P07486 (G3P1_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	332 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Glycolysis
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glycolysis Inferred from expression pattern PubMed 3149711. Source: FlyBase
Cellular_component	M 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_function	NAD 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 332	332	Glyceraldehyde-3-phosphate dehydrogenase 1		PRO_0000145521
Regions
	Nucleotide binding	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
Sites
	Active site	149	1	Nucleophile By similarity
	Binding site	32	1	NAD By similarity
	Binding site	77	1	NAD; via carbonyl oxygen By similarity
	Binding site	179	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	231	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	313	1	NAD By similarity
	Site	176	1	Activates thiol group during catalysis By similarity
Natural variations
	Natural variant	284	1	F → L in strain: HFL23, HFL5, VT10, VT6 and HFL2. Ref.1 Ref.2
	Natural variant	284	1	F → V in strain: VT37, HFL15 and HFL3. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P07486 [UniParc]. Last modified June 21, 2005. Version 2. Checksum: 3FB529173DFC6E42	FASTA	332	35,350
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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.
PIR	A22366.
RefSeq	NP_001033936.1. NM_001038847.1. NP_525108.2. NM_080369.2.
UniGene	Dm.23224.
3D structure databases
ProteinModelPortal	P07486.
SMR	P07486. Positions 2-332.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-1572825.
STRING	7227.FBpp0087977.
Proteomic databases
PaxDb	P07486.
PRIDE	P07486.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0088903; FBpp0087977; FBgn0001091. FBtr0100479; FBpp0099914; FBgn0001091.
GeneID	35728.
KEGG	dme:Dmel_CG12055.
Organism-specific databases
CTD	35728.
FlyBase	FBgn0001091. Gapdh1.
Phylogenomic databases
eggNOG	COG0057.
GeneTree	ENSGT00690000101860.
InParanoid	P07486.
KO	K00134.
OMA	AKIHLES.
OrthoDB	EOG4QRFKR.
PhylomeDB	P07486.
Enzyme and pathway databases
UniPathway	UPA00109; UER00184.
Gene expression databases
Bgee	P07486.
GermOnline	CG12055. Drosophila melanogaster.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
InterPro	IPR020831. 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]
PANTHER	PTHR10836. PTHR10836. 1 hit.
Pfam	PF02800. Gp_dh_C. 1 hit. PF00044. Gp_dh_N. 1 hit. [Graphical view]
PIRSF	PIRSF000149. GAP_DH. 1 hit.
PRINTS	PR00078. G3PDHDRGNASE.
SMART	SM00846. Gp_dh_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR01534. GAPDH-I. 1 hit.
PROSITE	PS00071. GAPDH. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	35728.
NextBio	794917.

Entry information

Entry name

G3P1_DROME

Accession

Primary (citable) accession number: P07486
Secondary accession number(s): A4UZ75 , 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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project