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P41570 (6PGD_CERCA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
6-phosphogluconate dehydrogenase, decarboxylating
EC=1.1.1.44
Gene names
Name:Pgd
OrganismCeratitis capitata (Mediterranean fruit fly) (Tephritis capitata)
Taxonomic identifier7213 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Tephritoidea › Tephritidae › Ceratitis › Ceratitis

Protein attributes

Sequence length481 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4814816-phosphogluconate dehydrogenase, decarboxylating
PRO_0000090068

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
P41570 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: F0ABB506AD1B86D0

FASTA48152,964
        10         20         30         40         50         60 
MSAKADIALI GLAVMGQNLV LNMNDKGFVV CAYNRTVEKV NQFLKNEAKG TNVIGATSLQ 

        70         80         90        100        110        120 
DMVNKLKLPR KIMLLVKAGS AVDDFIQQLV PLLSPGDVII DGGNSEYQDT ARRCDELRAK 

       130        140        150        160        170        180 
KILYVGSGVS GGEEGARHGP SLMPGGHPEA WPLIQPIFQS ICAKADKEPC CEWVGEGGAG 

       190        200        210        220        230        240 
HFVKMVHNGI EYGDMQLICE AYQIMKALGL SQAEMATEFE KWNSEELDSF LIEITRDILN 

       250        260        270        280        290        300 
YQDDRGYLLE RIRDTAGQKG TGKWTAISAL QYGVPVTLIG EAVFSRCLSA LKDERVAASK 

       310        320        330        340        350        360 
QLKGPNVNAK VEDLPKFLNH IKHALYCSKI VSYAQGFMLM REAAKENNWN LNYGGIALMW 

       370        380        390        400        410        420 
RGGCIIRSVF LGNIKDAYTR NPQLSNLLLD DFFKKAIEVG QNSWRQVVAN AFLWGIPVPA 

       430        440        450        460        470        480 
LSTALSFYDG YRTEKLPANL LQAQRDYFGA HTYELLGAEG KFVHTNWTGT GGNVSASTYQ 


A

« Hide

References

[1]"Isolation of cDNAs encoding 6-phosphogluconate dehydrogenase and glucose-6-phosphate dehydrogenase from the mediterranean fruit fly Ceratitis capitata: correlating genetic and physical maps of chromosome 5."
Scott M.J., Kriticou D., Robinson A.S.
Insect Mol. Biol. 1:213-222(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		S67873 mRNA. Translation: AAB29396.1.

3D structure databases

ProteinModelPortalP41570.
SMRP41570. Positions 3-472.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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. 6DGDH_C_like. 1 hit.
TIGRFAMsTIGR00873. gnd. 1 hit.
PROSITEPS00461. 6PGD. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry name6PGD_CERCA
AccessionPrimary (citable) accession number: P41570
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 3, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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