ID G6PD_ENCCU Reviewed; 434 AA. AC Q8SR89; DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 27-MAR-2024, entry version 109. DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase; DE Short=G6PD; DE EC=1.1.1.49 {ECO:0000250|UniProtKB:P11413}; GN Name=ZWF1; OrderedLocusNames=ECU08_1850; OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite). OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae; OC Encephalitozoon. OX NCBI_TaxID=284813; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GB-M1; RX PubMed=11719806; DOI=10.1038/35106579; RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F., RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P., RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J., RA Vivares C.P.; RT "Genome sequence and gene compaction of the eukaryote parasite RT Encephalitozoon cuniculi."; RL Nature 414:450-453(2001). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND RP DEVELOPMENTAL STAGE. RX PubMed=16691553; DOI=10.1002/pmic.200500796; RA Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.; RT "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi RT (microsporidia): a reference map for proteins expressed in late sporogonial RT stages."; RL Proteomics 6:3625-3635(2006). CC -!- FUNCTION: Catalyzes the rate-limiting step of the oxidative pentose- CC phosphate pathway, which represents a route for the dissimilation of CC carbohydrates besides glycolysis. The main function of this enzyme is CC to provide reducing power (NADPH) and pentose phosphates for fatty acid CC and nucleic acid synthesis (By similarity). CC {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 -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step CC 1/3. {ECO:0000305}. CC -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages. CC {ECO:0000269|PubMed:16691553}. 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; AL590448; CAD26488.1; -; Genomic_DNA. DR RefSeq; NP_597312.1; NM_001041921.1. DR AlphaFoldDB; Q8SR89; -. DR SMR; Q8SR89; -. DR STRING; 284813.Q8SR89; -. DR GeneID; 859734; -. DR KEGG; ecu:ECU08_1850; -. DR VEuPathDB; MicrosporidiaDB:ECU08_1850; -. DR HOGENOM; CLU_051220_0_0_1; -. DR InParanoid; Q8SR89; -. DR OMA; TLIYDCL; -. DR OrthoDB; 989808at2759; -. DR UniPathway; UPA00115; UER00408. DR Proteomes; UP000000819; Chromosome VIII. 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: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; IPR022675; G6P_DH_C. 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; 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. PE 1: Evidence at protein level; KW Carbohydrate metabolism; Glucose metabolism; NADP; Oxidoreductase; KW Reference proteome. FT CHAIN 1..434 FT /note="Glucose-6-phosphate 1-dehydrogenase" FT /id="PRO_0000381752" FT ACT_SITE 198 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P11411" FT BINDING 7..14 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 36 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 93 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 112 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 112 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 137..141 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 175 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 193 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 280 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" SQ SEQUENCE 434 AA; 49544 MW; 0FD1BE2052CF0D45 CRC64; MKVVIFGSSG DLAKRKLFPA LSRIDLEGVG VVGYARTKYN IEFSEVLQEV GNYSPEFLSK VTYIPGPYDD LSKLKEVSDS ETVLYFSVPS SVYTCLFREI SKLDYKVIGV EKPYGDSIES FMEIKGFDLG KTRFIDHYLL KPLVVAMPGI IRETGAIREV MSNRYVKSVE IVSKEVLGGE GRHYFDKNGI IRDMVLSHMG ELLGVVASDV TKPSRIMEAL ARMEVFKACT VDTERCIYGQ YDDYIKEIHK DSSTETFCMV PISIGTPRWS KVPFIIVAGK GMNEKRTEII LEFRRDVFAK CIELFSMPRQ SSCRIVHTNE IETVRLVFNI YPECEVFLEV LVGGEPVRYV LHDKKEIDGL MHDSYGGYHD YEIIFDSLVR GKDFSSVSSQ EAELLWKVFN PILSISKEDM LFYYSKGIDM PKEAEEMIRE IKDH //