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P12646 (G6PD_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length524 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. HAMAP-Rule MF_00966

Catalytic activity

D-glucose 6-phosphate + NADP+ = 6-phospho-D-glucono-1,5-lactone + NADPH. HAMAP-Rule MF_00966

Pathway

Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3. HAMAP-Rule MF_00966

Sequence similarities

Belongs to the glucose-6-phosphate dehydrogenase family.

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.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 524524Glucose-6-phosphate 1-dehydrogenase HAMAP-Rule MF_00966
PRO_0000068092

Regions

Nucleotide binding42 – 498NADP 1 By similarity
Nucleotide binding406 – 4083NADP 2 By similarity
Nucleotide binding426 – 4283NADP 2 By similarity
Region205 – 2095Substrate binding By similarity

Sites

Active site2671Proton acceptor By similarity
Binding site761NADP 1 By similarity
Binding site1751NADP 1; via carbonyl oxygen By similarity
Binding site1751Substrate By similarity
Binding site2431Substrate By similarity
Binding site2621Substrate By similarity
Binding site3621NADP 2 By similarity
Binding site3651Substrate By similarity
Binding site3701Substrate By similarity
Binding site3711NADP 2 By similarity
Binding site3751NADP 2 By similarity
Binding site3981NADP 2 By similarity
Binding site4001Substrate By similarity
Binding site4921NADP 2 By similarity
Binding site5081NADP 2 By similarity
Binding site5141NADP 2 By similarity

Amino acid modifications

Modified residue201Phosphoserine Ref.6

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 »

FASTA50258,008

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
Strain: Berkeley.
[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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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. NM_078687.1.
NP_728287.1. NM_167676.1.
UniGeneDm.225.

3D structure databases

ProteinModelPortalP12646.
SMRP12646. Positions 36-514.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid59270. 1 interaction.
DIPDIP-20748N.
IntActP12646. 2 interactions.
MINTMINT-882769.

Proteomic databases

PaxDbP12646.
PRIDEP12646.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID32974.
KEGGdme:Dmel_CG12529.

Organism-specific databases

CTD32974.
FlyBaseFBgn0004057. Zw.

Phylogenomic databases

eggNOGCOG0364.
InParanoidP12646.
KOK00036.
OrthoDBEOG7DRJ2T.
PhylomeDBP12646.

Enzyme and pathway databases

UniPathwayUPA00115; UER00408.

Gene expression databases

BgeeP12646.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_00966. G6PD.
InterProIPR001282. G6P_DH.
IPR019796. G6P_DH_AS.
IPR022675. G6P_DH_C.
IPR022674. G6P_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR23429. PTHR23429. 1 hit.
PfamPF02781. G6PD_C. 1 hit.
PF00479. G6PD_N. 1 hit.
[Graphical view]
PIRSFPIRSF000110. G6PD. 1 hit.
PRINTSPR00079. G6PDHDRGNASE.
TIGRFAMsTIGR00871. zwf. 1 hit.
PROSITEPS00069. G6P_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi32974.
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: April 16, 2014
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Drosophila

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