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P85968 (6PGD_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 51. 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length483 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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. UniProtKB P00349

Pathway

Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 3/3. UniProtKB P00349

Subunit structure

Homodimer By similarity. UniProtKB P00349

Subcellular location

Cytoplasm Ref.3.

Sequence similarities

Belongs to the 6-phosphogluconate dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 4834826-phosphogluconate dehydrogenase, decarboxylating
PRO_0000349115

Regions

Nucleotide binding10 – 156NADP By similarity
Nucleotide binding33 – 353NADP By similarity
Nucleotide binding75 – 773NADP By similarity
Nucleotide binding478 – 4814NADP; shared with dimeric partner By similarity
Region129 – 1313Substrate binding By similarity
Region187 – 1882Substrate binding By similarity

Sites

Active site1841Proton acceptor By similarity
Active site1911Proton donor By similarity
Binding site1031NADP By similarity
Binding site1031Substrate By similarity
Binding site1921Substrate By similarity
Binding site2611Substrate; via amide nitrogen By similarity
Binding site2881Substrate By similarity
Binding site4471Substrate; shared with dimeric partner By similarity
Binding site4531Substrate; shared with dimeric partner By similarity

Amino acid modifications

Modified residue381N6-acetyllysine By similarity
Modified residue591N6-acetyllysine By similarity
Modified residue2571Phosphoserine Ref.2
Modified residue2631Phosphothreonine Ref.2
Modified residue2671Phosphothreonine Ref.2
Modified residue2701Phosphoserine Ref.2

Sequences

Sequence LengthMass (Da)Tools
P85968 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: 7B3F308C3E9B17D4

FASTA48353,236
        10         20         30         40         50         60 
MAQADIALIG LAVMGQNLIL NMNDHGFVVC AFNRTVSKVD DFLAKEAKGT KVIGAKSLKD 

        70         80         90        100        110        120 
MVSKLKKPRR VILLVKAGQA VDDFIEKLVP LLDTGDIIID GGNSEYRDTT RRCQDLKAKG 

       130        140        150        160        170        180 
ILFVGSGVSG GEEGARYGPS LMPGGNKEAW PHIKTIFQAI AAKVGTGEPC CDWVGDEGAG 

       190        200        210        220        230        240 
HFVKMVHNGI EYGDMQLICE AYHLMKDVLG MRHEEMAQAF EDWNKTELDS FLIEITANIL 

       250        260        270        280        290        300 
KFQDTDGKEL LPKIRDSAGQ KGTGKWTAIS ALEYGMPVTL IGEAVFARCL SSLKEERVQA 

       310        320        330        340        350        360 
SRKLKGPKMV QLEGSKQAFL EDVRKALYAS KIISYAQGFM LLRQAATEFG WTLNYGGIAL 

       370        380        390        400        410        420 
MWRGGCIIRS VFLGKIKDAF ERNPELQNLL LDDFFKSAVD DCQDSWRRVI STGVQAGIPM 

       430        440        450        460        470        480 
PCFTTALSFY DGYRHEMLPA NLIQAQRDYF GAHTYELLSK PGEFIHTNWT GHGGSVSSSS 


YNA 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[2]"Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257; THR-263; THR-267 AND SER-270, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[3]"Proteome profile of the mature rat olfactory bulb."
Maurya D.K., Sundaram C.S., Bhargava P.
Proteomics 9:2593-2599(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AABR03040409 Genomic DNA. No translation available.
RefSeqXP_002729611.1. XM_002729565.3.
XP_003754166.1. XM_003754118.2.

3D structure databases

ProteinModelPortalP85968.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteP85968.

2D gel databases

World-2DPAGE0004:P85968.

Proteomic databases

PaxDbP85968.
PRIDEP85968.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000018609; ENSRNOP00000018609; ENSRNOG00000030317.
GeneID100360180.
KEGGrno:100360180.

Organism-specific databases

RGD1583832. Pgd.

Phylogenomic databases

eggNOGCOG5059.
GeneTreeENSGT00740000114943.
HOGENOMHOG000255147.
HOVERGENHBG000029.
KOK00033.

Enzyme and pathway databases

SABIO-RKP85968.
UniPathwayUPA00115; UER00410.

Gene expression databases

GenevestigatorP85968.

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...

Other

PROP85968.

Entry information

Entry name6PGD_RAT
AccessionPrimary (citable) accession number: P85968
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: September 2, 2008
Last modified: April 16, 2014
This is version 51 of the entry and version 1 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