[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1007/s002849900392; PubMed=9767718 [NCBI, ExPASy, EBI, Israel, Japan] Clark M.A., Baumann L., Baumann P.; "Buchnera aphidicola (Aphid endosymbiont) contains genes encoding enzymes of histidine biosynthesis."; Curr. Microbiol. 37:356-358(1998).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1126/science.1071278; PubMed=12089438 [NCBI, ExPASy, EBI, Israel, Japan] Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.; "50 million years of genomic stasis in endosymbiotic bacteria."; Science 296:2376-2379(2002).

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 .
SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.

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

AF067228; AAC97362.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE013218; AAM67670.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_660459.1; -.

3D structure databases

HSSP

P00349; 2PGD. [HSSP ENTRY / PDB]

ModBase

Q9ZHD9.

Enzyme and pathway databases

BioCyc

BAPH198804:BUSG100-MON; -.

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:0019521;	Biological process: D-gluconate metabolic process (inferred from electronic annotation from UniProtKB-KW).
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.
IPR006113; 6PGDH_decarbox.
IPR006115; 6PGDH_NAD-bd.
IPR006184; 6PGdom_BS.
IPR013328; DHase_multihelical.
IPR012284; Fibritin/6PGD_C-extension.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:1.20.5.320; Fibritin/6PGD_C-extension; 1.
G3DSA:3.40.50.720; NAD(P)-bd; 1.
G3DSA:1.10.1040.10; Opine_DH; 1.

Pfam

PF00393; 6PGD; 1.
PF03446; NAD_binding_2; 1.
Pfam graphical view of domain structure.

PRINTS

PR00076; 6PGDHDRGNASE.

TIGR00873; gnd; 1.

PS00461; 6PGD; 1.

Genome annotation databases

GeneID

1005917; -.

GenomeReviews

AE013218_GR; BUsg_100.

KEGG

bas:BUsg100; -.

Phylogenomic databases

HOGENOM

Q9ZHD9; -.

Genome annotation databases

CMR

Q9ZHD9; BUsg_100.

Other

UniRef

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

Keywords

Complete proteome; Gluconate utilization; NADP; Oxidoreductase; Pentose shunt.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 473`	`473`	`6-phosphogluconate dehydrogenase, decarboxylating.`	`PRO_0000090029`
`CONFLICT`	`158 158`		`K -> N (in Ref. 1; AAC97362).`
`CONFLICT`	`324 326`		`RRA -> TKS (in Ref. 1; AAC97362).`
`CONFLICT`	`348 348`		`K -> I (in Ref. 1; AAC97362).`

Sequence information

Length: 473 AA [This is the length of the unprocessed precursor]

Molecular weight: 53805 Da [This is the MW of the unprocessed precursor]

CRC64: A11842A037E1E984 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLKQQVGVIG MAVMGRNLAL NIESKKYTVS IFNRTQSVTE EVINNNKEKK IFPYFSIKDF 

        70         80         90        100        110        120 
VNSLRKPRCI LLMVKSGQPT DETIQFILPY LNKGDILIDG GNTFYKDSIR RSNDLMKCGI 

       130        140        150        160        170        180 
NFIGMGVSGG ELGALNGPSI MPGGSREAYD LVSSMLKKIS AKFKNEPCVS YIGPNGAGHY 

       190        200        210        220        230        240 
VKMIHNGIEY GDMQLISESY FILKNVLNMK NEELSNTFSQ WNKGELNSYL IEITKNIFLK 

       250        260        270        280        290        300 
KEKDGIHYLI DSILDHAEDK GTGKWISQDA LELHEPLSLI TESVFARYLS SLKDQRLIAS 

       310        320        330        340        350        360 
KILKGPILKC ISSQNKELFV EEVRRALYLG KIISYAQGFS QLKKASEKYS WNLQYGKIAK 

       370        380        390        400        410        420 
IFRAGCIIRA DFLERITDAF KSNNVTNLLL TPYFSEISNK YEKSLRYITS YAIKYGIPVP 

       430        440        450        460        470 
TFASAISYYD NYRTMSSSAN LIQAQRDYFG AHTYRRTDKK GYFHTNWLTK KEL

Q9ZHD9 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