G6PD1_MOUSE
ID G6PD1_MOUSE Reviewed; 515 AA.
AC Q00612;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase X;
DE Short=G6PD;
DE EC=1.1.1.49 {ECO:0000269|PubMed:12831846};
GN Name=G6pdx; Synonyms=G6pd, G6pd-1;
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 [MRNA].
RX PubMed=8400362; DOI=10.3109/10425179309020830;
RA Zollo M.Z., D'Urso M., Schlessinger D., Chen E.Y.;
RT "Sequence of mouse glucose-6-phosphate dehydrogenase cDNA.";
RL DNA Seq. 3:319-322(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
RC STRAIN=BALB/cJ;
RX PubMed=1874446; DOI=10.1016/0378-1119(91)90078-p;
RA Toniolo D., Filippi M., Dono R., Lettieri T., Martini G.;
RT "The CpG island in the 5' region of the G6PD gene of man and mouse.";
RL Gene 102:197-203(1991).
RN [4]
RP PROTEIN SEQUENCE OF 57-71; 175-191 AND 247-257, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 163-214 AND 352-454.
RC STRAIN=BALB/cJ;
RX PubMed=9330624; DOI=10.1016/s0027-5107(97)00109-7;
RA Kuraguchi M., Thomas G.A., Williams E.D.;
RT "Somatic mutation of the glucose-6-phosphate dehydrogenase (g6pd) gene in
RT colonic stem cells and crypt restricted loss of G6PD activity.";
RL Mutat. Res. 379:69-75(1997).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=12831846; DOI=10.1016/s0003-9861(03)00229-7;
RA Clarke J.L., Mason P.J.;
RT "Murine hexose-6-phosphate dehydrogenase: a bifunctional enzyme with broad
RT substrate specificity and 6-phosphogluconolactonase activity.";
RL Arch. Biochem. Biophys. 415:229-234(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-507, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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:12831846}.
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:12831846};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15842;
CC Evidence={ECO:0000305|PubMed:12831846};
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:12831846}.
CC -!- SUBUNIT: Homotetramer; dimer of dimers. Interacts with SIRT2; the
CC interaction is enhanced by H(2)O(2) treatment (By similarity).
CC {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 -!- 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}.
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DR EMBL; Z11911; CAA77967.1; -; mRNA.
DR EMBL; AK088135; BAC40166.1; -; mRNA.
DR EMBL; X53617; CAA37679.1; -; Genomic_DNA.
DR EMBL; U88533; AAB52998.1; -; Genomic_DNA.
DR EMBL; U88534; AAB52999.1; -; Genomic_DNA.
DR CCDS; CCDS30232.1; -.
DR PIR; A56686; A56686.
DR RefSeq; NP_032088.1; NM_008062.2.
DR AlphaFoldDB; Q00612; -.
DR SMR; Q00612; -.
DR BioGRID; 199790; 25.
DR IntAct; Q00612; 2.
DR MINT; Q00612; -.
DR STRING; 10090.ENSMUSP00000004327; -.
DR iPTMnet; Q00612; -.
DR PhosphoSitePlus; Q00612; -.
DR SwissPalm; Q00612; -.
DR REPRODUCTION-2DPAGE; IPI00228385; -.
DR REPRODUCTION-2DPAGE; Q00612; -.
DR EPD; Q00612; -.
DR jPOST; Q00612; -.
DR PaxDb; Q00612; -.
DR PeptideAtlas; Q00612; -.
DR PRIDE; Q00612; -.
DR ProteomicsDB; 267505; -.
DR DNASU; 14381; -.
DR Ensembl; ENSMUST00000004327; ENSMUSP00000004327; ENSMUSG00000031400.
DR GeneID; 14381; -.
DR KEGG; mmu:14381; -.
DR UCSC; uc009toy.1; mouse.
DR CTD; 14381; -.
DR MGI; MGI:105979; G6pdx.
DR VEuPathDB; HostDB:ENSMUSG00000031400; -.
DR eggNOG; KOG0563; Eukaryota.
DR GeneTree; ENSGT00530000063435; -.
DR HOGENOM; CLU_013524_2_3_1; -.
DR InParanoid; Q00612; -.
DR OMA; VEICVYE; -.
DR OrthoDB; 383995at2759; -.
DR PhylomeDB; Q00612; -.
DR TreeFam; TF300584; -.
DR Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-MMU-71336; Pentose phosphate pathway.
DR UniPathway; UPA00115; UER00408.
DR BioGRID-ORCS; 14381; 21 hits in 74 CRISPR screens.
DR ChiTaRS; G6pdx; mouse.
DR PRO; PR:Q00612; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q00612; protein.
DR Bgee; ENSMUSG00000031400; Expressed in granulocyte and 254 other tissues.
DR ExpressionAtlas; Q00612; baseline and differential.
DR Genevisible; Q00612; MM.
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; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005634; C:nucleus; 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; IPI:MGI.
DR GO; GO:0050661; F:NADP binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0001998; P:angiotensin-mediated vasoconstriction involved in regulation of systemic arterial blood pressure; IMP:MGI.
DR GO; GO:0002033; P:angiotensin-mediated vasodilation involved in regulation of systemic arterial blood pressure; IMP: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:0048821; P:erythrocyte development; IMP: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; IMP:MGI.
DR GO; GO:0006741; P:NADP biosynthetic process; IDA: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; IDA:MGI.
DR GO; GO:0006098; P:pentose-phosphate shunt; ISO:MGI.
DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IMP:MGI.
DR GO; GO:1904879; P:positive regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; ISO:MGI.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP: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:0006979; P:response to oxidative stress; IMP:MGI.
DR GO; GO:0046390; P:ribose phosphate biosynthetic process; ISO:MGI.
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 PANTHER; PTHR23429; PTHR23429; 1.
DR Pfam; PF02781; G6PD_C; 1.
DR Pfam; PF00479; G6PD_N; 1.
DR PIRSF; PIRSF000110; G6PD; 1.
DR PRINTS; PR00079; G6PDHDRGNASE.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00871; zwf; 1.
DR PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Carbohydrate metabolism; Cytoplasm; Direct protein sequencing;
KW Glucose metabolism; Membrane; NADP; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P05370"
FT CHAIN 2..515
FT /note="Glucose-6-phosphate 1-dehydrogenase X"
FT /id="PRO_0000068085"
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 BINDING 509
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:P05370"
FT MOD_RES 507
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT CONFLICT 24
FT /note="D -> Y (in Ref. 3; CAA37679)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 515 AA; 59263 MW; C8AF0D4099B7AEC3 CRC64;
MAEQVALSRT QVCGILREEL YQGDAFHQAD THIFIIMGAS GDLAKKKIYP TIWWLFRDGL
LPEDTFIVGY ARSRLTVDDI RKQSEPFFKA TPEERPKLEE FFARNSYVAG QYDDAASYKH
LNSHMNALHQ GMQANRLFYL ALPPTVYEAV TKNIQETCMS QTGWNRIIVE KPFGRDLQSS
NQLSNHISSL FREDQIYRID HYLGKEMVQN LMVLRFANRI FGPIWNRDNI ACVILTFKEP
FGTEGRGGYF DEFGIIRDVM QNHLLQMLCL VAMEKPATTG SDDVRDEKVK VLKCISEVET
DNVVLGQYVG NPNGEGEAAN GYLDDPTVPH GSTTATFAAA VLYVENERWD GVPFILRCGK
ALNERKAEVR LQFRDVAGDI FHQQCKRNEL VIRVQPNEAV YTKMMTKKPG MFFNPEESEL
DLTYGNRYKN VKLPDAYERL ILDVFCGSQM HFVRSDELRE AWRIFTPLLH KIDREKPQPI
PYVYGSRGPT EADELMKRVG FQYEGTYKWV NPHKL
