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Q4JCJ1

- CAPPA_SULAC

UniProt

Q4JCJ1 - CAPPA_SULAC

Protein

Phosphoenolpyruvate carboxylase

Gene

ppcA

Organism
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 47 (01 Oct 2014)
      Sequence version 2 (13 Nov 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.1 PublicationUniRule annotation

    Catalytic activityi

    Phosphate + oxaloacetate = H2O + phosphoenolpyruvate + HCO3-.1 PublicationUniRule annotation

    Cofactori

    Magnesium. Mg2+ can not be replaced by Mn2+.1 PublicationUniRule annotation

    Enzyme regulationi

    Allosterically inhibited by L-aspartate and L-malate. PEPC activity is not affected by allosteric activators of E.coli PEPC such as glucose 6-phosphate, fructose 1,6-bisphosphate, and acetyl coenzyme A.1 Publication

    Kineticsi

    1. KM=0.20 mM for phosphoenolpyruvate1 Publication

    pH dependencei

    Optimum pH is 8.0.1 Publication

    Temperature dependencei

    Optimum temperature is 90 degrees Celsius. Is extremely thermostable. No loss of activity is observed after incubation for 2 hours at 80 degrees Celsius. The times required for 50% loss of activity are about 60 minutes at 90 degrees Celsius, 10 minutes at 95 degrees Celsius, and 1 minute at 100 degrees Celsius.1 Publication

    GO - Molecular functioni

    1. magnesium ion binding Source: UniProtKB
    2. phosphoenolpyruvate carboxylase activity Source: UniProtKB

    GO - Biological processi

    1. carbon fixation Source: UniProtKB
    2. oxaloacetate metabolic process Source: UniProtKB
    3. tricarboxylic acid cycle Source: InterPro

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Carbon dioxide fixation

    Keywords - Ligandi

    Magnesium

    Enzyme and pathway databases

    BioCyciSACI330779:GH9J-59-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoenolpyruvate carboxylaseUniRule annotation (EC:4.1.1.31UniRule annotation)
    Short name:
    PEPCUniRule annotation
    Short name:
    PEPCaseUniRule annotation
    Gene namesi
    Name:ppcAUniRule annotation
    Ordered Locus Names:Saci_0059
    OrganismiSulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
    Taxonomic identifieri330779 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
    ProteomesiUP000001018: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 511511Phosphoenolpyruvate carboxylasePRO_0000309614Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.1 PublicationUniRule annotation

    Protein-protein interaction databases

    STRINGi330779.Saci_0059.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PEPCase type 2 family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1892.
    HOGENOMiHOG000038601.
    KOiK01595.

    Family and domain databases

    HAMAPiMF_01904. PEPcase_type2.
    InterProiIPR007566. PEP_COase_arc-type.
    IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
    [Graphical view]
    PfamiPF14010. PEPcase_2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF006677. UCP006677. 1 hit.
    SUPFAMiSSF51621. SSF51621. 1 hit.
    TIGRFAMsiTIGR02751. PEPCase_arch. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q4JCJ1-1 [UniParc]FASTAAdd to Basket

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    MRKIPRTMST QHPDNAKVPE WNQGEAISGE NEIIEAYLAF SRYGVEEVMW    50
    DAEGKDVDTH VVRKLLSQYP EFFRHRILGK DIFLTYRVPN PKIEGAERKV 100
    FAETLNTIPI TYDLAEKFYG ENPNPPVFEV ILPFTTSYEE LIAVIKFYEK 150
    VIVNSDNTKL VDDTYVKDII GETNPKKIEV IPLIEDRDSM LRIDTIVGKY 200
    IEIERPPYLR VFLARSDPAM NYGLLSAVLS VKYALSRLSK MEKIYGVKIF 250
    PLLGVGSLPF RGHFSPYNVE NTLNEYRGIY TFTVQSAFKY DYEDDLVISA 300
    IKKVNGTNVT EKIELSEEDE EIISNVTRKY TQGYQNKIEA LADVINKVAL 350
    LLPRRRARKL HIGLFGYSRS TGKVTLPRAI SFVGSLYTIG IPPEIIGLSS 400
    LSKMTDQELN AIFNNYKYLK NDLQFAARFV NFEALQLLKD IWNIDAEVVK 450
    AIKEDIDYAE NSLGIRIGES DYMSKKHVLL STLALLSIKE GKLDEAKTYI 500
    KEMAIVRRAI G 511
    Length:511
    Mass (Da):58,355
    Last modified:November 13, 2007 - v2
    Checksum:i1337C9AF4012A917
    GO

    Sequence cautioni

    The sequence AAY79488.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000077 Genomic DNA. Translation: AAY79488.1. Different initiation.
    RefSeqiYP_254781.1. NC_007181.1.

    Genome annotation databases

    EnsemblBacteriaiAAY79488; AAY79488; Saci_0059.
    GeneIDi3472974.
    KEGGisai:Saci_0059.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000077 Genomic DNA. Translation: AAY79488.1 . Different initiation.
    RefSeqi YP_254781.1. NC_007181.1.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 330779.Saci_0059.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAY79488 ; AAY79488 ; Saci_0059 .
    GeneIDi 3472974.
    KEGGi sai:Saci_0059.

    Phylogenomic databases

    eggNOGi COG1892.
    HOGENOMi HOG000038601.
    KOi K01595.

    Enzyme and pathway databases

    BioCyci SACI330779:GH9J-59-MONOMER.

    Family and domain databases

    HAMAPi MF_01904. PEPcase_type2.
    InterProi IPR007566. PEP_COase_arc-type.
    IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
    [Graphical view ]
    Pfami PF14010. PEPcase_2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF006677. UCP006677. 1 hit.
    SUPFAMi SSF51621. SSF51621. 1 hit.
    TIGRFAMsi TIGR02751. PEPCase_arch. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota."
      Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E., Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.
      J. Bacteriol. 187:4992-4999(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770.
    2. "Biochemical relationship of phosphoenolpyruvate carboxylases (PEPCs) from thermophilic archaea."
      Sako Y., Takai K., Nishizaka T., Ishida Y.
      FEMS Microbiol. Lett. 153:159-165(1997)
      Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
      Strain: ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770.

    Entry informationi

    Entry nameiCAPPA_SULAC
    AccessioniPrimary (citable) accession number: Q4JCJ1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2007
    Last sequence update: November 13, 2007
    Last modified: October 1, 2014
    This is version 47 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzyme, Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3