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Q9DCD0

- 6PGD_MOUSE

UniProt

Q9DCD0 - 6PGD_MOUSE

Protein

6-phosphogluconate dehydrogenase, decarboxylating

Gene

Pgd

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO2, with concomitant reduction of NADP to NADPH.By similarity

    Catalytic activityi

    6-phospho-D-gluconate + NADP+ = D-ribulose 5-phosphate + CO2 + NADPH.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei103 – 1031NADPBy similarity
    Binding sitei103 – 1031SubstrateBy similarity
    Active sitei184 – 1841Proton acceptorBy similarity
    Active sitei191 – 1911Proton donorBy similarity
    Binding sitei192 – 1921SubstrateBy similarity
    Binding sitei261 – 2611Substrate; via amide nitrogenBy similarity
    Binding sitei288 – 2881SubstrateBy similarity
    Binding sitei447 – 4471Substrate; shared with dimeric partnerBy similarity
    Binding sitei453 – 4531Substrate; shared with dimeric partnerBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi10 – 156NADPBy similarity
    Nucleotide bindingi33 – 353NADPBy similarity
    Nucleotide bindingi75 – 773NADPBy similarity
    Nucleotide bindingi478 – 4814NADP; shared with dimeric partnerBy similarity

    GO - Molecular functioni

    1. NADP binding Source: InterPro
    2. phosphogluconate dehydrogenase (decarboxylating) activity Source: UniProtKB

    GO - Biological processi

    1. D-gluconate metabolic process Source: UniProtKB-KW
    2. pentose biosynthetic process Source: MGI
    3. pentose-phosphate shunt Source: UniProtKB
    4. pentose-phosphate shunt, oxidative branch Source: Ensembl

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Gluconate utilization, Pentose shunt

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    UniPathwayiUPA00115; UER00410.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    6-phosphogluconate dehydrogenase, decarboxylating (EC:1.1.1.44)
    Gene namesi
    Name:Pgd
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:97553. Pgd.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 4834826-phosphogluconate dehydrogenase, decarboxylatingPRO_0000090064Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei38 – 381N6-acetyllysine1 Publication
    Modified residuei59 – 591N6-acetyllysineBy similarity
    Modified residuei257 – 2571PhosphoserineBy similarity
    Modified residuei263 – 2631PhosphothreonineBy similarity
    Modified residuei267 – 2671PhosphothreonineBy similarity
    Modified residuei270 – 2701PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9DCD0.
    PaxDbiQ9DCD0.
    PRIDEiQ9DCD0.

    PTM databases

    PhosphoSiteiQ9DCD0.

    Expressioni

    Gene expression databases

    BgeeiQ9DCD0.
    CleanExiMM_PGD.
    GenevestigatoriQ9DCD0.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    MINTiMINT-1868998.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9DCD0.
    SMRiQ9DCD0. Positions 2-470.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni129 – 1313Substrate bindingBy similarity
    Regioni187 – 1882Substrate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0362.
    GeneTreeiENSGT00390000009023.
    HOGENOMiHOG000255147.
    HOVERGENiHBG000029.
    InParanoidiQ9DCD0.
    KOiK00033.
    OMAiHFVGIGV.
    OrthoDBiEOG7K3TKV.
    PhylomeDBiQ9DCD0.
    TreeFamiTF300386.

    Family and domain databases

    Gene3Di1.10.1040.10. 1 hit.
    1.20.5.320. 1 hit.
    3.40.50.720. 1 hit.
    InterProiIPR008927. 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]
    PfamiPF00393. 6PGD. 1 hit.
    PF03446. NAD_binding_2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000109. 6PGD. 1 hit.
    SUPFAMiSSF48179. SSF48179. 1 hit.
    TIGRFAMsiTIGR00873. gnd. 1 hit.
    PROSITEiPS00461. 6PGD. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9DCD0-1 [UniParc]FASTAAdd to Basket

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    MAQADIALIG LAVMGQNLIL NMNDHGFVVC AFNRTVSKVD DFLANEAKGT    50
    KVVGAQSLKD MVSKLKKPRR VILLVKAGQA VDDFIEKLVP LLDTGDIIID 100
    GGNSEYRDTT RRCRDLKAKG ILFVGSGVSG GEEGARYGPS LMPGGNKEAW 150
    PHIKAIFQAI AAKVGTGEPC CDWVGDEGAG HFVKMVHNGI EYGDMQLICE 200
    AYHLMKDVLG MRHEEMAQAF EEWNKTELDS FLIEITANIL KYRDTDGKEL 250
    LPKIRDSAGQ KGTGKWTAIS ALEYGMPVTL IGEAVFARCL SSLKEERVQA 300
    SQKLKGPKVV QLEGSKKSFL EDIRKALYAS KIISYAQGFM LLRQAATEFG 350
    WTLNYGGIAL MWRGGCIIRS VFLGKIKDAF ERNPELQNLL LDDFFKSAVD 400
    NCQDSWRRVI STGVQAGIPM PCFTTALSFY DGYRHEMLPA NLIQAQRDYF 450
    GAHTYELLTK PGEFIHTNWT GHGGSVSSSS YNA 483
    Length:483
    Mass (Da):53,247
    Last modified:January 23, 2007 - v3
    Checksum:iCD0A3F72EEC2831E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS38974.1.
    RefSeqiNP_001074743.1. NM_001081274.1.
    UniGeneiMm.252080.

    Genome annotation databases

    EnsembliENSMUST00000084124; ENSMUSP00000081141; ENSMUSG00000028961.
    GeneIDi110208.
    KEGGimmu:110208.
    UCSCiuc008vvv.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS38974.1.
    RefSeqi NP_001074743.1. NM_001081274.1.
    UniGenei Mm.252080.

    3D structure databases

    ProteinModelPortali Q9DCD0.
    SMRi Q9DCD0. Positions 2-470.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-1868998.

    PTM databases

    PhosphoSitei Q9DCD0.

    Proteomic databases

    MaxQBi Q9DCD0.
    PaxDbi Q9DCD0.
    PRIDEi Q9DCD0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000084124 ; ENSMUSP00000081141 ; ENSMUSG00000028961 .
    GeneIDi 110208.
    KEGGi mmu:110208.
    UCSCi uc008vvv.1. mouse.

    Organism-specific databases

    CTDi 5226.
    MGIi MGI:97553. Pgd.

    Phylogenomic databases

    eggNOGi COG0362.
    GeneTreei ENSGT00390000009023.
    HOGENOMi HOG000255147.
    HOVERGENi HBG000029.
    InParanoidi Q9DCD0.
    KOi K00033.
    OMAi HFVGIGV.
    OrthoDBi EOG7K3TKV.
    PhylomeDBi Q9DCD0.
    TreeFami TF300386.

    Enzyme and pathway databases

    UniPathwayi UPA00115 ; UER00410 .

    Miscellaneous databases

    ChiTaRSi PGD. mouse.
    NextBioi 363535.
    PROi Q9DCD0.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9DCD0.
    CleanExi MM_PGD.
    Genevestigatori Q9DCD0.

    Family and domain databases

    Gene3Di 1.10.1040.10. 1 hit.
    1.20.5.320. 1 hit.
    3.40.50.720. 1 hit.
    InterProi IPR008927. 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 ]
    Pfami PF00393. 6PGD. 1 hit.
    PF03446. NAD_binding_2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000109. 6PGD. 1 hit.
    SUPFAMi SSF48179. SSF48179. 1 hit.
    TIGRFAMsi TIGR00873. gnd. 1 hit.
    PROSITEi PS00461. 6PGD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry namei6PGD_MOUSE
    AccessioniPrimary (citable) accession number: Q9DCD0
    Secondary accession number(s): Q3UD80
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 15, 2002
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 114 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3