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

 G6PD_RAT                Reviewed;         515 AA.
P05370;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
22-NOV-2017, entry version 161.
RecName: Full=Glucose-6-phosphate 1-dehydrogenase;
Short=G6PD;
EC=1.1.1.49;
Name=G6pdx; Synonyms=G6pd;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=3412913; DOI=10.1093/nar/16.15.7746;
Ho Y., Howard A.J., Crapo J.D.;
"Cloning and sequence of a cDNA encoding rat glucose-6-phosphate
dehydrogenase.";
Nucleic Acids Res. 16:7746-7746(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 2-514, CLEAVAGE OF INITIATOR METHIONINE, AND
ACETYLATION AT ALA-2.
STRAIN=Wistar; TISSUE=Liver;
PubMed=2606104; DOI=10.1111/j.1432-1033.1989.tb15242.x;
Jeffery J., Barros-Soederling J., Murray L., Wood I., Hansen R.,
Szepesi B., Joernvall H.;
"Glucose-6-phosphate dehydrogenase. Characteristics revealed by the
rat liver enzyme structure.";
Eur. J. Biochem. 186:551-556(1989).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-515.
Fritz R.S., Kletzien R.F.;
Submitted (NOV-1989) to the EMBL/GenBank/DDBJ databases.
[5]
PROTEIN SEQUENCE OF 58-72; 176-192 AND 228-257, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
Lubec G., Afjehi-Sadat L.;
Submitted (NOV-2006) to UniProtKB.
-!- 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; X07467; CAA30355.1; -; mRNA.
EMBL; BC081820; AAH81820.1; -; mRNA.
EMBL; M26655; AAA41179.1; -; Genomic_DNA.
EMBL; M26653; AAA41179.1; JOINED; Genomic_DNA.
EMBL; M26654; AAA41179.1; JOINED; Genomic_DNA.
PIR; S01233; S01233.
RefSeq; NP_058702.1; NM_017006.2.
UniGene; Rn.11040; -.
ProteinModelPortal; P05370; -.
SMR; P05370; -.
BioGrid; 246548; 1.
STRING; 10116.ENSRNOP00000053157; -.
iPTMnet; P05370; -.
PhosphoSitePlus; P05370; -.
World-2DPAGE; 0004:P05370; -.
PaxDb; P05370; -.
PRIDE; P05370; -.
Ensembl; ENSRNOT00000080887; ENSRNOP00000075297; ENSRNOG00000056728.
GeneID; 24377; -.
KEGG; rno:24377; -.
CTD; 2539; -.
RGD; 2645; G6pdx.
eggNOG; KOG0563; Eukaryota.
eggNOG; COG0364; LUCA.
GeneTree; ENSGT00530000063435; -.
HOGENOM; HOG000046192; -.
HOVERGEN; HBG000856; -.
InParanoid; P05370; -.
KO; K00036; -.
OMA; VEICVYE; -.
OrthoDB; EOG091G06FN; -.
PhylomeDB; P05370; -.
TreeFam; TF300584; -.
Reactome; R-RNO-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-RNO-71336; Pentose phosphate pathway (hexose monophosphate shunt).
SABIO-RK; P05370; -.
UniPathway; UPA00115; UER00408.
PRO; PR:P05370; -.
Proteomes; UP000002494; Chromosome X.
Bgee; ENSRNOG00000056728; -.
Genevisible; P05370; RN.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0030246; F:carbohydrate binding; IDA:RGD.
GO; GO:0005536; F:glucose binding; IDA:RGD.
GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IDA:CACAO.
GO; GO:0042802; F:identical protein binding; ISO:RGD.
GO; GO:0050661; F:NADP binding; IDA:RGD.
GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
GO; GO:0001998; P:angiotensin-mediated vasoconstriction involved in regulation of systemic arterial blood pressure; ISO:RGD.
GO; GO:0002033; P:angiotensin-mediated vasodilation involved in regulation of systemic arterial blood pressure; ISO:RGD.
GO; GO:0034599; P:cellular response to oxidative stress; ISO:RGD.
GO; GO:0006695; P:cholesterol biosynthetic process; ISO:RGD.
GO; GO:0001816; P:cytokine production; ISO:RGD.
GO; GO:0048821; P:erythrocyte development; ISO:RGD.
GO; GO:0043249; P:erythrocyte maturation; ISO:RGD.
GO; GO:0051156; P:glucose 6-phosphate metabolic process; IDA:RGD.
GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
GO; GO:0006749; P:glutathione metabolic process; ISO:RGD.
GO; GO:0032613; P:interleukin-10 production; ISO:RGD.
GO; GO:0032615; P:interleukin-12 production; ISO:RGD.
GO; GO:0006741; P:NADP biosynthetic process; ISO:RGD.
GO; GO:0006739; P:NADP metabolic process; ISS:UniProtKB.
GO; GO:0006740; P:NADPH regeneration; ISO:RGD.
GO; GO:0061052; P:negative regulation of cell growth involved in cardiac muscle cell development; IMP:RGD.
GO; GO:0010734; P:negative regulation of protein glutathionylation; ISO:RGD.
GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IMP:RGD.
GO; GO:0055114; P:oxidation-reduction process; ISO:RGD.
GO; GO:0019322; P:pentose biosynthetic process; ISO:RGD.
GO; GO:0006098; P:pentose-phosphate shunt; IDA:RGD.
GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IMP:RGD.
GO; GO:1904879; P:positive regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; IMP:RGD.
GO; GO:0040014; P:regulation of multicellular organism growth; ISO:RGD.
GO; GO:0043523; P:regulation of neuron apoptotic process; IDA:RGD.
GO; GO:0045471; P:response to ethanol; IDA:RGD.
GO; GO:0032094; P:response to food; IEP:RGD.
GO; GO:0010041; P:response to iron(III) ion; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0006979; P:response to oxidative stress; ISO:RGD.
GO; GO:0046390; P:ribose phosphate biosynthetic process; ISO:RGD.
GO; GO:0021762; P:substantia nigra development; ISO:RGD.
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:0000269|PubMed:2606104}.
CHAIN 2 515 Glucose-6-phosphate 1-dehydrogenase.
/FTId=PRO_0000068087.
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:0000269|PubMed:2606104}.
MOD_RES 8 8 Phosphoserine.
{ECO:0000250|UniProtKB:P11413}.
MOD_RES 10 10 Phosphothreonine.
{ECO:0000250|UniProtKB:P11413}.
MOD_RES 89 89 N6-acetyllysine.
{ECO:0000250|UniProtKB:P11413}.
MOD_RES 171 171 N6-acetyllysine.
{ECO:0000250|UniProtKB:P11413}.
MOD_RES 403 403 N6-acetyllysine.
{ECO:0000250|UniProtKB:P11413}.
MOD_RES 432 432 N6-acetyllysine.
{ECO:0000250|UniProtKB:P11413}.
MOD_RES 497 497 N6-acetyllysine.
{ECO:0000250|UniProtKB:P11413}.
MOD_RES 503 503 Phosphotyrosine.
{ECO:0000250|UniProtKB:P11413}.
CONFLICT 320 320 N -> D (in Ref. 3; AA sequence).
{ECO:0000305}.
SEQUENCE 515 AA; 59376 MW; 8E92FFF3BF5A959B CRC64;
MAEQVALSRT QVCGILREEL YQGDAFHQAD THIFIIMGAS GDLAKKKIYP TIWWLFRDGL
LPEDTFIVGY ARSRLTVDDI RKQSEPFFKV TPEERPKLEE FFARNSYVAG QYDDPASYKH
LNSHMNALHQ GMQANRLFYL ALPPTVYEAV TKNIQEICMS QTGWNRIIVE KPFGRDLQSS
NQLSNHISSL FREDQIYRID HYLGKEMVQN LMVLRFANRI FGPIWNRDNI ACVILTFKEP
FGTEGRGGYF DEFGIIRDVM QNHLLQMLCL VAMEKPASTD SDDVRDEKVK VLKCISEVET
DNVVLGQYVG NPSGEGEATN GYLDDPTVPH GSTTATFAAA VLYVENERWD GVPFILRCGK
ALNERKAEVR LQFRDVAGDI FHQQCKRNEL VIRVQPNEAV YTKMMTKKPG MFFNPEESEL
DLTYGNRYKN VKLPDAYERL ILDVFCGSQM HFVRSDELRE AWRIFTPLLH KIDREKPQPI
PYVYGSRGPT EADELMKRVG FQYEGTYKWV NPHKL


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