G6PD2_MOUSE
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 03-AUG-2022, entry version 159.
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 iPTMnet; P97324; -.
DR PhosphoSitePlus; P97324; -.
DR jPOST; P97324; -.
DR MaxQB; P97324; -.
DR PaxDb; P97324; -.
DR PeptideAtlas; P97324; -.
DR PRIDE; P97324; -.
DR ProteomicsDB; 267551; -.
DR DNASU; 14380; -.
DR GeneID; 14380; -.
DR KEGG; mmu:14380; -.
DR CTD; 14380; -.
DR MGI; MGI:105977; G6pd2.
DR eggNOG; KOG0563; Eukaryota.
DR InParanoid; P97324; -.
DR OrthoDB; 383995at2759; -.
DR UniPathway; UPA00115; UER00408.
DR BioGRID-ORCS; 14380; 5 hits in 73 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: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; 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 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; 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.
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
