Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q27638 (G6PD_DROYA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 82. 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·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
Gene names
Name:Zw
Synonyms:G6pd
OrganismDrosophila yakuba (Fruit fly)
Taxonomic identifier7245 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length518 AA.
Sequence statusFragment.
Protein existenceInferred from homology

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 518›518Glucose-6-phosphate 1-dehydrogenase HAMAP-Rule MF_00966
PRO_0000068094

Regions

Nucleotide binding36 – 438NADP 1 By similarity
Nucleotide binding400 – 4023NADP 2 By similarity
Nucleotide binding420 – 4223NADP 2 By similarity
Region199 – 2035Substrate binding By similarity

Sites

Active site2611Proton acceptor By similarity
Binding site701NADP 1 By similarity
Binding site1691NADP 1; via carbonyl oxygen By similarity
Binding site1691Substrate By similarity
Binding site2371Substrate By similarity
Binding site2561Substrate By similarity
Binding site3561NADP 2 By similarity
Binding site3591Substrate By similarity
Binding site3641Substrate By similarity
Binding site3651NADP 2 By similarity
Binding site3691NADP 2 By similarity
Binding site3921NADP 2 By similarity
Binding site3941Substrate By similarity
Binding site4861NADP 2 By similarity
Binding site5021NADP 2 By similarity
Binding site5081NADP 2 By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
Q27638 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 6AFA194E1D3A3E8B

FASTA51859,938
        10         20         30         40         50         60 
DHTALDLIIK SLKSPTMVCE GTHFDGKIPH TFVIFGASGD LAKKKIYPKL WWFYRDDLLP 

        70         80         90        100        110        120 
KLTKFCGYAR SMLTVDSIKE QCLPYMKVQS HEQKKYEEFW ALNEYVSGRY DGRTGFELLN 

       130        140        150        160        170        180 
QQLELMENKN KANRIFYLAL PPSVFEEVTV NIKQICMSVC GWNRVIIEKP FGRDDASSQA 

       190        200        210        220        230        240 
LSDHLAALFH EDQLYRIDHY LGKEMVQNLM TIRFGNKILS STWNRENIAS VLITFKEPFG 

       250        260        270        280        290        300 
TQGRGGYFDE FGIIRDVMQN HLLQILSLVA MEKPVSCHPD DIRDEKVKVL KSIETLTLKD 

       310        320        330        340        350        360 
MVLGQYLGNP QGTTDDARTG YVEDPTVSDD SNTPTYALGV LKINNERWQG VPFILRCGKR 

       370        380        390        400        410        420 
LNERKAEVRI QYQDVPGDIF EGNTKRNELV IRVQPGEALY FKMMTKSPGI TFDIEETELD 

       430        440        450        460        470        480 
LTYEHRYKDS YLPDAYERLI LDVFCGSQMH FVRSDQLREA WRIFTPILHQ IEREHIRPIT 

       490        500        510 
YQYGSRGPKE ADRMCEENNF KYSGSYKWHG GKAATSNL 

« Hide

References

[1]Eanes W.F., Kirchner M., Yoon J., Biermann C., Wang I., McCartney M., Verrelli B.C.
Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BG1016.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U42750 Genomic DNA. Translation: AAB02813.1.

3D structure databases

ProteinModelPortalQ27638.
SMRQ27638. Positions 30-508.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ27638.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

FlyBaseFBgn0015691. Dyak\Zw.

Phylogenomic databases

eggNOGCOG0364.
OrthoDBEOG7DRJ2T.

Enzyme and pathway databases

UniPathwayUPA00115; UER00408.

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...

Entry information

Entry nameG6PD_DROYA
AccessionPrimary (citable) accession number: Q27638
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: February 19, 2014
This is version 82 of the entry and version 1 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