ID   G6PD_CULPI              Reviewed;         153 AA.
AC   Q23711;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   22-FEB-2023, entry version 99.
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;
DE   Flags: Fragment;
GN   Name=ZW;
OS   Culex pipiens (House mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Culicini; Culex; Culex.
OX   NCBI_TaxID=7175;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   AGRICOLA=IND20440286;
RA   Soto-Adames F.N., Robertson H.M., Berlocher S.H.;
RT   "Phylogenetic utility of partial DNA sequences of G6PDH at different
RT   taxonomic levels in Hexapoda with emphasis on Diptera.";
RL   Ann. Entomol. Soc. Am. 87:723-736(1994).
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   -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; U09034; AAB02778.1; -; mRNA.
DR   AlphaFoldDB; Q23711; -.
DR   SMR; Q23711; -.
DR   UniPathway; UPA00115; UER00408.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; ISS:UniProtKB.
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; IEA:UniProtKB-KW.
DR   GO; GO:0006739; P:NADP metabolic process; ISS:UniProtKB.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR001282; G6P_DH.
DR   InterPro; IPR022674; G6P_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR23429:SF0; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE; 1.
DR   PANTHER; PTHR23429; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE G6PD; 1.
DR   Pfam; PF00479; G6PD_N; 1.
DR   PRINTS; PR00079; G6PDHDRGNASE.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Cytoplasm; Glucose metabolism; NADP;
KW   Oxidoreductase.
FT   CHAIN           <1..>153
FT                   /note="Glucose-6-phosphate 1-dehydrogenase"
FT                   /id="PRO_0000068091"
FT   BINDING         21
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         120
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10005"
FT   BINDING         150..153
FT                   /ligand="substrate"
FT   NON_TER         1
FT   NON_TER         153
SQ   SEQUENCE   153 AA;  17999 MW;  F82E2F41C39C82E6 CRC64;
     LWWLFRDNLL PSVTKFVGYA RTKLTVAELK EKCHPYMKVD AAHEEKYDEF WALNFYVAGS
     YDGRRDFELL NQEIGKFEVG KTANRLFYLR LPPSVFETVT VHIRNTCMGL KGWNRIIVEK
     PFGRDADSSN KLSEHLAKLF TEDQLYRIDH YLG
//