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

P14332 (6PGD_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 96. 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:PGD
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length250 AA.
Sequence statusFragment.
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.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the 6-phosphogluconate dehydrogenase family.

Sequence caution

The sequence CAA34633.1 differs from that shown. Reason: Frameshift at positions 226 and 249.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 250›2506-phosphogluconate dehydrogenase, decarboxylating
PRO_0000090065

Regions

Nucleotide binding245 – 2484NADP; shared with dimeric partner By similarity

Sites

Binding site291Substrate; via amide nitrogen By similarity
Binding site561Substrate By similarity
Binding site2141Substrate; shared with dimeric partner By similarity
Binding site2201Substrate; shared with dimeric partner By similarity

Amino acid modifications

Modified residue251Phosphoserine By similarity
Modified residue311Phosphothreonine By similarity
Modified residue351Phosphothreonine By similarity
Modified residue381Phosphoserine By similarity
Modified residue771N6-acetyllysine By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P14332 [UniParc].

Last modified October 10, 2003. Version 3.
Checksum: 8BBB0655D9A40C36

FASTA25027,806
        10         20         30         40         50         60 
IEITANILKF QDADGKHLLP KIRDSAGQKG TGKWTAISAL EYGVPVTLIG EAVFARCLSS 

        70         80         90        100        110        120 
LKDERVQASK KLKGPQKIQF SGDKKSFLED IRKALYASKI ISYTQGFMLL RQAAAEFGWS 

       130        140        150        160        170        180 
STTEHRLMWR GGCIIRSVFL GKIKDAFDRN PGLQNLLLDD FFKSAVEDCQ DSWRRAVSTG 

       190        200        210        220        230        240 
VQTGIPMPCF TTALSFYDGY RHEMLPANLI QAQRDYFGAH TYELLAKPGH FVHTNWTGHG 

       250 
GSVSSSSYNA 

« Hide

References

[1]"Isolation, characterization and chromosomal assignment of a partial cDNA for porcine 6-phosphogluconate dehydrogenase."
Harbitz I., Chowdhary B., Chowdhary R., Kran S., Frengen E., Gustavsson I., Davies W.
Hereditas 112:83-88(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Analysis of the gluconate (gnt) operon of Bacillus subtilis."
Reizer A., Deutscher J., Saier M.H. Jr., Reizer J.
Mol. Microbiol. 5:1081-1089(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF PROBABLE FRAMESHIFTS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X16638 mRNA. Translation: CAA34633.1. Frameshift.
PIRA48325.
UniGeneSsc.30761.

3D structure databases

ProteinModelPortalP14332.
SMRP14332. Positions 1-241.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9823.ENSSSCP00000003687.

Proteomic databases

PaxDbP14332.
PRIDEP14332.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0362.
HOGENOMHOG000255147.
HOVERGENHBG000029.

Enzyme and pathway databases

UniPathwayUPA00115; UER00410.

Family and domain databases

Gene3D1.10.1040.10. 1 hit.
1.20.5.320. 1 hit.
InterProIPR008927. 6-PGluconate_DH_C-like.
IPR006114. 6PGDH_C.
IPR006184. 6PGdom_BS.
IPR013328. DH_multihelical.
IPR012284. Fibritin/6PGD_C-extension.
[Graphical view]
PfamPF00393. 6PGD. 1 hit.
[Graphical view]
SUPFAMSSF48179. SSF48179. 1 hit.
PROSITEPS00461. 6PGD. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry name6PGD_PIG
AccessionPrimary (citable) accession number: P14332
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: October 10, 2003
Last modified: November 13, 2013
This is version 96 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways