ID G6PD_DROYA Reviewed; 518 AA. AC Q27638; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 24-JAN-2024, entry version 113. DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase; DE Short=G6PD; DE EC=1.1.1.49 {ECO:0000250|UniProtKB:P11413}; DE Flags: Fragment; GN Name=Zw; Synonyms=G6pd; OS Drosophila yakuba (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7245; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=BG1016; RA Eanes W.F., Kirchner M., Yoon J., Biermann C., Wang I., McCartney M., RA Verrelli B.C.; RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases. 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}. 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; U42750; AAB02813.1; -; Genomic_DNA. DR AlphaFoldDB; Q27638; -. DR SMR; Q27638; -. DR eggNOG; KOG0563; Eukaryota. 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 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. PE 3: Inferred from homology; KW Carbohydrate metabolism; Cytoplasm; Glucose metabolism; NADP; KW Oxidoreductase. FT CHAIN <1..518 FT /note="Glucose-6-phosphate 1-dehydrogenase" FT /id="PRO_0000068094" FT ACT_SITE 261 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 36..43 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 70 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 169 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 169 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 199..203 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 237 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 256 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 356 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 359 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 364 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 365 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 369 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 392 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 394 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 400..402 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 420..422 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 486 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 502 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 NON_TER 1 SQ SEQUENCE 518 AA; 59938 MW; 6AFA194E1D3A3E8B CRC64; DHTALDLIIK SLKSPTMVCE GTHFDGKIPH TFVIFGASGD LAKKKIYPKL WWFYRDDLLP KLTKFCGYAR SMLTVDSIKE QCLPYMKVQS HEQKKYEEFW ALNEYVSGRY DGRTGFELLN QQLELMENKN KANRIFYLAL PPSVFEEVTV NIKQICMSVC GWNRVIIEKP FGRDDASSQA LSDHLAALFH EDQLYRIDHY LGKEMVQNLM TIRFGNKILS STWNRENIAS VLITFKEPFG TQGRGGYFDE FGIIRDVMQN HLLQILSLVA MEKPVSCHPD DIRDEKVKVL KSIETLTLKD MVLGQYLGNP QGTTDDARTG YVEDPTVSDD SNTPTYALGV LKINNERWQG VPFILRCGKR LNERKAEVRI QYQDVPGDIF EGNTKRNELV IRVQPGEALY FKMMTKSPGI TFDIEETELD LTYEHRYKDS YLPDAYERLI LDVFCGSQMH FVRSDQLREA WRIFTPILHQ IEREHIRPIT YQYGSRGPKE ADRMCEENNF KYSGSYKWHG GKAATSNL //