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Q05893

- PCKG_ASCSU

UniProt

Q05893 - PCKG_ASCSU

Protein

Phosphoenolpyruvate carboxykinase [GTP]

Gene

PEPCK

Organism
Ascaris suum (Pig roundworm) (Ascaris lumbricoides)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 1 (01 Feb 1994)
      Previous versions | rss
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    Functioni

    In parasitic nematodes PEPCK carboxylates phosphoenolpyruvate to oxaloacetate thus introducing the products of glycolysis to mitochondrial metabolism.
    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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei102 – 1021SubstrateBy similarity
    Binding sitei255 – 2551Substrate; via amide nitrogenBy similarity
    Metal bindingi262 – 2621ManganeseBy similarity
    Binding sitei262 – 2621SubstrateBy similarity
    Metal bindingi282 – 2821Manganese; via tele nitrogenBy similarity
    Binding sitei304 – 3041SubstrateBy similarity
    Active sitei306 – 3061By similarity
    Metal bindingi329 – 3291ManganeseBy similarity
    Binding sitei424 – 4241GTPBy similarity
    Binding sitei455 – 4551GTPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi305 – 3106GTPBy similarity
    Nucleotide bindingi548 – 5514GTPBy 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: InterPro

    Keywords - Molecular functioni

    Decarboxylase, Lyase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-18260.
    SABIO-RKQ05893.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoenolpyruvate carboxykinase [GTP] (EC:4.1.1.32)
    Short name:
    PEPCK
    Gene namesi
    Name:PEPCK
    OrganismiAscaris suum (Pig roundworm) (Ascaris lumbricoides)
    Taxonomic identifieri6253 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaAscarididaAscaridoideaAscarididaeAscaris

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 643643Phosphoenolpyruvate carboxykinase [GTP]PRO_0000103632Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    3D structure databases

    ProteinModelPortaliQ05893.
    SMRiQ05893. Positions 27-641.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni422 – 4243Substrate bindingBy similarity

    Sequence similaritiesi

    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]

    Sequencei

    Sequence statusi: Complete.

    Q05893-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRCRSLSHFK DDDFAVVSEV VTHKQNHIPV IKGDFVSLPK HVQRFVAEKA    50
    ELMKPSAIFI CDGSQNEADE LIARCVERGV LVPLKAYKNN YLCRTDPRDV 100
    ARVESKTWMI TPEKYDSVCH TPEGVKPMMG QWMSPDEFGK ELDDRFPGCM 150
    AGRTMYVIPY SMGPVGGPLS KIGIELTDSD YVVLCMRIMT RMGEPVLKAL 200
    AKNNGEFVRC VHSVGQPKPV ATKVINHWPC NPEKTIIAHR PAEREIWSFG 250
    SGYGGNSLLG KKCFALRIAM NIGYDEGWMA EHMLIMGVTS PKGEERFVAA 300
    AFPSACGKTN LAMLEPTIPG WKVRVIGDDI AWMKFGADGR LYAINPEYGF 350
    FGVAPGTSHK TNPMAMASFQ ENTIFTNVAE TADGEYFWEG LEHEVKNPKV 400
    DMINWLGEPW HIGDESKAAH PNSRFTAPAG QCPIIHPDWE KPEGVPIDAI 450
    IFGGRRPEGV PLVFESRSWV HGIFVGACVK SEATAAAEHT GKQVMHDPMA 500
    MRPFMGYNFG RYMRHWMKLG QPPHKVPKIF HVNWFRQSAD HKFLWPGYGD 550
    NIRVIDWILR RCSGDATIAE ETPIGFIPKK GTINLEGLPN VNWDELMSIP 600
    KSYWLEDMVE TKTFFENQVG SDLPPEIAKE LEAQTERIKA LKE 643
    Length:643
    Mass (Da):72,230
    Last modified:February 1, 1994 - v1
    Checksum:iA9C369959AA79E27
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L01787 mRNA. Translation: AAA29378.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L01787 mRNA. Translation: AAA29378.1 .

    3D structure databases

    ProteinModelPortali Q05893.
    SMRi Q05893. Positions 27-641.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-18260.
    SABIO-RK Q05893.

    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. "Ascaris suum: cloning of a cDNA encoding phosphoenolpyruvate carboxykinase."
      Geary T.G., Winterrowd C.A., Alexander-Bowman S.J., Favreau M.A., Nulf S.C., Klein R.D.
      Exp. Parasitol. 77:155-161(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Nerve cord and Pharynx.

    Entry informationi

    Entry nameiPCKG_ASCSU
    AccessioniPrimary (citable) accession number: Q05893
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: February 1, 1994
    Last modified: October 1, 2014
    This is version 69 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3