[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Desouza M., Lobo Z., Maitra P.K.; Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 204511 / S288c / AB972; PubMed=8091229 [NCBI, ExPASy, EBI, Israel, Japan] Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M.; "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII."; Science 265:2077-2082(1994).
[3]	PROTEIN SEQUENCE OF 41-47 AND 120-131. STRAIN=ATCC 204508 / S288c; DOI=10.1002/elps.11501501210; PubMed=7895733 [NCBI, ExPASy, EBI, Israel, Japan] Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., Volpe T., Warner J.R., McLaughlin C.S.; "Protein identifications for a Saccharomyces cerevisiae protein database."; Electrophoresis 15:1466-1486(1994).
[4]	SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. DOI=10.1038/nature02026; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan] Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.; "Global analysis of protein localization in budding yeast."; Nature 425:686-691(2003).
[5]	LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan] Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.; "Global analysis of protein expression in yeast."; Nature 425:737-741(2003).
[6]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128, AND MASS SPECTROMETRY. DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan] Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; "A multidimensional chromatography technology for in-depth phosphoproteome analysis."; Mol. Cell. Proteomics 7:1389-1396(2008).

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 .
INTERACTION:
P02829:HSP82; NbExp=1; IntAct=EBI-1965, EBI-8659;
P33203:PRP40; NbExp=1; IntAct=EBI-1965, EBI-701;
P39940:RSP5; NbExp=1; IntAct=EBI-1965, EBI-16219;
P40318:SSM4; NbExp=1; IntAct=EBI-1965, EBI-18208;
Q06525:URN1; NbExp=1; IntAct=EBI-1965, EBI-35138;
SUBCELLULAR LOCATION: Cytoplasm.
MISCELLANEOUS: Present with 101000 molecules/cell in log phase SD medium.
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

Z46631; CAA86600.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00028; AAB68452.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U17155; AAA53637.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S46671; S46671.

RefSeq

NP_012053.1; -.

3D structure databases

PDB

2P4Q; X-ray; 2.37 A; A=1-489.

[ExPASy / RCSB / EBI]

PDBsum

2P4Q; -.

ModBase

P38720.

Protein-protein interaction databases

DIP

DIP:6604N; -.

IntAct

P38720; -.

Organism-specific databases

YHR183w; -.

S000001226; GND1.

Gene expression databases

GermOnline

YHR183W; Saccharomyces cerevisiae.

Ontologies

GO:0005739;	Cellular component: mitochondrion (inferred from direct assay from SGD).
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:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0009051;	Biological process: pentose-phosphate shunt, oxidative branch (inferred from genetic interaction from SGD).
GO:0006979;	Biological process: response to oxidative stress (inferred from mutant phenotype from SGD).
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.

Proteomic databases

P38720; -.

Genome annotation databases

Ensembl

YHR183W; Saccharomyces cerevisiae. [Contig view]

856589; -.

U00093_GR; YHR183W.

sce:YHR183W; -.

fig|4932.3.peg.3222; -.

Phylogenomic databases

HOGENOM

P38720; -.

Other

LinkHub

P38720; -.

NextBio

982464; -.

UniRef

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

Keywords

3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; NADP; Oxidoreductase; Pentose shunt; Phosphoprotein.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 489`	`489`	`6-phosphogluconate dehydrogenase, decarboxylating 1.`	`PRO_0000090075`
`MOD_RES`	`128 128`		`Phosphoserine.`
`STRAND`	`4 8`	`5`
`HELIX`	`12 23`	`12`
`STRAND`	`28 31`	`4`
`STRAND`	`33 35`	`3`
`HELIX`	`36 43`	`8`
`TURN`	`44 48`	`5`
`STRAND`	`49 52`	`4`
`HELIX`	`57 62`	`6`
`STRAND`	`69 72`	`4`
`HELIX`	`78 87`	`10`
`HELIX`	`88 90`	`3`
`STRAND`	`96 99`	`4`
`HELIX`	`105 117`	`13`
`STRAND`	`121 129`	`9`
`HELIX`	`130 136`	`7`
`STRAND`	`139 144`	`6`
`HELIX`	`146 148`	`3`
`HELIX`	`149 159`	`11`
`STRAND`	`166 168`	`3`
`HELIX`	`177 205`	`29`
`HELIX`	`211 222`	`12`
`TURN`	`223 226`	`4`
`HELIX`	`229 238`	`10`
`STRAND`	`245 247`	`3`
`HELIX`	`248 251`	`4`
`HELIX`	`261 272`	`12`
`HELIX`	`277 290`	`14`
`HELIX`	`292 301`	`10`
`HELIX`	`315 348`	`34`
`HELIX`	`354 362`	`9`
`STRAND`	`363 365`	`3`
`HELIX`	`370 381`	`12`
`HELIX`	`388 390`	`3`
`HELIX`	`392 415`	`24`
`HELIX`	`420 432`	`13`
`HELIX`	`439 449`	`11`
`HELIX`	`458 460`	`3`
`STRAND`	`463 465`	`3`

Sequence information

Length: 489 AA [This is the length of the unprocessed precursor]

Molecular weight: 53543 Da [This is the MW of the unprocessed precursor]

CRC64: 55CAE5DACDC6A00B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSADFGLIGL AVMGQNLILN AADHGFTVCA YNRTQSKVDH FLANEAKGKS IIGATSIEDF 

        70         80         90        100        110        120 
ISKLKRPRKV MLLVKAGAPV DALINQIVPL LEKGDIIIDG GNSHFPDSNR RYEELKKKGI 

       130        140        150        160        170        180 
LFVGSGVSGG EEGARYGPSL MPGGSEEAWP HIKNIFQSIS AKSDGEPCCE WVGPAGAGHY 

       190        200        210        220        230        240 
VKMVHNGIEY GDMQLICEAY DIMKRLGGFT DKEISDVFAK WNNGVLDSFL VEITRDILKF 

       250        260        270        280        290        300 
DDVDGKPLVE KIMDTAGQKG TGKWTAINAL DLGMPVTLIG EAVFARCLSA LKNERIRASK 

       310        320        330        340        350        360 
VLPGPEVPKD AVKDREQFVD DLEQALYASK IISYAQGFML IREAAATYGW KLNNPAIALM 

       370        380        390        400        410        420 
WRGGCIIRSV FLGQITKAYR EEPDLENLLF NKFFADAVTK AQSGWRKSIA LATTYGIPTP 

       430        440        450        460        470        480 
AFSTALSFYD GYRSERLPAN LLQAQRDYFG AHTFRVLPEC ASDNLPVDKD IHINWTGHGG 


NVSSSTYQA

P38720 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