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

P41573 (6PGD_DROSI) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 76. 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:
6-phosphogluconate dehydrogenase, decarboxylating

EC=1.1.1.44
Gene names
Name:Pgd
OrganismDrosophila simulans (Fruit fly)
Taxonomic identifier7240 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length481 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO2, with concomitant reduction of NADP to NADPH By similarity.

Catalytic activity

6-phospho-D-gluconate + NADP+ = D-ribulose 5-phosphate + CO2 + NADPH.

Pathway

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

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the 6-phosphogluconate dehydrogenase family.

Ontologies

Keywords
   Biological processGluconate utilization
Pentose shunt
   LigandNADP
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological_processD-gluconate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

pentose-phosphate shunt

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionNADP binding

Inferred from electronic annotation. Source: InterPro

phosphogluconate dehydrogenase (decarboxylating) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4814816-phosphogluconate dehydrogenase, decarboxylating
PRO_0000090070

Regions

Nucleotide binding11 – 166NADP By similarity
Nucleotide binding34 – 363NADP By similarity
Nucleotide binding76 – 783NADP By similarity
Region130 – 1323Substrate binding By similarity
Region187 – 1882Substrate binding By similarity

Sites

Active site1841Proton acceptor By similarity
Active site1911Proton donor By similarity
Binding site1041NADP By similarity
Binding site1041Substrate By similarity
Binding site1921Substrate By similarity
Binding site2591Substrate; via amide nitrogen By similarity
Binding site2861Substrate By similarity
Binding site4451Substrate; shared with dimeric partner By similarity
Binding site4511Substrate; shared with dimeric partner By similarity

Sequences

Sequence LengthMass (Da)Tools
P41573 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 49F97625D5B94822

FASTA48152,394
        10         20         30         40         50         60 
MSGQADIALI GLAVMGQNLI LNMDEKGFVV CAYNRTVAKV KEFLANEAKG TNVIGADSLK 

        70         80         90        100        110        120 
DMVSKLKSPR KVMLLVKGGS AVDDFIQQLV PLLSAGDVII DGGNSEYQDT SRRCDELAKL 

       130        140        150        160        170        180 
GLLYVGSGVS GGEEGARHGP SLMPGGHEAA WPLIQPIFQA ICAKADGEPC CEWVGDGGAG 

       190        200        210        220        230        240 
HFVKMVHNGI EYGDMQLICE AYHIMQSLGL SADQMADEFG KWNSAELDSF LIEITRDILK 

       250        260        270        280        290        300 
YKDGKGHLLE RIRDTAGQKG TGKWTAIAAL QYGVPVTLIG EAVFSRCLSA LKDERVQASS 

       310        320        330        340        350        360 
VLKGPSTKAE VANLTKFLDD IKHALYCAKI VSYAQGFMLM REAARENKWR LNYGGIALMW 

       370        380        390        400        410        420 
RGGCIIRSVF LGNIKDAYTS QPQLSNLLLD DFFKKAIERG QDSWREVVAN AFRWGIPVPA 

       430        440        450        460        470        480 
LSTALSFYDG YRTAKLPANL LQAQRDYFGA HTYELLGQEG QFHHTNWTGT GGNVSASTYQ 


A 

« Hide

References

[1]"Evolutionary inferences from DNA variation at the 6-phosphogluconate dehydrogenase locus in natural populations of Drosophila: selection and geographic differentiation."
Begun D.J.
Genetics 136:155-171(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U02288 Unassigned DNA. Translation: AAA18587.1.

3D structure databases

ProteinModelPortalP41573.
SMRP41573. Positions 3-472.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP41573.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

FlyBaseFBgn0012849. Dsim\Pgd.

Phylogenomic databases

OrthoDBEOG7K3TKV.

Enzyme and pathway databases

UniPathwayUPA00115; UER00410.

Family and domain databases

Gene3D1.10.1040.10. 1 hit.
1.20.5.320. 1 hit.
3.40.50.720. 1 hit.
InterProIPR008927. 6-PGluconate_DH_C-like.
IPR006114. 6PGDH_C.
IPR006113. 6PGDH_decarbox.
IPR006115. 6PGDH_NADP-bd.
IPR006184. 6PGdom_BS.
IPR013328. DH_multihelical.
IPR012284. Fibritin/6PGD_C-extension.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF00393. 6PGD. 1 hit.
PF03446. NAD_binding_2. 1 hit.
[Graphical view]
PIRSFPIRSF000109. 6PGD. 1 hit.
SUPFAMSSF48179. SSF48179. 1 hit.
TIGRFAMsTIGR00873. gnd. 1 hit.
PROSITEPS00461. 6PGD. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry name6PGD_DROSI
AccessionPrimary (citable) accession number: P41573
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 13, 2013
This is version 76 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