ID   6PGD_DROME              Reviewed;         481 AA.
AC   P41572; M9PIS3; Q9W519;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2026, sequence version 2.
DT   02-SEP-2026, entry version 174.
DE   RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating;
DE            EC=1.1.1.44;
GN   Name=Pgd; ORFNames=CG3724;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-206.
RC   STRAIN=Canton-S;
RX   PubMed=1765265; DOI=10.1016/0378-1119(91)90607-d;
RA   Scott M.J., Lucchesi J.C.;
RT   "Structure and expression of the Drosophila melanogaster gene encoding 6-
RT   phosphogluconate dehydrogenase.";
RL   Gene 109:177-183(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NL01, NL02, NL11, NL12, NL14, NL15, NL16, NL17, NL18, NL19,
RC   NL20, ZK082, ZK084, ZK095, ZK131, ZK145, ZK157, ZK186, ZK191, ZK229,
RC   ZK377, ZK384, and ZK398;
RX   PubMed=25855066; DOI=10.1534/genetics.115.177030;
RA   Voigt S., Laurent S., Litovchenko M., Stephan W.;
RT   "Positive Selection at the Polyhomeotic Locus Led to Decreased
RT   Thermosensitivity of Gene Expression in Temperate Drosophila
RT   melanogaster.";
RL   Genetics 200:591-599(2015).
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 GENOMIC DNA].
RC   STRAIN=Oregon-R;
RX   PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA   Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA   Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA   Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA   Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA   Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA   Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA   McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA   Glover D.M.;
RT   "From sequence to chromosome: the tip of the X chromosome of D.
RT   melanogaster.";
RL   Science 287:2220-2222(2000).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Testis;
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).
CC   -!- FUNCTION: Catalyzes the oxidative decarboxylation of 6-phosphogluconate
CC       to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP
CC       to NADPH. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-phospho-D-gluconate + NADP(+) = D-ribulose 5-phosphate + CO2
CC         + NADPH; Xref=Rhea:RHEA:10116, ChEBI:CHEBI:16526, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58121, ChEBI:CHEBI:58349, ChEBI:CHEBI:58759; EC=1.1.1.44;
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC       3/3.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; M80598; AAA28786.1; -; Genomic_DNA.
DR   EMBL; KR024139; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KR024140; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KR024141; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KR024142; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KR024144; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KR024145; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KR024146; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KR024147; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KR024148; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KR024149; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KR024150; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KR024151; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KR024152; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KR024153; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KR024154; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KR024155; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KR024156; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KR024157; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KR024158; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KR024159; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KR024160; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KR024161; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KR024162; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AE014298; AAF45732.1; -; Genomic_DNA.
DR   EMBL; AE014298; AGB95021.1; -; Genomic_DNA.
DR   EMBL; Z98269; CAB10974.1; -; Genomic_DNA.
DR   EMBL; AY089447; AAL90185.1; -; mRNA.
DR   PIR; JH0531; JH0531.
DR   RefSeq; NP_001259175.1; NM_001272246.1.
DR   RefSeq; NP_476860.2; NM_057512.3.
DR   AlphaFoldDB; P41572; -.
DR   SMR; P41572; -.
DR   BioGRID; 57726; 36.
DR   FunCoup; P41572; 1170.
DR   IntAct; P41572; 156.
DR   STRING; 7227.FBpp0070368; -.
DR   PaxDb; 7227-FBpp0070368; -.
DR   PeptideAtlas; P41572; -.
DR   EnsemblMetazoa; FBtr0070384; FBpp0070368; FBgn0004654.
DR   GeneID; 31185; -.
DR   KEGG; dme:Dmel_CG3724; -.
DR   AGR; FB:FBgn0004654; -.
DR   CTD; 5226; -.
DR   FlyBase; FBgn0004654; Pgd.
DR   VEuPathDB; VectorBase:FBgn0004654; -.
DR   eggNOG; KOG2653; Eukaryota.
DR   HOGENOM; CLU_024540_4_2_1; -.
DR   InParanoid; P41572; -.
DR   OMA; CVTHVGP; -.
DR   OrthoDB; 434986at2759; -.
DR   PhylomeDB; P41572; -.
DR   Reactome; R-DME-71336; Pentose phosphate pathway.
DR   UniPathway; UPA00115; UER00410.
DR   BioGRID-ORCS; 31185; 2 hits in 3 CRISPR screens.
DR   GenomeRNAi; 31185; -.
DR   PRO; PR:P41572; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0004654; Expressed in fat body cell in male reproductive gland and 135 other cell types or tissues.
DR   ExpressionAtlas; P41572; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISS:FlyBase.
DR   GO; GO:0050661; F:NADP binding; IBA:GO_Central.
DR   GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IDA:FlyBase.
DR   GO; GO:0042593; P:glucose homeostasis; IMP:FlyBase.
DR   GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IMP:FlyBase.
DR   FunFam; 1.10.1040.10:FF:000002; 6-phosphogluconate dehydrogenase, decarboxylating; 1.
DR   FunFam; 1.20.5.320:FF:000002; 6-phosphogluconate dehydrogenase, decarboxylating; 1.
DR   FunFam; 3.40.50.720:FF:000007; 6-phosphogluconate dehydrogenase, decarboxylating; 1.
DR   Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1.
DR   Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR006114; 6PGDH_C.
DR   InterPro; IPR006113; 6PGDH_Gnd/GntZ.
DR   InterPro; IPR006115; 6PGDH_NADP-bd.
DR   InterPro; IPR006184; 6PGdom_BS.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR006183; Pgluconate_DH.
DR   NCBIfam; TIGR00873; gnd; 1.
DR   NCBIfam; NF006765; PRK09287.1; 1.
DR   PANTHER; PTHR11811; 6-PHOSPHOGLUCONATE DEHYDROGENASE; 1.
DR   Pfam; PF00393; 6PGD; 1.
DR   Pfam; PF03446; NAD_binding_2; 1.
DR   PIRSF; PIRSF000109; 6PGD; 1.
DR   PRINTS; PR00076; 6PGDHDRGNASE.
DR   SMART; SM01350; 6PGD; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00461; 6PGD; 1.
PE   2: Evidence at transcript level;
KW   Gluconate utilization; NADP; Oxidoreductase; Pentose shunt;
KW   Reference proteome.
FT   CHAIN           1..481
FT                   /note="6-phosphogluconate dehydrogenase, decarboxylating"
FT                   /id="PRO_0000090069"
FT   ACT_SITE        184
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        191
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         11..16
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         34..36
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         76..78
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         130..132
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         187..188
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         192
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         259
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         286
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         445
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
FT   BINDING         451
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
FT   VARIANT         206
FT                   /note="Q -> K (in strain: Canton-S)"
FT                   /evidence="ECO:0000269|PubMed:1765265"
SQ   SEQUENCE   481 AA;  52491 MW;  CB1A9D93315561BF CRC64;
     MSGQADIALI GLAVMGQNLI LNMDEKGFVV CAYNRTVAKV KEFLANEAKD TKVIGADSLE
     DMVSKLKSPR KVMLLVKAGS AVDDFIQQLV PLLSAGDVII DGGNSEYQDT SRRCDELAKL
     GLLFVGSGVS GGEEGARHGP SLMPGGHEAA WPLIQPIFQA ICAKADGEPC CEWVGDGGAG
     HFVKMVHNGI EYGDMQLICE AYHIMQSLGL SADQMADEFG KWNSAELDSF LIEITRDILK
     YKDGKGYLLE RIRDTAGQKG TGKWTAIAAL QYGVPVTLIG EAVFSRCLSA LKDERVQASS
     VLKGPSTKAQ VANLTKFLDD IKHALYCAKI VSYAQGFMLM REAARENKWR LNYGGIALMW
     RGGCIIRSVF LGNIKDAYTS QPELSNLLLD DFFKKAIERG QDSWREVVAN AFRWGIPVPA
     LSTALSFYDG YRTAKLPANL LQAQRDYFGA HTYELLGQEG QFHHTNWTGT GGNVSASTYQ
     A
//