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Q9DCD0 (6PGD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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.

Pathway

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

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

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_0000090064

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

Sequences

Sequence LengthMass (Da)Tools
Q9DCD0 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: CD0A3F72EEC2831E

FASTA48353,247
        10         20         30         40         50         60 
MAQADIALIG LAVMGQNLIL NMNDHGFVVC AFNRTVSKVD DFLANEAKGT KVVGAQSLKD 

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

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

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

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

       310        320        330        340        350        360 
SQKLKGPKVV QLEGSKKSFL EDIRKALYAS KIISYAQGFM LLRQAATEFG WTLNYGGIAL 

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

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


YNA 

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: BALB/c and C57BL/6J.
Tissue: Bone marrow and Kidney.
[2]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-38, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK002894 mRNA. Translation: BAB22439.1.
AK145602 mRNA. Translation: BAE26535.1.
AK150210 mRNA. Translation: BAE29381.1.
AK153409 mRNA. Translation: BAE31969.1.
AK155027 mRNA. Translation: BAE32999.1.
AK166733 mRNA. Translation: BAE38978.1.
AK166947 mRNA. Translation: BAE39134.1.
AK167215 mRNA. Translation: BAE39341.1.
AK168251 mRNA. Translation: BAE40201.1.
CCDSCCDS38974.1.
RefSeqNP_001074743.1. NM_001081274.1.
UniGeneMm.252080.

3D structure databases

ProteinModelPortalQ9DCD0.
SMRQ9DCD0. Positions 2-470.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-1868998.

PTM databases

PhosphoSiteQ9DCD0.

Proteomic databases

MaxQBQ9DCD0.
PaxDbQ9DCD0.
PRIDEQ9DCD0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000084124; ENSMUSP00000081141; ENSMUSG00000028961.
GeneID110208.
KEGGmmu:110208.
UCSCuc008vvv.1. mouse.

Organism-specific databases

CTD5226.
MGIMGI:97553. Pgd.

Phylogenomic databases

eggNOGCOG0362.
GeneTreeENSGT00390000009023.
HOGENOMHOG000255147.
HOVERGENHBG000029.
InParanoidQ9DCD0.
KOK00033.
OMAHFVGIGV.
OrthoDBEOG7K3TKV.
PhylomeDBQ9DCD0.
TreeFamTF300386.

Enzyme and pathway databases

UniPathwayUPA00115; UER00410.

Gene expression databases

BgeeQ9DCD0.
CleanExMM_PGD.
GenevestigatorQ9DCD0.

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

ChiTaRSPGD. mouse.
NextBio363535.
PROQ9DCD0.
SOURCESearch...

Entry information

Entry name6PGD_MOUSE
AccessionPrimary (citable) accession number: Q9DCD0
Secondary accession number(s): Q3UD80
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2002
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 113 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot