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Glucose-6-phosphate 1-dehydrogenase X (G6PD) (EC 1.1.1.49)

 G6PD1_MOUSE             Reviewed;         515 AA.
Q00612;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
20-MAR-2007, sequence version 3.
20-JUN-2018, entry version 165.
RecName: Full=Glucose-6-phosphate 1-dehydrogenase X;
Short=G6PD;
EC=1.1.1.49;
Name=G6pdx; Synonyms=G6pd, G6pd-1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8400362; DOI=10.3109/10425179309020830;
Zollo M.Z., D'Urso M., Schlessinger D., Chen E.Y.;
"Sequence of mouse glucose-6-phosphate dehydrogenase cDNA.";
DNA Seq. 3:319-322(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=NOD; TISSUE=Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
STRAIN=BALB/cJ;
PubMed=1874446; DOI=10.1016/0378-1119(91)90078-P;
Toniolo D., Filippi M., Dono R., Lettieri T., Martini G.;
"The CpG island in the 5' region of the G6PD gene of man and mouse.";
Gene 102:197-203(1991).
[4]
PROTEIN SEQUENCE OF 57-71; 175-191 AND 247-257, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=Brain, and Hippocampus;
Lubec G., Klug S., Yang J.W., Zigmond M.;
Submitted (JUL-2007) to UniProtKB.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 163-214 AND 352-454.
STRAIN=BALB/cJ;
PubMed=9330624; DOI=10.1016/S0027-5107(97)00109-7;
Kuraguchi M., Thomas G.A., Williams E.D.;
"Somatic mutation of the glucose-6-phosphate dehydrogenase (g6pd) gene
in colonic stem cells and crypt restricted loss of G6PD activity.";
Mutat. Res. 379:69-75(1997).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-507, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Mast cell;
PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell
signaling.";
J. Immunol. 179:5864-5876(2007).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Catalyzes the rate-limiting step of the oxidative
pentose-phosphate pathway, which represents a route for the
dissimilation of carbohydrates besides glycolysis. The main
function of this enzyme is to provide reducing power (NADPH) and
pentose phosphates for fatty acid and nucleic acid synthesis (By
similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-
glucono-1,5-lactone + NADPH.
-!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage):
step 1/3.
-!- SUBUNIT: Homotetramer; dimer of dimers. Interacts with SIRT2; the
interaction is enhanced by H(2)O(2) treatment (By similarity).
{ECO:0000250}.
-!- PTM: Acetylated by ELP3 at Lys-403; acetylation inhibits its
homodimerization and enzyme activity. Deacetylated by SIRT2 at
Lys-403; deacetylation stimulates its enzyme activity (By
similarity). {ECO:0000250}.
-!- MISCELLANEOUS: Has NADP both as cofactor (bound to the N-terminal
domain) and as structural element bound to the C-terminal domain.
-!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase
family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; Z11911; CAA77967.1; -; mRNA.
EMBL; AK088135; BAC40166.1; -; mRNA.
EMBL; X53617; CAA37679.1; -; Genomic_DNA.
EMBL; U88533; AAB52998.1; -; Genomic_DNA.
EMBL; U88534; AAB52999.1; -; Genomic_DNA.
CCDS; CCDS30232.1; -.
PIR; A56686; A56686.
RefSeq; NP_032088.1; NM_008062.2.
UniGene; Mm.27210; -.
ProteinModelPortal; Q00612; -.
SMR; Q00612; -.
BioGrid; 199790; 2.
IntAct; Q00612; 3.
MINT; Q00612; -.
STRING; 10090.ENSMUSP00000004327; -.
iPTMnet; Q00612; -.
PhosphoSitePlus; Q00612; -.
SwissPalm; Q00612; -.
REPRODUCTION-2DPAGE; IPI00228385; -.
REPRODUCTION-2DPAGE; Q00612; -.
EPD; Q00612; -.
PaxDb; Q00612; -.
PeptideAtlas; Q00612; -.
PRIDE; Q00612; -.
Ensembl; ENSMUST00000004327; ENSMUSP00000004327; ENSMUSG00000031400.
GeneID; 14381; -.
KEGG; mmu:14381; -.
UCSC; uc009toy.1; mouse.
CTD; 14381; -.
MGI; MGI:105979; G6pdx.
eggNOG; KOG0563; Eukaryota.
eggNOG; COG0364; LUCA.
GeneTree; ENSGT00530000063435; -.
HOGENOM; HOG000046192; -.
HOVERGEN; HBG000856; -.
InParanoid; Q00612; -.
KO; K00036; -.
OMA; VEICVYE; -.
OrthoDB; EOG091G06FN; -.
PhylomeDB; Q00612; -.
TreeFam; TF300584; -.
Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-MMU-71336; Pentose phosphate pathway (hexose monophosphate shunt).
UniPathway; UPA00115; UER00408.
PRO; PR:Q00612; -.
Proteomes; UP000000589; Chromosome X.
Bgee; ENSMUSG00000031400; -.
CleanEx; MM_G6PDX; -.
ExpressionAtlas; Q00612; baseline and differential.
Genevisible; Q00612; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0030246; F:carbohydrate binding; ISO:MGI.
GO; GO:0005536; F:glucose binding; ISO:MGI.
GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IDA:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0050661; F:NADP binding; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; IPI:MGI.
GO; GO:0001998; P:angiotensin-mediated vasoconstriction involved in regulation of systemic arterial blood pressure; IMP:MGI.
GO; GO:0002033; P:angiotensin-mediated vasodilation involved in regulation of systemic arterial blood pressure; IMP:MGI.
GO; GO:0034599; P:cellular response to oxidative stress; ISO:MGI.
GO; GO:0006695; P:cholesterol biosynthetic process; ISO:MGI.
GO; GO:0001816; P:cytokine production; IMP:MGI.
GO; GO:0048821; P:erythrocyte development; IMP:MGI.
GO; GO:0043249; P:erythrocyte maturation; ISO:MGI.
GO; GO:0051156; P:glucose 6-phosphate metabolic process; ISS:UniProtKB.
GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
GO; GO:0006749; P:glutathione metabolic process; IMP:MGI.
GO; GO:0032613; P:interleukin-10 production; IMP:MGI.
GO; GO:0032615; P:interleukin-12 production; IMP:MGI.
GO; GO:0006741; P:NADP biosynthetic process; IDA:MGI.
GO; GO:0006739; P:NADP metabolic process; ISS:UniProtKB.
GO; GO:0006740; P:NADPH regeneration; ISO:MGI.
GO; GO:0061052; P:negative regulation of cell growth involved in cardiac muscle cell development; ISO:MGI.
GO; GO:0010734; P:negative regulation of protein glutathionylation; ISO:MGI.
GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; ISO:MGI.
GO; GO:0055114; P:oxidation-reduction process; ISO:MGI.
GO; GO:0019322; P:pentose biosynthetic process; IDA:MGI.
GO; GO:0006098; P:pentose-phosphate shunt; ISO:MGI.
GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; ISO:MGI.
GO; GO:1904879; P:positive regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; ISO:MGI.
GO; GO:0040014; P:regulation of multicellular organism growth; IMP:MGI.
GO; GO:0043523; P:regulation of neuron apoptotic process; ISO:MGI.
GO; GO:0045471; P:response to ethanol; ISO:MGI.
GO; GO:0006979; P:response to oxidative stress; IMP:MGI.
GO; GO:0046390; P:ribose phosphate biosynthetic process; ISO:MGI.
HAMAP; MF_00966; G6PD; 1.
InterPro; IPR001282; G6P_DH.
InterPro; IPR019796; G6P_DH_AS.
InterPro; IPR022675; G6P_DH_C.
InterPro; IPR022674; G6P_DH_NAD-bd.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
PANTHER; PTHR23429; PTHR23429; 1.
Pfam; PF02781; G6PD_C; 1.
Pfam; PF00479; G6PD_N; 1.
PIRSF; PIRSF000110; G6PD; 1.
PRINTS; PR00079; G6PDHDRGNASE.
SUPFAM; SSF51735; SSF51735; 1.
TIGRFAMs; TIGR00871; zwf; 1.
PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
1: Evidence at protein level;
Acetylation; Carbohydrate metabolism; Complete proteome;
Direct protein sequencing; Glucose metabolism; NADP; Oxidoreductase;
Phosphoprotein; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P05370}.
CHAIN 2 515 Glucose-6-phosphate 1-dehydrogenase X.
/FTId=PRO_0000068085.
NP_BIND 38 45 NADP 1. {ECO:0000250}.
NP_BIND 401 403 NADP 2. {ECO:0000250}.
NP_BIND 421 423 NADP 2. {ECO:0000250}.
REGION 201 205 Substrate binding. {ECO:0000250}.
ACT_SITE 263 263 Proton acceptor. {ECO:0000250}.
BINDING 72 72 NADP 1. {ECO:0000250}.
BINDING 147 147 NADP 1. {ECO:0000250}.
BINDING 171 171 NADP 1; via carbonyl oxygen.
{ECO:0000250}.
BINDING 171 171 Substrate. {ECO:0000250}.
BINDING 239 239 Substrate. {ECO:0000250}.
BINDING 258 258 Substrate. {ECO:0000250}.
BINDING 357 357 NADP 2. {ECO:0000250}.
BINDING 360 360 Substrate. {ECO:0000250}.
BINDING 365 365 Substrate. {ECO:0000250}.
BINDING 366 366 NADP 2. {ECO:0000250}.
BINDING 370 370 NADP 2. {ECO:0000250}.
BINDING 393 393 NADP 2. {ECO:0000250}.
BINDING 395 395 Substrate. {ECO:0000250}.
BINDING 487 487 NADP 2. {ECO:0000250}.
BINDING 503 503 NADP 2. {ECO:0000250}.
BINDING 509 509 NADP 2. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P05370}.
MOD_RES 507 507 Phosphotyrosine.
{ECO:0000244|PubMed:17947660}.
CONFLICT 24 24 D -> Y (in Ref. 3; CAA37679).
{ECO:0000305}.
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


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