ID Q95WK4_ANOQU Unreviewed; 153 AA. AC Q95WK4; DT 01-DEC-2001, integrated into UniProtKB/TrEMBL. DT 01-DEC-2001, sequence version 1. DT 27-NOV-2024, entry version 80. DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000256|ARBA:ARBA00020444}; DE EC=1.1.1.49 {ECO:0000256|ARBA:ARBA00013019}; DE Flags: Fragment; GN Name=G6pd {ECO:0000313|EMBL:AAL18428.1}; OS Anopheles quadrimaculatus (Common malaria mosquito). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae; OC Anophelinae; Anopheles. OX NCBI_TaxID=7166 {ECO:0000313|EMBL:AAL18428.1}; RN [1] {ECO:0000313|EMBL:AAL18428.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=12116652; DOI=10.1080/106351501750435095; RA Krzywinski J., Wilkerson R.C., Besansky N.J.; RT "Toward understanding Anophelinae (Diptera, Culicidae) phylogeny: insights RT from nuclear single-copy genes and the weight of evidence."; RL Syst. Biol. 50:540-556(2001). 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:0000256|ARBA:ARBA00002914}. CC -!- CATALYTIC ACTIVITY: CC Reaction=D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5- CC lactone + NADPH + H(+); 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:0000256|ARBA:ARBA00001220}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15842; CC Evidence={ECO:0000256|ARBA:ARBA00001220}; CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step CC 1/3. {ECO:0000256|ARBA:ARBA00004937}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000256|ARBA:ARBA00004514}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF317809; AAL18428.1; -; Genomic_DNA. DR AlphaFoldDB; Q95WK4; -. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW. DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IEA:TreeGrafter. DR FunFam; 3.40.50.720:FF:000111; Glucose-6-phosphate 1-dehydrogenase; 1. 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 4: Predicted; KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277}; KW Glucose metabolism {ECO:0000256|ARBA:ARBA00022526}; KW NADP {ECO:0000256|ARBA:ARBA00022857}. FT DOMAIN 1..152 FT /note="Glucose-6-phosphate dehydrogenase NAD-binding" FT /evidence="ECO:0000259|Pfam:PF00479" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AAL18428.1" FT NON_TER 153 FT /evidence="ECO:0000313|EMBL:AAL18428.1" SQ SEQUENCE 153 AA; 17901 MW; 48F4D50B38AC19DD CRC64; LWWLFRDNLV PSDTKFVGYA RSKLSVAELK EKCRQYMKVK DAELEKFDEF WSVNFYVAGS YDSRRDFELL NQEIAKFEVG RAANRLFYLA LPPSVFESVT VHIRNTCMGE KGWNRIIVEK PFGRDASSSN ALSAHLSKLF SEDQLYRIDH YLV //