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Q9RNU9

- CAPP_STRCO

UniProt

Q9RNU9 - CAPP_STRCO

Protein

Phosphoenolpyruvate carboxylase

Gene

ppc

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.UniRule annotation

    Catalytic activityi

    Phosphate + oxaloacetate = H2O + phosphoenolpyruvate + HCO3-.UniRule annotation

    Cofactori

    Magnesium.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei137 – 1371UniRule annotation
    Active sitei569 – 5691UniRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

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

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Carbon dioxide fixation

    Keywords - Ligandi

    Magnesium

    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:ppcUniRule annotation
    Ordered Locus Names:SCO3127
    ORF Names:SCE66.06c
    OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
    Taxonomic identifieri100226 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
    ProteomesiUP000001973: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 911911Phosphoenolpyruvate carboxylasePRO_0000166628Add
    BLAST

    Proteomic databases

    PRIDEiQ9RNU9.

    Interactioni

    Protein-protein interaction databases

    STRINGi100226.SCO3127.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9RNU9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PEPCase type 1 family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG2352.
    HOGENOMiHOG000238647.
    KOiK01595.
    OMAiELSTISC.
    OrthoDBiEOG6TJ7T8.
    PhylomeDBiQ9RNU9.

    Family and domain databases

    HAMAPiMF_00595. PEPcase_type1.
    InterProiIPR021135. PEP_COase.
    IPR018129. PEP_COase_AS.
    IPR022805. PEP_COase_bac/pln-type.
    IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
    [Graphical view]
    PfamiPF00311. PEPcase. 1 hit.
    [Graphical view]
    PRINTSiPR00150. PEPCARBXLASE.
    SUPFAMiSSF51621. SSF51621. 1 hit.
    PROSITEiPS00781. PEPCASE_1. 1 hit.
    PS00393. PEPCASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9RNU9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSADDQTTT TTSSELRADI RRLGDLLGET LVRQEGPELL ELVEKVRRLT    50
    REDGEAAAEL LRGTELETAA KLVRAFSTYF HLANVTEQVH RGRELGAKRA 100
    AEGGLLARTA DRLKDADPEH LRETVRNLNV RPVFTAHPTE AARRSVLNKL 150
    RRIAALLDTP VNESDRRRLD TRLAENIDLV WQTDELRVVR PEPADEARNA 200
    IYYLDELHLG AVGDVLEDLT AELERAGVKL PDDTRPLTFG TWIGGDRDGN 250
    PNVTPQVTWD VLILQHEHGI NDALEMIDEL RGFLSNSIRY AGATEELLAS 300
    LQADLERLPE ISPRYKRLNA EEPYRLKATC IRQKLENTKQ RLAKGTPHED 350
    GRDYLGTAQL IDDLRIVQTS LREHRGGLFA DGRLARTIRT LAAFGLQLAT 400
    MDVREHADAH HHALGQLFDR LGEESWRYAD MPREYRTKLL AKELRSRRPL 450
    APSPAPVDAP GEKTLGVFQT VRRALEVFGP EVIESYIISM CQGADDVFAA 500
    AVLAREAGLI DLHAGWAKIG IVPLLETTDE LKAADTILED LLADPSYRRL 550
    VALRGDVQEV MLGYSDSSKF GGITTSQWEI HRAQRRLRDV AHRYGVRLRL 600
    FHGRGGTVGR GGGPTHDAIL AQPWGTLEGE IKVTEQGEVI SDKYLIPALA 650
    RENLELTVAA TLQASALHTA PRQSDEALAR WDAAMDVVSD AAHTAYRHLV 700
    EDPDLPTYFL ASTPVDQLAD LHLGSRPSRR PGSGVSLDGL RAIPWVFGWT 750
    QSRQIVPGWY GVGSGLKALR EAGLDTVLDE MHQQWHFFRN FISNVEMTLA 800
    KTDLRIAQHY VDTLVPDELK HVFDTIKAEH ELTVAEVLRV TGESELLDAD 850
    PVLKQTFTIR DAYLDPISYL QVALLGRQRE AAAANEDPDP LLARALLLTV 900
    NGVAAGLRNT G 911
    Length:911
    Mass (Da):101,297
    Last modified:May 1, 2000 - v1
    Checksum:i5192E0BB96881273
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF177946 Genomic DNA. Translation: AAD53311.1.
    AF160253 Genomic DNA. Translation: AAM54458.1.
    AL939115 Genomic DNA. Translation: CAB95920.1.
    RefSeqiNP_627344.1. NC_003888.3.

    Genome annotation databases

    EnsemblBacteriaiCAB95920; CAB95920; CAB95920.
    GeneIDi1098561.
    KEGGisco:SCO3127.
    PATRICi23736002. VBIStrCoe124346_3191.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF177946 Genomic DNA. Translation: AAD53311.1 .
    AF160253 Genomic DNA. Translation: AAM54458.1 .
    AL939115 Genomic DNA. Translation: CAB95920.1 .
    RefSeqi NP_627344.1. NC_003888.3.

    3D structure databases

    ProteinModelPortali Q9RNU9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 100226.SCO3127.

    Proteomic databases

    PRIDEi Q9RNU9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB95920 ; CAB95920 ; CAB95920 .
    GeneIDi 1098561.
    KEGGi sco:SCO3127.
    PATRICi 23736002. VBIStrCoe124346_3191.

    Phylogenomic databases

    eggNOGi COG2352.
    HOGENOMi HOG000238647.
    KOi K01595.
    OMAi ELSTISC.
    OrthoDBi EOG6TJ7T8.
    PhylomeDBi Q9RNU9.

    Family and domain databases

    HAMAPi MF_00595. PEPcase_type1.
    InterProi IPR021135. PEP_COase.
    IPR018129. PEP_COase_AS.
    IPR022805. PEP_COase_bac/pln-type.
    IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
    [Graphical view ]
    Pfami PF00311. PEPcase. 1 hit.
    [Graphical view ]
    PRINTSi PR00150. PEPCARBXLASE.
    SUPFAMi SSF51621. SSF51621. 1 hit.
    PROSITEi PS00781. PEPCASE_1. 1 hit.
    PS00393. PEPCASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Phosphoenolpyruvate carboxylase from Streptomyces coelicolor A3(2): purification of the enzyme, cloning of the ppc gene and over-expression of the protein in a streptomycete."
      Bramwell H., Nimmo H.G., Hunter I.S., Coggins J.R.
      Biochem. J. 293:131-136(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
      Strain: A3(2) / NRRL B-16638.
    2. "The ppc gene of Streptomyces coelicolor A3(2)."
      Ricketts A.D.J., Hunter I.S.
      Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: A3(2) / NRRL B-16638.
    3. "Characterization of the phosphoenolpyruvate carboxylase gene from Streptomyces coelicolor A3(2) and a ppc gene disruption mutant."
      Alves A.M.C.R., te Poele E., White J., Bibb M.J., Dijkhuizen L.
      Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: A3(2) / NRRL B-16638.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-471 / A3(2) / M145.

    Entry informationi

    Entry nameiCAPP_STRCO
    AccessioniPrimary (citable) accession number: Q9RNU9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2002
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 86 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3