G3P1_DROME
ID G3P1_DROME Reviewed; 332 AA.
AC P07486; A4UZ75; A5XCT3; A5XCT7; Q8SXG8; Q9V318;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 1;
DE EC=1.2.1.12;
DE AltName: Full=Glyceraldehyde-3-phosphate dehydrogenase I;
DE Short=GAPDH I;
GN Name=Gapdh1; Synonyms=Gadph-1; ORFNames=CG12055;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE, AND VARIANT
RP LEU-284.
RX PubMed=2989282; DOI=10.1016/s0021-9258(17)39584-4;
RA Tso J.Y., Sun X.-H., Wu R.;
RT "Structure of two unlinked Drosophila melanogaster glyceraldehyde-3-
RT phosphate dehydrogenase genes.";
RL J. Biol. Chem. 260:8220-8228(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-284 AND VAL-284.
RC STRAIN=HFL15, HFL2, HFL23, HFL3, HFL5, VT1, VT10, VT11, VT37, VT44, VT6,
RC and VT9;
RX PubMed=17379620; DOI=10.1093/molbev/msm057;
RA Flowers J., Sezgin E., Kumagai S., Duvernell D., Matzkin L., Schmidt P.,
RA Eanes W.;
RT "Adaptive evolution of metabolic pathways in Drosophila.";
RL Mol. Biol. Evol. 24:1347-1354(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-
CC phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10009};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DEVELOPMENTAL STAGE: Expressed during adult stages.
CC {ECO:0000269|PubMed:2989282}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; M11254; AAA28560.1; -; Genomic_DNA.
DR EMBL; DQ864083; ABH06718.1; -; Genomic_DNA.
DR EMBL; DQ864084; ABH06719.1; -; Genomic_DNA.
DR EMBL; DQ864085; ABH06720.1; -; Genomic_DNA.
DR EMBL; DQ864086; ABH06721.1; -; Genomic_DNA.
DR EMBL; DQ864087; ABH06722.1; -; Genomic_DNA.
DR EMBL; DQ864088; ABH06723.1; -; Genomic_DNA.
DR EMBL; DQ864089; ABH06724.1; -; Genomic_DNA.
DR EMBL; DQ864090; ABH06725.1; -; Genomic_DNA.
DR EMBL; DQ864091; ABH06726.1; -; Genomic_DNA.
DR EMBL; DQ864092; ABH06727.1; -; Genomic_DNA.
DR EMBL; DQ864093; ABH06728.1; -; Genomic_DNA.
DR EMBL; DQ864094; ABH06729.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF59192.2; -; Genomic_DNA.
DR EMBL; AE013599; ABC66066.1; -; Genomic_DNA.
DR EMBL; AY089643; AAL90381.1; -; mRNA.
DR EMBL; BT004485; AAO42649.1; -; mRNA.
DR PIR; A22366; A22366.
DR RefSeq; NP_001033936.1; NM_001038847.2.
DR RefSeq; NP_525108.2; NM_080369.3.
DR AlphaFoldDB; P07486; -.
DR SMR; P07486; -.
DR BioGRID; 61596; 21.
DR IntAct; P07486; 13.
DR STRING; 7227.FBpp0087977; -.
DR PaxDb; P07486; -.
DR PRIDE; P07486; -.
DR DNASU; 35728; -.
DR EnsemblMetazoa; FBtr0088903; FBpp0087977; FBgn0001091.
DR EnsemblMetazoa; FBtr0100479; FBpp0099914; FBgn0001091.
DR GeneID; 35728; -.
DR KEGG; dme:Dmel_CG12055; -.
DR CTD; 35728; -.
DR FlyBase; FBgn0001091; Gapdh1.
DR VEuPathDB; VectorBase:FBgn0001091; -.
DR eggNOG; KOG0657; Eukaryota.
DR GeneTree; ENSGT00940000153298; -.
DR HOGENOM; CLU_030140_0_3_1; -.
DR InParanoid; P07486; -.
DR OMA; HETYKGE; -.
DR OrthoDB; 945145at2759; -.
DR PhylomeDB; P07486; -.
DR UniPathway; UPA00109; UER00184.
DR BioGRID-ORCS; 35728; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 35728; -.
DR PRO; PR:P07486; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0001091; Expressed in oviduct (Drosophila) and 48 other tissues.
DR Genevisible; P07486; DM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0031430; C:M band; IDA:FlyBase.
DR GO; GO:0030018; C:Z disc; IDA:FlyBase.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IDA:FlyBase.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0035605; F:peptidyl-cysteine S-nitrosylase activity; ISS:FlyBase.
DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEP:FlyBase.
DR InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10836; PTHR10836; 1.
DR Pfam; PF02800; Gp_dh_C; 1.
DR Pfam; PF00044; Gp_dh_N; 1.
DR PIRSF; PIRSF000149; GAP_DH; 1.
DR PRINTS; PR00078; G3PDHDRGNASE.
DR SMART; SM00846; Gp_dh_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR PROSITE; PS00071; GAPDH; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Glycolysis; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..332
FT /note="Glyceraldehyde-3-phosphate dehydrogenase 1"
FT /id="PRO_0000145521"
FT ACT_SITE 149
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 11..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 32
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 148..150
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 208..209
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 313
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 176
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250"
FT VARIANT 284
FT /note="F -> L (in strain: HFL23, HFL5, VT10, VT6 and HFL2)"
FT /evidence="ECO:0000269|PubMed:17379620,
FT ECO:0000269|PubMed:2989282"
FT VARIANT 284
FT /note="F -> V (in strain: VT37, HFL15 and HFL3)"
FT /evidence="ECO:0000269|PubMed:17379620"
SQ SEQUENCE 332 AA; 35350 MW; 3FB529173DFC6E42 CRC64;
MSKIGINGFG RIGRLVLRAA IDKGASVVAV NDPFIDVNYM VYLFKFDSTH GRFKGTVAAE
GGFLVVNGQK ITVFSERDPA NINWASAGAE YVVESTGVFT TIDKASTHLK GGAKKVIISA
PSADAPMFVC GVNLDAYSPD MKVVSNASCT TNCLAPLAKV INDNFEIVEG LMTTVHATTA
TQKTVDGPSG KLWRDGRGAA QNIIPAATGA AKAVGKVIPA LNGKLTGMAF RVPTPNVSVV
DLTVRLGKGA TYDEIKAKVE EASKGPLKGI LGYTDEEVVS TDFFSDTHSS VFDAKAGISL
NDKFVKLISW YDNEFGYSNR VIDLIKYMQS KD
