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Protein

Glucose-6-phosphate 1-dehydrogenase X

Gene

G6pdx

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

D-glucose 6-phosphate + NADP+ = 6-phospho-D-glucono-1,5-lactone + NADPH.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei72 – 721NADP 1By similarity
Binding sitei147 – 1471NADP 1By similarity
Binding sitei171 – 1711NADP 1; via carbonyl oxygenBy similarity
Binding sitei171 – 1711SubstrateBy similarity
Binding sitei239 – 2391SubstrateBy similarity
Binding sitei258 – 2581SubstrateBy similarity
Active sitei263 – 2631Proton acceptorBy similarity
Binding sitei357 – 3571NADP 2By similarity
Binding sitei360 – 3601SubstrateBy similarity
Binding sitei365 – 3651SubstrateBy similarity
Binding sitei366 – 3661NADP 2By similarity
Binding sitei370 – 3701NADP 2By similarity
Binding sitei393 – 3931NADP 2By similarity
Binding sitei395 – 3951SubstrateBy similarity
Binding sitei487 – 4871NADP 2By similarity
Binding sitei503 – 5031NADP 2By similarity
Binding sitei509 – 5091NADP 2By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi38 – 458NADP 1By similarity
Nucleotide bindingi401 – 4033NADP 2By similarity
Nucleotide bindingi421 – 4233NADP 2By similarity

GO - Molecular functioni

  1. glucose-6-phosphate dehydrogenase activity Source: MGI
  2. glucose binding Source: MGI
  3. identical protein binding Source: MGI
  4. NADP binding Source: MGI
  5. protein homodimerization activity Source: MGI

GO - Biological processi

  1. angiotensin mediated vasoconstriction involved in regulation of systemic arterial blood pressure Source: MGI
  2. cellular response to oxidative stress Source: MGI
  3. cholesterol biosynthetic process Source: MGI
  4. cytokine production Source: MGI
  5. erythrocyte development Source: MGI
  6. erythrocyte maturation Source: MGI
  7. glucose 6-phosphate metabolic process Source: UniProtKB
  8. glucose metabolic process Source: UniProtKB-KW
  9. glutathione metabolic process Source: MGI
  10. interleukin-10 production Source: MGI
  11. interleukin-12 production Source: MGI
  12. NADP biosynthetic process Source: MGI
  13. NADPH regeneration Source: MGI
  14. NADP metabolic process Source: UniProtKB
  15. negative regulation of protein glutathionylation Source: MGI
  16. oxidation-reduction process Source: MGI
  17. pentose biosynthetic process Source: MGI
  18. pentose-phosphate shunt Source: MGI
  19. pentose-phosphate shunt, oxidative branch Source: MGI
  20. regulation of multicellular organism growth Source: MGI
  21. response to oxidative stress Source: MGI
  22. ribose phosphate biosynthetic process Source: MGI
  23. vasodilation by angiotensin involved in regulation of systemic arterial blood pressure Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

ReactomeiREACT_328939. Pentose phosphate pathway (hexose monophosphate shunt).
UniPathwayiUPA00115; UER00408.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucose-6-phosphate 1-dehydrogenase X (EC:1.1.1.49)
Short name:
G6PD
Gene namesi
Name:G6pdx
Synonyms:G6pd, G6pd-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:105979. G6pdx.

Subcellular locationi

GO - Cellular componenti

  1. centrosome Source: MGI
  2. cytoplasm Source: MGI
  3. cytoplasmic side of plasma membrane Source: MGI
  4. cytosol Source: MGI
  5. extracellular vesicular exosome Source: MGI
  6. intracellular membrane-bounded organelle Source: MGI
  7. membrane Source: MGI
  8. microtubule organizing center Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 515514Glucose-6-phosphate 1-dehydrogenase XPRO_0000068085Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei507 – 5071Phosphotyrosine1 Publication

Post-translational modificationi

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).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ00612.
PaxDbiQ00612.
PRIDEiQ00612.

2D gel databases

REPRODUCTION-2DPAGEIPI00228385.
Q00612.

PTM databases

PhosphoSiteiQ00612.

Expressioni

Gene expression databases

BgeeiQ00612.
CleanExiMM_G6PDX.
ExpressionAtlasiQ00612. baseline and differential.
GenevestigatoriQ00612.

Interactioni

Subunit structurei

Homotetramer; dimer of dimers. Interacts with SIRT2; the interaction is enhanced by H2O2 treatment (By similarity).By similarity

Protein-protein interaction databases

IntActiQ00612. 3 interactions.
MINTiMINT-4095477.

Structurei

3D structure databases

ProteinModelPortaliQ00612.
SMRiQ00612. Positions 28-515.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni201 – 2055Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0364.
HOGENOMiHOG000046192.
HOVERGENiHBG000856.
InParanoidiQ00612.
KOiK00036.
OMAiHNLQTTK.
OrthoDBiEOG7DRJ2T.
PhylomeDBiQ00612.
TreeFamiTF300584.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00966. G6PD.
InterProiIPR001282. G6P_DH.
IPR019796. G6P_DH_AS.
IPR022675. G6P_DH_C.
IPR022674. G6P_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR23429. PTHR23429. 1 hit.
PfamiPF02781. G6PD_C. 1 hit.
PF00479. G6PD_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000110. G6PD. 1 hit.
PRINTSiPR00079. G6PDHDRGNASE.
TIGRFAMsiTIGR00871. zwf. 1 hit.
PROSITEiPS00069. G6P_DEHYDROGENASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q00612-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEQVALSRT QVCGILREEL YQGDAFHQAD THIFIIMGAS GDLAKKKIYP
60 70 80 90 100
TIWWLFRDGL LPEDTFIVGY ARSRLTVDDI RKQSEPFFKA TPEERPKLEE
110 120 130 140 150
FFARNSYVAG QYDDAASYKH LNSHMNALHQ GMQANRLFYL ALPPTVYEAV
160 170 180 190 200
TKNIQETCMS QTGWNRIIVE KPFGRDLQSS NQLSNHISSL FREDQIYRID
210 220 230 240 250
HYLGKEMVQN LMVLRFANRI FGPIWNRDNI ACVILTFKEP FGTEGRGGYF
260 270 280 290 300
DEFGIIRDVM QNHLLQMLCL VAMEKPATTG SDDVRDEKVK VLKCISEVET
310 320 330 340 350
DNVVLGQYVG NPNGEGEAAN GYLDDPTVPH GSTTATFAAA VLYVENERWD
360 370 380 390 400
GVPFILRCGK ALNERKAEVR LQFRDVAGDI FHQQCKRNEL VIRVQPNEAV
410 420 430 440 450
YTKMMTKKPG MFFNPEESEL DLTYGNRYKN VKLPDAYERL ILDVFCGSQM
460 470 480 490 500
HFVRSDELRE AWRIFTPLLH KIDREKPQPI PYVYGSRGPT EADELMKRVG
510
FQYEGTYKWV NPHKL
Length:515
Mass (Da):59,263
Last modified:March 19, 2007 - v3
Checksum:iC8AF0D4099B7AEC3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 241D → Y in CAA37679 (PubMed:1874446).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11911 mRNA. Translation: CAA77967.1.
AK088135 mRNA. Translation: BAC40166.1.
X53617 Genomic DNA. Translation: CAA37679.1.
U88533 Genomic DNA. Translation: AAB52998.1.
U88534 Genomic DNA. Translation: AAB52999.1.
CCDSiCCDS30232.1.
PIRiA56686.
RefSeqiNP_032088.1. NM_008062.2.
UniGeneiMm.27210.

Genome annotation databases

EnsembliENSMUST00000004327; ENSMUSP00000004327; ENSMUSG00000031400.
GeneIDi14381.
KEGGimmu:14381.
UCSCiuc009toy.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11911 mRNA. Translation: CAA77967.1.
AK088135 mRNA. Translation: BAC40166.1.
X53617 Genomic DNA. Translation: CAA37679.1.
U88533 Genomic DNA. Translation: AAB52998.1.
U88534 Genomic DNA. Translation: AAB52999.1.
CCDSiCCDS30232.1.
PIRiA56686.
RefSeqiNP_032088.1. NM_008062.2.
UniGeneiMm.27210.

3D structure databases

ProteinModelPortaliQ00612.
SMRiQ00612. Positions 28-515.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ00612. 3 interactions.
MINTiMINT-4095477.

PTM databases

PhosphoSiteiQ00612.

2D gel databases

REPRODUCTION-2DPAGEIPI00228385.
Q00612.

Proteomic databases

MaxQBiQ00612.
PaxDbiQ00612.
PRIDEiQ00612.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000004327; ENSMUSP00000004327; ENSMUSG00000031400.
GeneIDi14381.
KEGGimmu:14381.
UCSCiuc009toy.1. mouse.

Organism-specific databases

CTDi14381.
MGIiMGI:105979. G6pdx.

Phylogenomic databases

eggNOGiCOG0364.
HOGENOMiHOG000046192.
HOVERGENiHBG000856.
InParanoidiQ00612.
KOiK00036.
OMAiHNLQTTK.
OrthoDBiEOG7DRJ2T.
PhylomeDBiQ00612.
TreeFamiTF300584.

Enzyme and pathway databases

UniPathwayiUPA00115; UER00408.
ReactomeiREACT_328939. Pentose phosphate pathway (hexose monophosphate shunt).

Miscellaneous databases

NextBioi285893.
PROiQ00612.
SOURCEiSearch...

Gene expression databases

BgeeiQ00612.
CleanExiMM_G6PDX.
ExpressionAtlasiQ00612. baseline and differential.
GenevestigatoriQ00612.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00966. G6PD.
InterProiIPR001282. G6P_DH.
IPR019796. G6P_DH_AS.
IPR022675. G6P_DH_C.
IPR022674. G6P_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR23429. PTHR23429. 1 hit.
PfamiPF02781. G6PD_C. 1 hit.
PF00479. G6PD_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000110. G6PD. 1 hit.
PRINTSiPR00079. G6PDHDRGNASE.
TIGRFAMsiTIGR00871. zwf. 1 hit.
PROSITEiPS00069. G6P_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of mouse glucose-6-phosphate dehydrogenase cDNA."
    Zollo M.Z., D'Urso M., Schlessinger D., Chen E.Y.
    DNA Seq. 3:319-322(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: NOD.
    Tissue: Thymus.
  3. "The CpG island in the 5' region of the G6PD gene of man and mouse."
    Toniolo D., Filippi M., Dono R., Lettieri T., Martini G.
    Gene 102:197-203(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
    Strain: BALB/c.
  4. Lubec G., Klug S., Yang J.W., Zigmond M.
    Submitted (JUN-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 57-71; 175-191 AND 247-257, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Hippocampus.
  5. "Somatic mutation of the glucose-6-phosphate dehydrogenase (g6pd) gene in colonic stem cells and crypt restricted loss of G6PD activity."
    Kuraguchi M., Thomas G.A., Williams E.D.
    Mutat. Res. 379:69-75(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 163-214 AND 352-454.
    Strain: BALB/c.
  6. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-507, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.

Entry informationi

Entry nameiG6PD1_MOUSE
AccessioniPrimary (citable) accession number: Q00612
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 31, 1993
Last sequence update: March 19, 2007
Last modified: March 31, 2015
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Has NADP both as cofactor (bound to the N-terminal domain) and as structural element bound to the C-terminal domain.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.