GO
GO:0005811; Cellular component: lipid particle (inferred from direct assay from FlyBase).
GO:0004365; Molecular function: glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity (inferred from direct assay from FlyBase).
GO:0006096; Biological process: glycolysis (inferred from expression pattern from FlyBase).
QuickGo view.
Family and domain databases
InterPro IPR000173; GlycerAld_3-P_DHase.
IPR006424; Glyceraldehyde-3-P_DHase_1.
Graphical view of domain structure.
PANTHER PTHR10836; GAP_DH; 1.
Pfam PF02800; Gp_dh_C; 1.
PF00044; Gp_dh_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000149; GAP_DH; 1.
PRINTS PR00078; G3PDHDRGNASE.
TIGRFAMs TIGR01534; GAPDH-I; 1.
PROSITE PS00071; GAPDH; 1.
BLOCKS P07486.
ProtoNet P07486.
Genome annotation databases
Ensembl CG12055; Drosophila melanogaster. [Contig view]
GeneID 35728; -.
KEGG dme:Dmel_CG12055; -.
NMPDR fig|7227.3.peg.3729; -.
Phylogenomic databases
HOGENOM P07486; -.
Other
NextBio 794917; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Glycolysis; NAD; Oxidoreductase; Polymorphism.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   332  332     Glyceraldehyde-3-phosphate dehydrogenase 1. PRO_0000145521
NP_BIND   11    12  2     NAD (By similarity). 
REGION   148   150  3     Glyceraldehyde 3-phosphate binding (By similarity). 
REGION   208   209  2     Glyceraldehyde 3-phosphate binding (By similarity). 
ACT_SITE   149   149        Nucleophile (By similarity). 
BINDING   32    32        NAD (By similarity). 
BINDING   77    77        NAD; via carbonyl oxygen (By similarity). 
BINDING   179   179        Glyceraldehyde 3-phosphate (By similarity). 
BINDING   231   231        Glyceraldehyde 3-phosphate (By similarity). 
BINDING   313   313        NAD (By similarity). 
SITE   176   176  1     Activates thiol group during catalysis (By similarity). 
VARIANT   284   284  1     F -> L (in strain: HFL23, HFL5, VT10, VT6 and HFL2). 
VARIANT   284   284  1     F -> V (in strain: VT37, HFL15 and HFL3). 
Sequence information
Length: 332 AA [This is the length of the unprocessed precursor] Molecular weight: 35350 Da [This is the MW of the unprocessed precursor] CRC64: 3FB529173DFC6E42 [This is a checksum on the sequence]
        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 

P07486 in FASTA format

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