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O13287 (6PGD_CANAX) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 78. 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:DOR14
OrganismCandida albicans (Yeast)
Taxonomic identifier5476 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length517 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 – 5175176-phosphogluconate dehydrogenase, decarboxylating
PRO_0000090072

Regions

Nucleotide binding35 – 406NADP By similarity
Nucleotide binding58 – 603NADP By similarity
Nucleotide binding100 – 1023NADP By similarity
Region154 – 1563Substrate binding By similarity
Region211 – 2122Substrate binding By similarity

Sites

Active site2081Proton acceptor By similarity
Active site2151Proton donor By similarity
Binding site1281NADP By similarity
Binding site1281Substrate By similarity
Binding site2161Substrate By similarity
Binding site2861Substrate; via amide nitrogen By similarity
Binding site3131Substrate By similarity
Binding site4741Substrate; shared with dimeric partner By similarity
Binding site4801Substrate; shared with dimeric partner By similarity

Sequences

Sequence LengthMass (Da)Tools
O13287 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 91E3F520FFCABF7A

FASTA51756,924
        10         20         30         40         50         60 
MKNFNALSRL SILSKQLSFN NTNSSIARGD IGLIGLAVMG QNLILNMADH GYTVVAYNRT 

        70         80         90        100        110        120 
TAKVDRFLEN EAKGKSILGA HSIKELVDQL KRPRRIMLLV KAGAPVDEFI NQLLPYLEEG 

       130        140        150        160        170        180 
DIIIDGGNSH FPDSNRRYEE LAKKGILFVG SGVSGGEEGA RTGPSLMPGG NEKAWPHIKE 

       190        200        210        220        230        240 
IFQDVAAKSD GEPCCDWVGD AGAGHYVKMV HNGIEYGDMQ LICEAYDLMK RVGKFEDKEI 

       250        260        270        280        290        300 
GDVFATWNKG VLDSFLIEIT RDILYYNDPT DGKPLVEKIL DTAGQKGTGK WTAVNALDLG 

       310        320        330        340        350        360 
IPVTLIGEAV FSRCLSAMKA ERVEASKALK GPQVTGESPI TDKKQFIDDL EQALYASKII 

       370        380        390        400        410        420 
SYTQGFMLMN QAAKDYGWKL NNAGIALMWR GGCIIRSVFL AEITAAYRKK PDLENLLLYP 

       430        440        450        460        470        480 
FFNDAITKAQ SGWRASVGKA IQYGIPTPAF STALAFYDGL RSERLPANLL QAQRDYFGAH 

       490        500        510 
TFKVLPGQEN ELLKKDEWIH INWTGRGGDV SSTTYDA 

« Hide

References

[1]"Molecular cloning of DOR14 gene for 6-phosphogluconate dehydrogenase (6PGD) from Candida albicans."
Watanabe M., Ishii N., Arisawa M., Aoki Y.
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 10259 / CBS 5796 / DSM 5817 / JCM 2078 / NBRC 1060.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB006102 Genomic DNA. Translation: BAA21690.1.

3D structure databases

ProteinModelPortalO13287.
SMRO13287. Positions 29-504.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEO13287.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0362.

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_CANAX
AccessionPrimary (citable) accession number: O13287
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: October 16, 2013
This is version 78 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