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Q00612

- G6PD1_MOUSE

UniProt

Q00612 - G6PD1_MOUSE

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Protein

Glucose-6-phosphate 1-dehydrogenase X

Gene

G6pdx

Organism
Mus musculus (Mouse)
Status
Reviewed - 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. NADP binding Source: InterPro
  3. protein homodimerization activity Source: MGI

GO - Biological processi

  1. angiotensin mediated vasoconstriction involved in regulation of systemic arterial blood pressure Source: MGI
  2. cytokine production Source: MGI
  3. erythrocyte development Source: MGI
  4. glucose 6-phosphate metabolic process Source: UniProtKB
  5. glutathione metabolic process Source: MGI
  6. interleukin-10 production Source: MGI
  7. interleukin-12 production Source: MGI
  8. NADP biosynthetic process Source: MGI
  9. NADP metabolic process Source: UniProtKB
  10. pentose biosynthetic process Source: MGI
  11. pentose-phosphate shunt Source: UniProtKB-UniPathway
  12. regulation of multicellular organism growth Source: MGI
  13. response to oxidative stress Source: MGI
  14. 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

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: Chromosome X

Organism-specific databases

MGIiMGI:105979. G6pdx.

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 residuei403 – 4031N6-acetyllysineBy 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.
OMAiHAFTESS.
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 20, 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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS30232.1.
PIRi A56686.
RefSeqi NP_032088.1. NM_008062.2.
UniGenei Mm.27210.

3D structure databases

ProteinModelPortali Q00612.
SMRi Q00612. Positions 28-515.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q00612. 3 interactions.
MINTi MINT-4095477.

PTM databases

PhosphoSitei Q00612.

2D gel databases

REPRODUCTION-2DPAGE IPI00228385.
Q00612.

Proteomic databases

MaxQBi Q00612.
PaxDbi Q00612.
PRIDEi Q00612.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000004327 ; ENSMUSP00000004327 ; ENSMUSG00000031400 .
GeneIDi 14381.
KEGGi mmu:14381.
UCSCi uc009toy.1. mouse.

Organism-specific databases

CTDi 14381.
MGIi MGI:105979. G6pdx.

Phylogenomic databases

eggNOGi COG0364.
HOGENOMi HOG000046192.
HOVERGENi HBG000856.
InParanoidi Q00612.
KOi K00036.
OMAi HAFTESS.
OrthoDBi EOG7DRJ2T.
PhylomeDBi Q00612.
TreeFami TF300584.

Enzyme and pathway databases

UniPathwayi UPA00115 ; UER00408 .

Miscellaneous databases

NextBioi 285893.
PROi Q00612.
SOURCEi Search...

Gene expression databases

Bgeei Q00612.
CleanExi MM_G6PDX.
ExpressionAtlasi Q00612. baseline and differential.
Genevestigatori Q00612.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
HAMAPi MF_00966. G6PD.
InterProi IPR001282. G6P_DH.
IPR019796. G6P_DH_AS.
IPR022675. G6P_DH_C.
IPR022674. G6P_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
PANTHERi PTHR23429. PTHR23429. 1 hit.
Pfami PF02781. G6PD_C. 1 hit.
PF00479. G6PD_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000110. G6PD. 1 hit.
PRINTSi PR00079. G6PDHDRGNASE.
TIGRFAMsi TIGR00871. zwf. 1 hit.
PROSITEi PS00069. G6P_DEHYDROGENASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1993) [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(2005) [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(1991) [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 (JUL-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(1997) [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(2007) [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: April 1, 1993
Last sequence update: March 20, 2007
Last modified: October 29, 2014
This is version 136 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