ID G6PD_CERCA Reviewed; 526 AA. AC P41571; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-SEP-2023, entry version 101. 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; OS Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea; OC Tephritidae; Ceratitis; Ceratitis. OX NCBI_TaxID=7213; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8269100; DOI=10.1111/j.1365-2583.1993.tb00094.x; RA Scott M.J., Kriticou D., Robinson A.S.; RT "Isolation of cDNAs encoding 6-phosphogluconate dehydrogenase and glucose- RT 6-phosphate dehydrogenase from the mediterranean fruit fly Ceratitis RT capitata: correlating genetic and physical maps of chromosome 5."; RL Insect Mol. Biol. 1:213-222(1993). 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; S67872; AAB29395.1; -; mRNA. DR RefSeq; NP_001266304.1; NM_001279375.1. DR AlphaFoldDB; P41571; -. DR SMR; P41571; -. DR EnsemblMetazoa; NM_001279375.1; NP_001266304.1; GeneID_101453374. DR GeneID; 101453374; -. DR KEGG; ccat:101453374; -. DR CTD; 32974; -. DR OrthoDB; 989808at2759; -. 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 2: Evidence at transcript level; KW Carbohydrate metabolism; Cytoplasm; Glucose metabolism; NADP; KW Oxidoreductase. FT CHAIN 1..526 FT /note="Glucose-6-phosphate 1-dehydrogenase" FT /id="PRO_0000068090" FT ACT_SITE 276 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 50..57 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 84 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 184 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 184 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 214..218 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 252 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 271 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 370 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 373 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 378 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 379 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 383 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 406 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 408 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 414..416 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 434..436 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 500 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 516 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 522 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250" SQ SEQUENCE 526 AA; 60592 MW; 4047EBF7444C4917 CRC64; MATQHFTNGS ATDDGETALE HIIKSLETPT MKCEGTHFDS HVPHTFVIFG ASGDLAKKKI YPTLWWLYRD NLLPKSTKFC GYARSKLTIE ELRAKCHQYM KVQPDEQAKY EEFWQNHDYA AGSYDQRSDF VALKERLSSL ESCNCSCNRI FYLALPPSVF ERVTVNIKDI CLAERGWNRV IIEKPFGRDD VTSKKLSDHL ASLFHEDQLY RIDHYLGKEM VQNLMTIRFA NKILNSTWNR ENIASVLITF KEPFGTQGRG GYFDEFGIIR DVMQNHLLQI LSLVAMEKPT SCQPDDIRDE KVKVLKSIPA LTLDDMVLGQ YVGNPNGVGE QREGYLDDPT VSNDSNTPTY AQGVLRINNE RWDGVPFILR CGKALDERKA VVRIQYRDVP GDIFEGNSKR NELVIRVQPG EALYFKMMTK SPGITFDIEE TELDLTYEHR YKNSYLPDAY ERLILDVFCG SQMHFVRSDE LSEAWRIFTP VLNEIENNKV KPIPYVFGSR GPKEADQKTS ENNFKYYGSY KWIGKK //