G3P2_DROME
ID G3P2_DROME Reviewed; 332 AA.
AC P07487; A5XCW0; Q541C2; Q9VXM7;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 2;
DE EC=1.2.1.12;
DE AltName: Full=Glyceraldehyde-3-phosphate dehydrogenase II;
DE Short=GAPDH II;
GN Name=Gapdh2; ORFNames=CG8893;
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].
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 VARIANT VAL-80.
RC STRAIN=AF8, AF9, HFL1, HFL2, HFL3, HFL4, MA2, MA7, SC1, SC2, VT1, VT2, VT3,
RC VT4, Zh23, and Zh33;
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=Head;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-273 AND THR-274, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
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 -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; M11255; AAA28561.1; -; Genomic_DNA.
DR EMBL; DQ864106; ABH06741.1; -; Genomic_DNA.
DR EMBL; DQ864107; ABH06742.1; -; Genomic_DNA.
DR EMBL; DQ864108; ABH06743.1; -; Genomic_DNA.
DR EMBL; DQ864109; ABH06744.1; -; Genomic_DNA.
DR EMBL; DQ864110; ABH06745.1; -; Genomic_DNA.
DR EMBL; DQ864111; ABH06746.1; -; Genomic_DNA.
DR EMBL; DQ864112; ABH06747.1; -; Genomic_DNA.
DR EMBL; DQ864113; ABH06748.1; -; Genomic_DNA.
DR EMBL; DQ864114; ABH06749.1; -; Genomic_DNA.
DR EMBL; DQ864115; ABH06750.1; -; Genomic_DNA.
DR EMBL; DQ864116; ABH06751.1; -; Genomic_DNA.
DR EMBL; DQ864117; ABH06752.1; -; Genomic_DNA.
DR EMBL; DQ864118; ABH06753.1; -; Genomic_DNA.
DR EMBL; DQ864119; ABH06754.1; -; Genomic_DNA.
DR EMBL; DQ864120; ABH06755.1; -; Genomic_DNA.
DR EMBL; DQ864121; ABH06756.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF48531.1; -; Genomic_DNA.
DR EMBL; AY094940; AAM11293.1; -; mRNA.
DR PIR; B22366; B22366.
DR RefSeq; NP_001259584.1; NM_001272655.1.
DR RefSeq; NP_542445.1; NM_080714.4.
DR AlphaFoldDB; P07487; -.
DR SMR; P07487; -.
DR BioGRID; 58893; 36.
DR DIP; DIP-17969N; -.
DR IntAct; P07487; 3.
DR STRING; 7227.FBpp0073922; -.
DR iPTMnet; P07487; -.
DR PaxDb; P07487; -.
DR PRIDE; P07487; -.
DR DNASU; 32545; -.
DR EnsemblMetazoa; FBtr0074112; FBpp0073922; FBgn0001092.
DR EnsemblMetazoa; FBtr0332618; FBpp0304864; FBgn0001092.
DR GeneID; 32545; -.
DR KEGG; dme:Dmel_CG8893; -.
DR CTD; 32545; -.
DR FlyBase; FBgn0001092; Gapdh2.
DR VEuPathDB; VectorBase:FBgn0001092; -.
DR eggNOG; KOG0657; Eukaryota.
DR GeneTree; ENSGT00940000153298; -.
DR HOGENOM; CLU_030140_0_3_1; -.
DR InParanoid; P07487; -.
DR OMA; NCVAPMA; -.
DR OrthoDB; 945145at2759; -.
DR PhylomeDB; P07487; -.
DR SignaLink; P07487; -.
DR UniPathway; UPA00109; UER00184.
DR BioGRID-ORCS; 32545; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Gapdh2; fly.
DR GenomeRNAi; 32545; -.
DR PRO; PR:P07487; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0001092; Expressed in ovary and 13 other tissues.
DR ExpressionAtlas; P07487; baseline and differential.
DR Genevisible; P07487; DM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0042593; P:glucose homeostasis; IMP: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 1: Evidence at protein level;
KW Cytoplasm; Glycolysis; NAD; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..332
FT /note="Glyceraldehyde-3-phosphate dehydrogenase 2"
FT /id="PRO_0000145522"
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 MOD_RES 273
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 274
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT VARIANT 80
FT /note="A -> V (in strain: MA2)"
FT /evidence="ECO:0000269|PubMed:17379620"
FT CONFLICT 38
FT /note="N -> K (in Ref. 1; AAA28561)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 332 AA; 35369 MW; 5D5D274B8D3B4839 CRC64;
MSKIGINGFG RIGRLVLRAA IDKGANVVAV NDPFIDVNYM VYLFKFDSTH GRFKGTVAAE
GGFLVVNGQK ITVFSERDPA NINWASAGAE YIVESTGVFT TIDKASTHLK GGAKKVIISA
PSADAPMFVC GVNLDAYKPD MKVVSNASCT TNCLAPLAKV INDNFEIVEG LMTTVHATTA
TQKTVDGPSG KLWRDGRGAA QNIIPASTGA AKAVGKVIPA LNGKLTGMAF RVPTPNVSVV
DLTVRLGKGA SYDEIKAKVQ EAANGPLKGI LGYTDEEVVS TDFLSDTHSS VFDAKAGISL
NDKFVKLISW YDNEFGYSNR VIDLIKYMQS KD
