[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; DOI=10.1111/j.1601-5223.1990.tb00141.x; PubMed=2361879 [NCBI, ExPASy, EBI, Israel, Japan] Harbitz I., Chowdhary B., Chowdhary R., Kran S., Frengen E., Gustavsson I., Davies W.; "Isolation, characterization and chromosomal assignment of a partial cDNA for porcine 6-phosphogluconate dehydrogenase."; Hereditas 112:83-88(1990).
[2]	IDENTIFICATION OF PROBABLE FRAMESHIFTS. DOI=10.1111/j.1365-2958.1991.tb01880.x; PubMed=1659648 [NCBI, ExPASy, EBI, Israel, Japan] Reizer A., Deutscher J., Saier M.H. Jr., Reizer J.; "Analysis of the gluconate (gnt) operon of Bacillus subtilis."; Mol. Microbiol. 5:1081-1089(1991).

Comments

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: Homodimer.
SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
SEQUENCE CAUTION:
- Sequence=CAA34633.1; Type=Frameshift; Positions=226, 249;

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X16638; CAA34633.1; ALT_FRAME; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A48325; A48325.

UniGene

Ssc.36928

3D structure databases

HSSP

P00349; 2PGD. [HSSP ENTRY / PDB]

SMR

P14332; 1-241.

ModBase

P14332.

Ontologies

GO:0050661;	Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0004616;	Molecular function: phosphogluconate dehydrogenase (decarboxylating) activity (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006098;	Biological process: pentose-phosphate shunt (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR006183; 6-phosphogluconate_DHase.
IPR006114; 6PGDH_C.
IPR006184; 6PGdom_BS.
IPR013328; DHase_multihelical.
IPR012284; Fibritin/6PGD_C-extension.
Graphical view of domain structure.

Gene3D

G3DSA:1.20.5.320; Fibritin/6PGD_C-extension; 1.
G3DSA:1.10.1040.10; Opine_DH; 1.

Pfam

PF00393; 6PGD; 1.
Pfam graphical view of domain structure.

PRINTS

PR00076; 6PGDHDRGNASE.

PROSITE

PS00461; 6PGD; 1.

ProtoNet

P14332.

Phylogenomic databases

HOVERGEN

P14332; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

NADP; Oxidoreductase; Pentose shunt.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`<1 250`	`>250`	`6-phosphogluconate dehydrogenase, decarboxylating.`	`PRO_0000090065`
`NON_TER`	`1 1`

Sequence information

Length: 250 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 27806 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 8BBB0655D9A40C36 [This is a checksum on the sequence]

        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

P14332 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools