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P20007

- PCKG_DROME

UniProt

P20007 - PCKG_DROME

Protein

Phosphoenolpyruvate carboxykinase [GTP]

Gene

Pepck

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 2 (01 Dec 2000)
      Previous versions | rss
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    Functioni

    Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle.By similarity

    Catalytic activityi

    GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO2.

    Cofactori

    Binds 1 manganese ion per subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei112 – 1121SubstrateBy similarity
    Binding sitei263 – 2631Substrate; via amide nitrogenBy similarity
    Metal bindingi270 – 2701ManganeseBy similarity
    Binding sitei270 – 2701SubstrateBy similarity
    Metal bindingi290 – 2901Manganese; via tele nitrogenBy similarity
    Binding sitei312 – 3121SubstrateBy similarity
    Active sitei314 – 3141By similarity
    Metal bindingi337 – 3371ManganeseBy similarity
    Binding sitei431 – 4311GTPBy similarity
    Binding sitei462 – 4621GTPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi313 – 3186GTPBy similarity
    Nucleotide bindingi554 – 5574GTPBy similarity

    GO - Molecular functioni

    1. GTP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. phosphoenolpyruvate carboxykinase (GTP) activity Source: UniProtKB-EC

    GO - Biological processi

    1. gluconeogenesis Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Decarboxylase, Lyase

    Keywords - Biological processi

    Gluconeogenesis

    Keywords - Ligandi

    GTP-binding, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_184366. Abacavir metabolism.
    REACT_220315. Gluconeogenesis.
    UniPathwayiUPA00138.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoenolpyruvate carboxykinase [GTP] (EC:4.1.1.32)
    Short name:
    PEPCK
    Gene namesi
    Name:Pepck
    Synonyms:ZDF4
    ORF Names:CG17725
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2R

    Organism-specific databases

    FlyBaseiFBgn0003067. Pepck.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 647647Phosphoenolpyruvate carboxykinase [GTP]PRO_0000103635Add
    BLAST

    Proteomic databases

    PaxDbiP20007.
    PRIDEiP20007.

    Expressioni

    Gene expression databases

    BgeeiP20007.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    BioGridi62806. 3 interactions.
    DIPiDIP-22737N.
    MINTiMINT-762297.
    STRINGi7227.FBpp0085880.

    Structurei

    3D structure databases

    ProteinModelPortaliP20007.
    SMRiP20007. Positions 43-647.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni429 – 4313Substrate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1274.
    GeneTreeiENSGT00390000001912.
    InParanoidiP20007.
    KOiK01596.
    OMAiPDHIHIC.
    OrthoDBiEOG7KSX81.
    PhylomeDBiP20007.

    Family and domain databases

    Gene3Di3.40.449.10. 1 hit.
    3.90.228.20. 2 hits.
    HAMAPiMF_00452. PEPCK_GTP.
    InterProiIPR018091. PEP_carboxykin_GTP_CS.
    IPR013035. PEP_carboxykinase_C.
    IPR008209. PEP_carboxykinase_GTP.
    IPR008210. PEP_carboxykinase_N.
    [Graphical view]
    PANTHERiPTHR11561. PTHR11561. 1 hit.
    PfamiPF00821. PEPCK. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001348. PEP_carboxykinase_GTP. 1 hit.
    SUPFAMiSSF68923. SSF68923. 1 hit.
    PROSITEiPS00505. PEPCK_GTP. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform A (identifier: P20007-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MPELIEQSKI ISGNVCGLPQ LHKLRQDNCG LYSHIRGIPI SYGNVDLLTT    50
    GVRAFVEEGI ALCQPDQVHI CDGSEQENKV LIKSLLEAGT IVPLPKYDNC 100
    WLARTNPADV ARVESRTFIC TERREETIPT PVEGVKGTLG NWISPSDMDA 150
    AVQQRFPGCM KGRTMYVVPF SMGPVGSPLS KIGIELTDSA YVVASMRIMT 200
    RMGAAVLRQL AKKEEFVRAL HSVGAPANGQ VEQPSWPCDP ERTIILHKPA 250
    ENLIVSYGSG YGGNSLLGKK CFALRIGSTI AKQEGWLAEH MLILGITDPK 300
    GEKKYITAAF PSACGKTNLA MLNPSLANYK VECVGDDIAW MKFDSQGVLR 350
    AINPENGFFG VAPGTSMETN PIAMNTVFKN TIFTNVASTS DGGVFWEGME 400
    SSLAPNVQIT DWLGKPWTKD SGKPAAHPNS RFCTPAAQCP IIDEAWEDPA 450
    GVPISAMLFG GRRPAGVPLI YEARDWTHGV FIGAAMRSEA TAAAEHKGKV 500
    IMHDPFAMRP FFGYNFGDYV AHWLSMEKRG QVPKIFHVNW FRKSAEGKFM 550
    WPGYGENSRV LEWILRRVNG ESCYVDSAIG HIPAEGALNL DGMKDKVDVK 600
    EIFSLPKEFW SQEVKDIRTY FESQVGADLP ASIYQQLDEL SSRVDNL 647
    Length:647
    Mass (Da):71,129
    Last modified:December 1, 2000 - v2
    Checksum:i0DB81B3D9E1B1FBB
    GO
    Isoform B (identifier: P20007-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-147: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:500
    Mass (Da):54,949
    Checksum:iF49B9BEAD8D0E15E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti302 – 3021E → V in CAA68463. (PubMed:3114718)Curated
    Sequence conflicti408 – 4081Q → R in CAA68463. (PubMed:3114718)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 147147Missing in isoform B. CuratedVSP_026173Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00402 mRNA. Translation: CAA68463.1.
    AE013599 Genomic DNA. Translation: AAF57676.1.
    AE013599 Genomic DNA. Translation: AAM68462.1.
    BT003447 mRNA. Translation: AAO39450.1.
    PIRiA26809. QYFFGM.
    RefSeqiNP_523784.2. NM_079060.2. [P20007-1]
    NP_725802.1. NM_166293.1. [P20007-2]
    UniGeneiDm.6919.

    Genome annotation databases

    EnsemblMetazoaiFBtr0086701; FBpp0085880; FBgn0003067. [P20007-1]
    GeneIDi37131.
    KEGGidme:Dmel_CG17725.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00402 mRNA. Translation: CAA68463.1 .
    AE013599 Genomic DNA. Translation: AAF57676.1 .
    AE013599 Genomic DNA. Translation: AAM68462.1 .
    BT003447 mRNA. Translation: AAO39450.1 .
    PIRi A26809. QYFFGM.
    RefSeqi NP_523784.2. NM_079060.2. [P20007-1 ]
    NP_725802.1. NM_166293.1. [P20007-2 ]
    UniGenei Dm.6919.

    3D structure databases

    ProteinModelPortali P20007.
    SMRi P20007. Positions 43-647.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 62806. 3 interactions.
    DIPi DIP-22737N.
    MINTi MINT-762297.
    STRINGi 7227.FBpp0085880.

    Proteomic databases

    PaxDbi P20007.
    PRIDEi P20007.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0086701 ; FBpp0085880 ; FBgn0003067 . [P20007-1 ]
    GeneIDi 37131.
    KEGGi dme:Dmel_CG17725.

    Organism-specific databases

    CTDi 37131.
    FlyBasei FBgn0003067. Pepck.

    Phylogenomic databases

    eggNOGi COG1274.
    GeneTreei ENSGT00390000001912.
    InParanoidi P20007.
    KOi K01596.
    OMAi PDHIHIC.
    OrthoDBi EOG7KSX81.
    PhylomeDBi P20007.

    Enzyme and pathway databases

    UniPathwayi UPA00138 .
    Reactomei REACT_184366. Abacavir metabolism.
    REACT_220315. Gluconeogenesis.

    Miscellaneous databases

    ChiTaRSi PCK2. drosophila.
    GenomeRNAii 37131.
    NextBioi 802101.

    Gene expression databases

    Bgeei P20007.

    Family and domain databases

    Gene3Di 3.40.449.10. 1 hit.
    3.90.228.20. 2 hits.
    HAMAPi MF_00452. PEPCK_GTP.
    InterProi IPR018091. PEP_carboxykin_GTP_CS.
    IPR013035. PEP_carboxykinase_C.
    IPR008209. PEP_carboxykinase_GTP.
    IPR008210. PEP_carboxykinase_N.
    [Graphical view ]
    PANTHERi PTHR11561. PTHR11561. 1 hit.
    Pfami PF00821. PEPCK. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001348. PEP_carboxykinase_GTP. 1 hit.
    SUPFAMi SSF68923. SSF68923. 1 hit.
    PROSITEi PS00505. PEPCK_GTP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide and deduced amino acid sequence of the phosphoenolpyruvate carboxykinase (GTP) from Drosophila melanogaster."
      Gundelfinger E.D., Hermans-Borgmeyer I., Grenningloh G., Zopf D.
      Nucleic Acids Res. 15:6745-6745(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
      Strain: Canton-S.
      Tissue: Head.
    2. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    3. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
      Strain: Berkeley.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
      Strain: Berkeley.
      Tissue: Head.

    Entry informationi

    Entry nameiPCKG_DROME
    AccessioniPrimary (citable) accession number: P20007
    Secondary accession number(s): A1ZB97, Q53YF8, Q9V8J0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: December 1, 2000
    Last modified: October 1, 2014
    This is version 118 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3