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O60037 (6PGD_CUNEL) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:6-PGD
OrganismCunninghamella elegans
Taxonomic identifier4853 [NCBI]
Taxonomic lineageEukaryotaFungiFungi incertae sedisEarly diverging fungal lineagesMucoromycotinaMucoralesCunninghamellaceaeCunninghamella

Protein attributes

Sequence length485 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: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4854856-phosphogluconate dehydrogenase, decarboxylating
PRO_0000090073

Regions

Nucleotide binding12 – 176NADP By similarity
Nucleotide binding35 – 373NADP By similarity
Nucleotide binding77 – 793NADP By similarity
Region131 – 1333Substrate binding By similarity
Region189 – 1902Substrate binding By similarity

Sites

Active site1861Proton acceptor By similarity
Active site1931Proton donor By similarity
Binding site1051NADP By similarity
Binding site1051Substrate By similarity
Binding site1941Substrate By similarity
Binding site2631Substrate; via amide nitrogen By similarity
Binding site2901Substrate By similarity
Binding site4491Substrate; shared with dimeric partner By similarity
Binding site4551Substrate; shared with dimeric partner By similarity

Sequences

Sequence LengthMass (Da)Tools
O60037 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: F7E6DDFF3D21EFB2

FASTA48553,102
        10         20         30         40         50         60 
MVEAVADIGL IGLAVMGQNL ILNMNDHGFV VCAYNRTTSK VDDFLANEAK GTNVVGAHSV 

        70         80         90        100        110        120 
EELCAKLKRP RKVMLLVKAG SAVDAFIDQL LPHLEEGDII IDGGNSHFPD SIRRTKELEA 

       130        140        150        160        170        180 
KGILFVGSGV SGGEEGARYG PSLMPGGNSK AWEHIQPIFQ AIAAKAPDGA SCCEWVGETG 

       190        200        210        220        230        240 
AGHYVKMVHN GIEYGDMQLI TEVYQILHEG LGLSHDEMAD IFEEWNKGDL DSFLIEITRD 

       250        260        270        280        290        300 
ILRFKDTDGQ PLVTKIRDTA GQKGTGKWTA IDSLDRGIPV TLIGEAVYSR CLSSLKDERV 

       310        320        330        340        350        360 
RASKILQGPS SSKFTGDKKT FIAQLGQALY AAKIVSYAQG YMLMRQAAKD YEWKLNNAGI 

       370        380        390        400        410        420 
ALMWRGGCII RSVFLGKIRD AYTKNPELEN LLFDDFFKDA TAKAQDAWRN VTAQAVLMGI 

       430        440        450        460        470        480 
PTPALSTALN FYDGLRHEIL PANLLQAQRD YFGAHTYELL HTPGKWVHTN WTGRGGNVSA 


STYDA 

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References

[1]"Identification and sequencing of a cDNA encoding 6-phosphogluconate dehydrogenase from a fungus, Cunninghamella elegans and expression of the gene in Escherichia coli."
Wang R.F., Khan A.A., Cao W.W., Cerniglia C.E.
FEMS Microbiol. Lett. 169:397-402(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ATCC 36112 / DSM 8217.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y17297 mRNA. Translation: CAA76734.1.

3D structure databases

ProteinModelPortalO60037.
SMRO60037. Positions 4-476.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEO60037.

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. SSF48179. 1 hit.
TIGRFAMsTIGR00873. gnd. 1 hit.
PROSITEPS00461. 6PGD. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry name6PGD_CUNEL
AccessionPrimary (citable) accession number: O60037
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: August 1, 1998
Last modified: October 16, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways