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Reviewed, UniProtKB/Swiss-Prot P12646 (G6PD_DROME)

Last modified November 25, 2008. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glucose-6-phosphate 1-dehydrogenase
      Short name=G6PD
    EC=1.1.1.49
Alternative name(s):
    Zwischenferment
Gene names
Name: Zw
Synonyms: G6PD
ORF Names: CG12529
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length524 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Sequence similarities

Belongs to the glucose-6-phosphate dehydrogenase family.

Ontologies

Keywords

   Biological processCarbohydrate metabolism
Glucose metabolism
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandNADP
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processglucose metabolic process

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionglucose-6-phosphate dehydrogenase activity

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

spn-BO771351EBI-223492,EBI-185987

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: P12646-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform B (identifier: P12646-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-22: Missing.
Notes: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 524524Glucose-6-phosphate 1-dehydrogenase
PRO_0000068092

Sites

Active site2671Proton acceptor By similarity
Binding site441NADP By similarity
Binding site761NADP By similarity
Binding site2051Substrate By similarity
Binding site2091Substrate By similarity

Amino acid modifications

Modified residue201Phosphoserine

Natural variations

Alternative sequence1 – 2222Missing in isoform B.
VSP_001593
Natural variant321G → C in strain: F24.1, MT32 and MT68.
Natural variant801T → N in strain: Z74.
Natural variant3821L → P in strain: F23.3, MT41, Z3, Z5, Z11, Z16, Z21, Z27, Z42, Z55, Z64, Z74 and Berkeley.

Experimental info

Sequence conflict185 – 1862QA → AG in AAA51463. Ref.1
Sequence conflict2141N → K in AAA51463. Ref.1
Sequence conflict344 – 3463LGV → ARS in AAA51463. Ref.1
Sequence conflict461 – 4655DELRE → AAAQ in AAA51463. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: ABF81B763A82F1FD

FASTA52460,431
        10         20         30         40         50         60 
MATQKEDHTA LDLIIKSLKS PTMVCEGTHF DGKIPHTFVI FGASGDLAKK KIYPTLWWLY 

        70         80         90        100        110        120 
RDDLLPKPTK FCGYARSMLT VDSIKEQCLP YMKVQPHEQK KYEEFWALNE YVSGRYDGRT 

       130        140        150        160        170        180 
GFELLNQQLE IMENKNKANR IFYLALPPSV FEEVTVNIKQ ICMSVCGWNR VIIEKPFGRD 

       190        200        210        220        230        240 
DASSQALSDH LAGLFQEDQL YRIDHYLGKE MVQNLMTIRF GNKILSSTWN RENIASVLIT 

       250        260        270        280        290        300 
FKEPFGTQGR GGYFDEFGII RDVMQNHLLQ ILSLVAMEKP VSCHPDDIRD EKVKVLKSIE 

       310        320        330        340        350        360 
ALTLDDMVLG QYLGNPQGTN DDARTGYVED PTVSNDSNTP TYALGVLKIN NERWQGVPFI 

       370        380        390        400        410        420 
LRCGKALNER KAEVRIQYQD VLGDIFEGNT KRNELVIRVQ PGEALYFKMM TKSPGITFDI 

       430        440        450        460        470        480 
EETELDLTYE HRYKDSYLPD AYERLILDVF CGSQMHFVRS DELREAWRIF TPILHQIEKE 

       490        500        510        520 
HIRPITYQYG SRGPKEADRK CEENNFKYSG SYKWHGGKAA TSNH 

« Hide

Isoform B [UniParc].

Checksum: DFF55A83782BEDAC
Show »

50258,008

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the Drosophila glucose-6-phosphate dehydrogenase gene and comparison with the homologous human gene."
Fouts D., Ganguly R., Gutierrez A.G., Lucchesi J.C., Manning J.E.
Gene 63:261-275(1988) [PubMed: 2838391] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE (ISOFORM A).
[2]"Historical selection, amino acid polymorphism and lineage-specific divergence at the G6pd locus in Drosophila melanogaster and D. simulans."
Eanes W.F., Kirchner M., Yoon J., Biermann C.H., Wang I.N., McCartney M.A., Verrelli B.C.
Genetics 144:1027-1041(1996) [PubMed: 8913747] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE (ISOFORM A).
Strain: F23.3, F24.1, MT32, MT41, MT68, Z11, Z16, Z21, Z27, Z3, Z41, Z42, Z5, Z55, Z62, Z64 and Z74.
[3]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[4]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
[5]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
Strain: Berkeley.
Tissue: Embryo.
[6]"Phosphoproteome analysis of Drosophila melanogaster embryos."
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, MASS SPECTROMETRY.
Tissue: Embryo.

Cross-references

Sequence databases

M26674, M26673 Genomic DNA. Translation: AAA51463.1.
U42738 Genomic DNA. Translation: AAB02801.1.
U42739 Genomic DNA. Translation: AAB02802.1.
U42740 Genomic DNA. Translation: AAB02803.1.
U42741 Genomic DNA. Translation: AAB02804.1.
U42742 Genomic DNA. Translation: AAB02805.1.
U42743 Genomic DNA. Translation: AAB02806.1.
U42744 Genomic DNA. Translation: AAB02807.1.
U42745 Genomic DNA. Translation: AAB02808.1.
U42746 Genomic DNA. Translation: AAB02809.1.
U42747 Genomic DNA. Translation: AAB02810.1.
U42748 Genomic DNA. Translation: AAB02811.1.
U42749 Genomic DNA. Translation: AAB02812.1.
U43165 Genomic DNA. Translation: AAA99071.1.
U43166 Genomic DNA. Translation: AAA99072.1.
U43167 Genomic DNA. Translation: AAA99073.1.
U44721 Genomic DNA. Translation: AAA99092.1.
U45985 Genomic DNA. Translation: AAA99107.1.
AE014298 Genomic DNA. Translation: AAF48999.1.
AE014298 Genomic DNA. Translation: AAF49000.2.
AY052079 mRNA. Translation: AAK93503.1.
PIRA47740.
DEFFG6. JT0272.
RefSeqNP_523411.1.
NP_728287.1.
UniGeneDm.225

3D structure databases

HSSPHSSP built from PDB template 1QKI based on UniProtKB P11413.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:20748N.
IntActP12646.

Genome annotation databases

EnsemblCG12529. Drosophila melanogaster. [Contig view]
GeneID32974.
KEGGdme:Dmel_CG12529.

Organism-specific databases

FlyBaseFBgn0004057. Zw.

Gene expression databases

ArrayExpressP12646.
GermOnlineCG12529. Drosophila melanogaster.

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

NextBio781313.

Entry information

Entry nameG6PD_DROME
AccessionPrimary (citable) accession number: P12646
Secondary accession number(s): Q27574 expand/collapse secondary AC list , Q27872, Q27879, Q27881, Q9VWE2, Q9VWE3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: July 15, 1998
Last modified: November 25, 2008
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

PATHWAY comments

Index of metabolic and biosynthesis pathways

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

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