ID G6PD2_MOUSE Reviewed; 513 AA. AC P97324; Q0VB18; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 164. DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase 2; DE Short=G6PD; DE EC=1.1.1.49 {ECO:0000269|PubMed:9169132}; GN Name=G6pd2; Synonyms=G6pd-2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, RP SUBUNIT, AND TISSUE SPECIFICITY. RC STRAIN=SWR/J; RX PubMed=9169132; DOI=10.1006/geno.1997.4673; RA Hendriksen P.J.M., Hoogerbrugge J.W., Baarends W.M., de Boer P., RA Vreeburg J.T.M., Vos E.A., van der Lende T., Grootegoed A.J.; RT "Testis-specific expression of a functional retroposon encoding glucose-6- RT phosphate dehydrogenase in the mouse."; RL Genomics 41:350-359(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). 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. {ECO:0000269|PubMed:9169132}. 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:0000269|PubMed:9169132}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15842; CC Evidence={ECO:0000305|PubMed:9169132}; CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step CC 1/3. {ECO:0000269|PubMed:9169132}. CC -!- SUBUNIT: Homotetramer; dimer of dimers (PubMed:9169132). Interacts with CC SIRT2; the interaction is enhanced by H(2)O(2) treatment (By CC similarity). {ECO:0000250|UniProtKB:P11413, CC ECO:0000269|PubMed:9169132}. 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 -!- TISSUE SPECIFICITY: Testis. {ECO:0000269|PubMed:9169132}. CC -!- PTM: Acetylated by ELP3; acetylation inhibits its homodimerization and CC enzyme activity. Deacetylated by SIRT2; deacetylation stimulates its CC enzyme activity (By similarity). {ECO:0000250|UniProtKB:P11413}. CC -!- MISCELLANEOUS: Has NADP both as cofactor (bound to the N-terminal CC domain) and as structural element bound to the C-terminal domain. 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; Z84471; CAB06476.1; -; Genomic_DNA. DR EMBL; BC120827; AAI20828.1; -; mRNA. DR EMBL; BC137684; AAI37685.1; -; mRNA. DR CCDS; CCDS19297.1; -. DR RefSeq; NP_062341.2; NM_019468.2. DR AlphaFoldDB; P97324; -. DR SMR; P97324; -. DR STRING; 10090.ENSMUSP00000131163; -. DR GlyGen; P97324; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P97324; -. DR PhosphoSitePlus; P97324; -. DR SwissPalm; P97324; -. DR jPOST; P97324; -. DR MaxQB; P97324; -. DR PaxDb; 10090-ENSMUSP00000131163; -. DR PeptideAtlas; P97324; -. DR ProteomicsDB; 267551; -. DR DNASU; 14380; -. DR GeneID; 14380; -. DR KEGG; mmu:14380; -. DR AGR; MGI:105977; -. DR CTD; 14380; -. DR MGI; MGI:105977; G6pd2. DR eggNOG; KOG0563; Eukaryota. DR InParanoid; P97324; -. DR OrthoDB; 989808at2759; -. DR UniPathway; UPA00115; UER00408. DR BioGRID-ORCS; 14380; 5 hits in 78 CRISPR screens. DR PRO; PR:P97324; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; P97324; Protein. DR GO; GO:0034451; C:centriolar satellite; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:MGI. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI. DR GO; GO:0030246; F:carbohydrate binding; ISO:MGI. DR GO; GO:0005536; F:glucose binding; ISO:MGI. DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IDA:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0050661; F:NADP binding; ISO:MGI. DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI. DR GO; GO:0034599; P:cellular response to oxidative stress; ISO:MGI. DR GO; GO:0006695; P:cholesterol biosynthetic process; ISO:MGI. DR GO; GO:0043249; P:erythrocyte maturation; ISO:MGI. DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; ISS:UniProtKB. DR GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central. DR GO; GO:0006749; P:glutathione metabolic process; ISO:MGI. DR GO; GO:0006739; P:NADP metabolic process; ISS:UniProtKB. DR GO; GO:0006740; P:NADPH regeneration; ISO:MGI. DR GO; GO:0061052; P:negative regulation of cell growth involved in cardiac muscle cell development; ISO:MGI. DR GO; GO:0010734; P:negative regulation of protein glutathionylation; ISO:MGI. DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; ISO:MGI. DR GO; GO:0019322; P:pentose biosynthetic process; ISO:MGI. DR GO; GO:0006098; P:pentose-phosphate shunt; ISO:MGI. DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; ISO:MGI. DR GO; GO:1904879; P:positive regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; ISO:MGI. DR GO; GO:0043523; P:regulation of neuron apoptotic process; ISO:MGI. DR GO; GO:0045471; P:response to ethanol; ISO:MGI. DR GO; GO:0046390; P:ribose phosphate biosynthetic process; ISO:MGI. 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 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. PE 1: Evidence at protein level; KW Acetylation; Carbohydrate metabolism; Cytoplasm; Glucose metabolism; KW Hydroxylation; Membrane; NADP; Oxidoreductase; Phosphoprotein; KW Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P11413" FT CHAIN 2..513 FT /note="Glucose-6-phosphate 1-dehydrogenase 2" FT /id="PRO_0000068086" FT ACT_SITE 263 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P11411" FT BINDING 38..45 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 72 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 147 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 171 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 171 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 201..205 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 239 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 258 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 357 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 360 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 365 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 366 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 370 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 393 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 395 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 401..403 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 421..423 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 487 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 503 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P11413" 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 432 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 513 AA; 59126 MW; 655830EB767B6C53 CRC64; MAEQVTLSRT QVCGILREEL YQNDAFHQAD THIFIIMGAS GDLAKKKIYP TIWWLFRDGL LPKETFIVGY ARSQLTVDDI QKQSEPFFKA TPEERPKLEE FFTRNSYVVG QYDDPASYKH LNSYINALHQ GMQANHLFYL ALPPTVYEAV TKNIQETCMS QTGFNRIIVE KPFGRDLQSS NQLSNHISSL FREDQIYRID HYLDKEMVQN LMVLRFANRI FGPIWNGDNI VCVILTFKEP FGTEGRGGYF DEFGIIRDVM QSHLLQMLCL VAMEKPATTD SDDVRNEKVK VLKCISEVET DNVILGQYVG NPNGEGEAAN GYLDDPTVPR GSTTATFAAA VLYVKNERWD GVPFILRCGK ALNERKAEVR LQFRDIPGDI FHQKCKRNEL VIRMQPNEAV YTTMMTKKPG MFFNPEESEL DLTYGNKYKN VKLPGAYERL ILDVFCGCQM HFVRTDELRE GWRIFTPLLH KIEREKPQPF PYVYGSRGPT EADELMRRVG FQYKGTYKGT HKH //