ID G6PD_CRIGR Reviewed; 515 AA. AC O55044; DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 127. DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase; DE Short=G6PD; DE EC=1.1.1.49 {ECO:0000250|UniProtKB:P11413}; GN Name=G6PD; OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; OC Cricetidae; Cricetinae; Cricetulus. OX NCBI_TaxID=10029; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Ovary; RA Perez M.L., Stamato T.D.; RT "cDNA sequence of Chinese hamster glucose-6-phosphate Dehydrogenase."; RL Submitted (JAN-1998) 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 -!- SUBUNIT: Homotetramer; dimer of dimers. Interacts with SIRT2; the CC interaction is enhanced by H(2)O(2) treatment (By similarity). Forms a CC ternary complex with ALDOB and TP53; this interaction is direct. ALDOB CC stabilizes the complex inhibiting G6PD activity and keeping oxidative CC pentose phosphate metabolism in check. {ECO:0000250|UniProtKB:P11413}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:P11413}. Membrane CC {ECO:0000250|UniProtKB:P11413}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:P11413}. CC -!- PTM: Acetylated by ELP3 at Lys-403; acetylation inhibits its CC homodimerization and enzyme activity. Deacetylated by SIRT2 at Lys-403; CC deacetylation stimulates its enzyme activity (By similarity). 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; AF044676; AAC00204.1; -; mRNA. DR RefSeq; NP_001233656.1; NM_001246727.1. DR AlphaFoldDB; O55044; -. DR SMR; O55044; -. DR PaxDb; 10029-NP_001233656-1; -. DR Ensembl; ENSCGRT00001011414.1; ENSCGRP00001007382.1; ENSCGRG00001009805.1. DR GeneID; 100689469; -. DR KEGG; cge:100689469; -. DR CTD; 2539; -. DR eggNOG; KOG0563; Eukaryota. DR GeneTree; ENSGT00530000063435; -. DR OrthoDB; 989808at2759; -. DR UniPathway; UPA00115; UER00408. DR Proteomes; UP000694386; Unplaced. DR Proteomes; UP001108280; Chromosome X. DR GO; GO:0034451; C:centriolar satellite; IEA:Ensembl. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:Ensembl. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:Ensembl. DR GO; GO:0005536; F:glucose binding; IEA:Ensembl. DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; ISS:UniProtKB. DR GO; GO:0050661; F:NADP binding; IEA:Ensembl. DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl. DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl. DR GO; GO:0006695; P:cholesterol biosynthetic process; IEA:Ensembl. DR GO; GO:0043249; P:erythrocyte maturation; IEA:Ensembl. 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:0006749; P:glutathione metabolic process; IEA:Ensembl. DR GO; GO:0006739; P:NADP metabolic process; ISS:UniProtKB. DR GO; GO:0010734; P:negative regulation of protein glutathionylation; IEA:Ensembl. DR GO; GO:0019322; P:pentose biosynthetic process; IEA:Ensembl. DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IEA:Ensembl. DR GO; GO:0046390; P:ribose phosphate biosynthetic process; IEA:Ensembl. 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 Acetylation; Carbohydrate metabolism; Cytoplasm; Glucose metabolism; KW Hydroxylation; Membrane; NADP; Oxidoreductase; Phosphoprotein. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P11413" FT CHAIN 2..515 FT /note="Glucose-6-phosphate 1-dehydrogenase" FT /id="PRO_0000068081" FT ACT_SITE 263 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 38..45 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 72 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 147 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 171 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 171 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 201..205 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 239 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 258 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 357 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 360 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 365 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 366 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" 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 393 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 395 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 401..403 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 421..423 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 487 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 503 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 509 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:P11413" FT MOD_RES 8 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P11413" FT MOD_RES 10 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P11413" FT MOD_RES 89 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P11413" FT MOD_RES 171 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT MOD_RES 171 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT MOD_RES 403 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P11413" FT MOD_RES 432 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P11413" FT MOD_RES 497 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P11413" FT MOD_RES 503 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P11413" SQ SEQUENCE 515 AA; 59326 MW; 892DD70C86C7438C CRC64; MAEQVALSRT QVCGILREEL YQGDAFHQAD THIFIIMGAS GDLAKKKIYP TIWWLFRDGL LPEDTFIVGY ARSRLTVDDI RKQSEPFFKA TPEERPKLEE FFARNSYVAG QYDDPASYKH LNSHMNALHQ GMQANRLFYL ALPPTVYEAV TKNIQETCMS QTGWNRIIVE KPFGRDLQSS NQLSNHISSL FREDQIYRID HYLGKEMVQN LMVLRFANRI FGPIWNRDNI ACVILTFKEP FGTEGRGGYF DEFGIIRDVM QNHLLQMLCL VAMEKPASTD SDDVRDEKVK VLKCISEVET SNVVLGQYVG NPNGEGEATN GYLDDPTVPR GSTTATFAAA VLYVENERWD GVPFILRCGK ALNERKAEVR LQFRDVAGDI FHQQCKRNEL VIRVQPNEAV YTKMMTKKPG MFFNPEESEL DLTYGNRYKN VKLPDAYERL ILDVFCGSQM HFVRSDELRE AWRIFTPLLH KIDQEKPQPI PYVYGSRGPT EADELMKRVG FQYEGTYKWV NPHKL //