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Reviewed, UniProtKB/Swiss-Prot Q00612 (G6PD1_MOUSE)

Last modified November 25, 2008. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glucose-6-phosphate 1-dehydrogenase X
      Short name=G6PD
    EC=1.1.1.49
Gene names
Name: G6pdx
Synonyms: G6pd, G6pd-1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length515 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

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

Pathway

Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.

Miscellaneous

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

Sequence similarities

Belongs to the glucose-6-phosphate dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 515514Glucose-6-phosphate 1-dehydrogenase X
PRO_0000068085

Sites

Active site2631Proton acceptor By similarity
Binding site401NADP By similarity
Binding site721NADP By similarity
Binding site2011Substrate By similarity
Binding site2051Substrate By similarity
Binding site2381NADP By similarity
Binding site3571NADP By similarity
Binding site4871NADP By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue4011Phosphotyrosine
Modified residue5031Phosphotyrosine
Modified residue5071Phosphotyrosine

Experimental info

Sequence conflict241D → Y in CAA37679. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q00612-1 [UniParc].

Last modified March 20, 2007. Version 3.
Checksum: C8AF0D4099B7AEC3

FASTA51559,263
        10         20         30         40         50         60 
MAEQVALSRT QVCGILREEL YQGDAFHQAD THIFIIMGAS GDLAKKKIYP TIWWLFRDGL 

        70         80         90        100        110        120 
LPEDTFIVGY ARSRLTVDDI RKQSEPFFKA TPEERPKLEE FFARNSYVAG QYDDAASYKH 

       130        140        150        160        170        180 
LNSHMNALHQ GMQANRLFYL ALPPTVYEAV TKNIQETCMS QTGWNRIIVE KPFGRDLQSS 

       190        200        210        220        230        240 
NQLSNHISSL FREDQIYRID HYLGKEMVQN LMVLRFANRI FGPIWNRDNI ACVILTFKEP 

       250        260        270        280        290        300 
FGTEGRGGYF DEFGIIRDVM QNHLLQMLCL VAMEKPATTG SDDVRDEKVK VLKCISEVET 

       310        320        330        340        350        360 
DNVVLGQYVG NPNGEGEAAN GYLDDPTVPH GSTTATFAAA VLYVENERWD GVPFILRCGK 

       370        380        390        400        410        420 
ALNERKAEVR LQFRDVAGDI FHQQCKRNEL VIRVQPNEAV YTKMMTKKPG MFFNPEESEL 

       430        440        450        460        470        480 
DLTYGNRYKN VKLPDAYERL ILDVFCGSQM HFVRSDELRE AWRIFTPLLH KIDREKPQPI 

       490        500        510 
PYVYGSRGPT EADELMKRVG FQYEGTYKWV NPHKL 

« Hide

References

« Hide 'large scale' references
[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: 8400362] [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. expand/collapse author list , 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: 16141072] [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: 1874446] [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, 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: 9330624] [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: 17947660] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-507, MASS SPECTROMETRY.
Tissue: Mast cell.
[7]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-401; TYR-503 AND TYR-507, MASS SPECTROMETRY.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
PIRA56686.
RefSeqNP_032088.1.
UniGeneMm.27210

3D structure databases

HSSPHSSP built from PDB template 1QKI based on UniProtKB P11413.
SMRQ00612. Positions 28-515.
ModBaseSearch...

Protein-protein interaction databases

IntActQ00612.

PTM databases

PhosphoSiteQ00612.

2-D gel databases

REPRODUCTION-2DPAGEQ00612.

Genome annotation databases

EnsemblENSMUSG00000031400. Mus musculus. [Contig view]
GeneID14381.
KEGGmmu:14381.

Organism-specific databases

MGIMGI:105979. G6pdx.

Phylogenomic databases

HOGENOMQ00612.
HOVERGENQ00612.

Gene expression databases

ArrayExpressQ00612.
CleanExMM_G6PDX.
GermOnlineENSMUSG00000031400. Mus musculus.

Family and domain databases

InterProIPR001282. Glc-6-P_DHase.
IPR016040. NAD(P)-bd.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR23429. G6PDH. 1 hit.
PfamPF02781. G6PD_C. 1 hit.
PF00479. G6PD_N. 1 hit.
[Graphical view]
PIRSFPIRSF000110. G6PD. 1 hit.
PRINTSPR00079. G6PDHDRGNASE.
ProDomPD001129. G6PD. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00871. zwf. 1 hit.
PROSITEPS00069. G6P_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio285893.
SOURCESearch...

Entry information

Entry nameG6PD1_MOUSE
AccessionPrimary (citable) accession number: Q00612
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: March 20, 2007
Last modified: November 25, 2008
This is version 81 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents