G6PD_DROME
ID G6PD_DROME Reviewed; 524 AA.
AC P12646; Q27574; Q27872; Q27879; Q27881; Q9VWE2; Q9VWE3;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase;
DE Short=G6PD;
DE EC=1.1.1.49 {ECO:0000250|UniProtKB:P11413};
DE AltName: Full=Zwischenferment;
GN Name=Zw; Synonyms=G6PD; ORFNames=CG12529;
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 (ISOFORM A).
RX PubMed=2838391; DOI=10.1016/0378-1119(88)90530-6;
RA Fouts D., Ganguly R., Gutierrez A.G., Lucchesi J.C., Manning J.E.;
RT "Nucleotide sequence of the Drosophila glucose-6-phosphate dehydrogenase
RT gene and comparison with the homologous human gene.";
RL Gene 63:261-275(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORM A).
RC STRAIN=F23.3, F24.1, MT32, MT41, MT68, Z11, Z16, Z21, Z27, Z3, Z41, Z42,
RC Z5, Z55, Z62, Z64, and Z74;
RX PubMed=8913747; DOI=10.1093/genetics/144.3.1027;
RA Eanes W.F., Kirchner M., Yoon J., Biermann C.H., Wang I.N., McCartney M.A.,
RA Verrelli B.C.;
RT "Historical selection, amino acid polymorphism and lineage-specific
RT divergence at the G6pd locus in Drosophila melanogaster and D. simulans.";
RL Genetics 144:1027-1041(1996).
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, AND ALTERNATIVE SPLICING.
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] (ISOFORM A).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Cytosolic glucose-6-phosphate dehydrogenase that catalyzes
CC the first and rate-limiting step of the oxidative branch within the
CC pentose phosphate pathway/shunt, an alternative route to glycolysis for
CC the dissimilation of carbohydrates and a major source of reducing power
CC and metabolic intermediates for fatty acid and nucleic acid
CC biosynthetic processes. {ECO:0000250|UniProtKB:P11413}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-
CC lactone + H(+) + NADPH; Xref=Rhea:RHEA:15841, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57955, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:61548; EC=1.1.1.49;
CC Evidence={ECO:0000250|UniProtKB:P11413};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15842;
CC Evidence={ECO:0000250|UniProtKB:P11413};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC 1/3. {ECO:0000250|UniProtKB:P11413}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P11413}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=P12646-1; Sequence=Displayed;
CC Name=B;
CC IsoId=P12646-2; Sequence=VSP_001593;
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; M26674; AAA51463.1; -; Genomic_DNA.
DR EMBL; M26673; AAA51463.1; JOINED; Genomic_DNA.
DR EMBL; U42738; AAB02801.1; -; Genomic_DNA.
DR EMBL; U42739; AAB02802.1; -; Genomic_DNA.
DR EMBL; U42740; AAB02803.1; -; Genomic_DNA.
DR EMBL; U42741; AAB02804.1; -; Genomic_DNA.
DR EMBL; U42742; AAB02805.1; -; Genomic_DNA.
DR EMBL; U42743; AAB02806.1; -; Genomic_DNA.
DR EMBL; U42744; AAB02807.1; -; Genomic_DNA.
DR EMBL; U42745; AAB02808.1; -; Genomic_DNA.
DR EMBL; U42746; AAB02809.1; -; Genomic_DNA.
DR EMBL; U42747; AAB02810.1; -; Genomic_DNA.
DR EMBL; U42748; AAB02811.1; -; Genomic_DNA.
DR EMBL; U42749; AAB02812.1; -; Genomic_DNA.
DR EMBL; U43165; AAA99071.1; -; Genomic_DNA.
DR EMBL; U43166; AAA99072.1; -; Genomic_DNA.
DR EMBL; U43167; AAA99073.1; -; Genomic_DNA.
DR EMBL; U44721; AAA99092.1; -; Genomic_DNA.
DR EMBL; U45985; AAA99107.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF48999.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF49000.2; -; Genomic_DNA.
DR EMBL; AY052079; AAK93503.1; -; mRNA.
DR PIR; A47740; A47740.
DR PIR; JT0272; DEFFG6.
DR RefSeq; NP_001285456.1; NM_001298527.1.
DR RefSeq; NP_523411.1; NM_078687.2.
DR RefSeq; NP_728287.1; NM_167676.2.
DR AlphaFoldDB; P12646; -.
DR SMR; P12646; -.
DR BioGRID; 59270; 11.
DR DIP; DIP-20748N; -.
DR IntAct; P12646; 2.
DR STRING; 7227.FBpp0074517; -.
DR iPTMnet; P12646; -.
DR PaxDb; P12646; -.
DR PRIDE; P12646; -.
DR DNASU; 32974; -.
DR GeneID; 32974; -.
DR KEGG; dme:Dmel_CG12529; -.
DR CTD; 32974; -.
DR FlyBase; FBgn0004057; Zw.
DR VEuPathDB; VectorBase:FBgn0004057; -.
DR eggNOG; KOG0563; Eukaryota.
DR InParanoid; P12646; -.
DR PhylomeDB; P12646; -.
DR Reactome; R-DME-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-DME-71336; Pentose phosphate pathway.
DR UniPathway; UPA00115; UER00408.
DR BioGRID-ORCS; 32974; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 32974; -.
DR PRO; PR:P12646; -.
DR Proteomes; UP000000803; Chromosome X.
DR ExpressionAtlas; P12646; baseline and differential.
DR Genevisible; P12646; DM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IMP:FlyBase.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; ISS:UniProtKB.
DR GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
DR GO; GO:0006739; P:NADP metabolic process; ISS:UniProtKB.
DR GO; GO:0006098; P:pentose-phosphate shunt; IMP:FlyBase.
DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IBA:GO_Central.
DR HAMAP; MF_00966; G6PD; 1.
DR InterPro; IPR001282; G6P_DH.
DR InterPro; IPR019796; G6P_DH_AS.
DR InterPro; IPR022675; G6P_DH_C.
DR InterPro; IPR022674; G6P_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR23429; PTHR23429; 1.
DR Pfam; PF02781; G6PD_C; 1.
DR Pfam; PF00479; G6PD_N; 1.
DR PIRSF; PIRSF000110; G6PD; 1.
DR PRINTS; PR00079; G6PDHDRGNASE.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00871; zwf; 1.
DR PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Carbohydrate metabolism; Cytoplasm;
KW Glucose metabolism; NADP; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..524
FT /note="Glucose-6-phosphate 1-dehydrogenase"
FT /id="PRO_0000068092"
FT ACT_SITE 267
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 42..49
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 205..209
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 365
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 370
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 371
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 375
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 398
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 400
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 406..408
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 426..428
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 492
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 508
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 514
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1..22
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_001593"
FT VARIANT 32
FT /note="G -> C (in strain: F24.1, MT32 and MT68)"
FT VARIANT 80
FT /note="T -> N (in strain: Z74)"
FT VARIANT 382
FT /note="L -> P (in strain: F23.3, MT41, Z3, Z5, Z11, Z16,
FT Z21, Z27, Z42, Z55, Z64, Z74 and Berkeley)"
FT CONFLICT 185..186
FT /note="QA -> AG (in Ref. 1; AAA51463)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="N -> K (in Ref. 1; AAA51463)"
FT /evidence="ECO:0000305"
FT CONFLICT 344..346
FT /note="LGV -> ARS (in Ref. 1; AAA51463)"
FT /evidence="ECO:0000305"
FT CONFLICT 461..465
FT /note="DELRE -> AAAQ (in Ref. 1; AAA51463)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 524 AA; 60431 MW; ABF81B763A82F1FD CRC64;
MATQKEDHTA LDLIIKSLKS PTMVCEGTHF DGKIPHTFVI FGASGDLAKK KIYPTLWWLY
RDDLLPKPTK FCGYARSMLT VDSIKEQCLP YMKVQPHEQK KYEEFWALNE YVSGRYDGRT
GFELLNQQLE IMENKNKANR IFYLALPPSV FEEVTVNIKQ ICMSVCGWNR VIIEKPFGRD
DASSQALSDH LAGLFQEDQL YRIDHYLGKE MVQNLMTIRF GNKILSSTWN RENIASVLIT
FKEPFGTQGR GGYFDEFGII RDVMQNHLLQ ILSLVAMEKP VSCHPDDIRD EKVKVLKSIE
ALTLDDMVLG QYLGNPQGTN DDARTGYVED PTVSNDSNTP TYALGVLKIN NERWQGVPFI
LRCGKALNER KAEVRIQYQD VLGDIFEGNT KRNELVIRVQ PGEALYFKMM TKSPGITFDI
EETELDLTYE HRYKDSYLPD AYERLILDVF CGSQMHFVRS DELREAWRIF TPILHQIEKE
HIRPITYQYG SRGPKEADRK CEENNFKYSG SYKWHGGKAA TSNH
