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   08-NOV-2023, entry version 185.
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,
RC   Z42, 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; 7227-FBpp0074517; -.
DR   DNASU; 32974; -.
DR   GeneID; 32974; -.
DR   KEGG; dme:Dmel_CG12529; -.
DR   AGR; FB:FBgn0004057; -.
DR   CTD; 32974; -.
DR   FlyBase; FBgn0004057; Zw.
DR   VEuPathDB; VectorBase:FBgn0004057; -.
DR   eggNOG; KOG0563; Eukaryota.
DR   InParanoid; P12646; -.
DR   OrthoDB; 989808at2759; -.
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   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   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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   NCBIfam; TIGR00871; zwf; 1.
DR   PANTHER; PTHR23429:SF0; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE; 1.
DR   PANTHER; PTHR23429; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE G6PD; 1.
DR   Pfam; PF02781; G6PD_C; 1.
DR   Pfam; PF00479; G6PD_N; 1.
DR   PIRSF; PIRSF000110; G6PD; 1.
DR   PRINTS; PR00079; G6PDHDRGNASE.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
DR   Genevisible; P12646; DM.
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
//