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P95474

- CPKA_PYRFU

UniProt

P95474 - CPKA_PYRFU

Protein

Carbamate kinase

Gene

cpkA

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
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    Functioni

    Carbamate kinase that plays a biosynthetic role in that it produces carbamoyl-phosphate.1 Publication

    Catalytic activityi

    ATP + NH3 + CO2 = ADP + carbamoyl phosphate.

    Temperature dependencei

    50% activity is retained after 1 hour at 100 degrees Celsius or 3 hours at 95 degrees Celsius.

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. carbamate kinase activity Source: UniProtKB-EC

    GO - Biological processi

    1. arginine metabolic process Source: InterPro

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carbamate kinase (EC:2.7.2.2)
    Alternative name(s):
    Carbamate kinase-like carbamoylphosphate synthase
    Gene namesi
    Name:cpkA
    Synonyms:cpa
    Ordered Locus Names:PF0676
    OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
    Taxonomic identifieri186497 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
    ProteomesiUP000001013: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 314314Carbamate kinasePRO_0000185149Add
    BLAST

    Proteomic databases

    PRIDEiP95474.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    STRINGi186497.PF0676.

    Structurei

    Secondary structure

    1
    314
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 85
    Helixi11 – 133
    Helixi23 – 4220
    Beta strandi46 – 505
    Helixi54 – 7118
    Helixi78 – 10326
    Beta strandi110 – 1134
    Beta strandi116 – 1194
    Helixi124 – 1263
    Beta strandi131 – 1377
    Helixi139 – 14911
    Beta strandi152 – 1554
    Beta strandi161 – 1655
    Beta strandi170 – 1734
    Helixi176 – 1849
    Beta strandi188 – 1903
    Helixi193 – 1953
    Beta strandi197 – 2026
    Beta strandi205 – 2084
    Helixi215 – 22511
    Beta strandi229 – 23911
    Turni243 – 2453
    Beta strandi254 – 2563
    Helixi257 – 2659
    Turni271 – 2733
    Helixi274 – 28714
    Beta strandi290 – 2967
    Helixi297 – 2993
    Helixi300 – 3045
    Beta strandi307 – 3137

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1E19X-ray1.50A/B1-314[»]
    ProteinModelPortaliP95474.
    SMRiP95474. Positions 2-314.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP95474.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the carbamate kinase family.Curated

    Phylogenomic databases

    eggNOGiCOG0549.
    HOGENOMiHOG000277403.
    KOiK00926.
    OMAiKGTYEEQ.

    Family and domain databases

    Gene3Di3.40.1160.10. 1 hit.
    InterProiIPR001048. Asp/Glu/Uridylate_kinase.
    IPR003964. Carb_kinase.
    [Graphical view]
    PfamiPF00696. AA_kinase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000723. Carbamate_kin. 1 hit.
    PRINTSiPR01469. CARBMTKINASE.
    SUPFAMiSSF53633. SSF53633. 1 hit.
    TIGRFAMsiTIGR00746. arcC. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P95474-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGKRVVIALG GNALQQRGQK GSYEEMMDNV RKTARQIAEI IARGYEVVIT    50
    HGNGPQVGSL LLHMDAGQAT YGIPAQPMDV AGAMSQGWIG YMIQQALKNE 100
    LRKRGMEKKV VTIITQTIVD KNDPAFQNPT KPVGPFYDEE TAKRLAREKG 150
    WIVKEDSGRG WRRVVPSPDP KGHVEAETIK KLVERGVIVI ASGGGGVPVI 200
    LEDGEIKGVE AVIDKDLAGE KLAEEVNADI FMILTDVNGA ALYYGTEKEQ 250
    WLREVKVEEL RKYYEEGHFK AGSMGPKVLA AIRFIEWGGE RAIIAHLEKA 300
    VEALEGKTGT QVLP 314
    Length:314
    Mass (Da):34,429
    Last modified:May 1, 1997 - v1
    Checksum:iB4496B827581EF42
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y09829 Genomic DNA. Translation: CAA70972.1.
    AB016521 Genomic DNA. Translation: BAA32017.1.
    AE009950 Genomic DNA. Translation: AAL80800.1.
    PIRiT43855.
    RefSeqiNP_578405.1. NC_003413.1.

    Genome annotation databases

    EnsemblBacteriaiAAL80800; AAL80800; PF0676.
    GeneIDi1468522.
    KEGGipfu:PF0676.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y09829 Genomic DNA. Translation: CAA70972.1 .
    AB016521 Genomic DNA. Translation: BAA32017.1 .
    AE009950 Genomic DNA. Translation: AAL80800.1 .
    PIRi T43855.
    RefSeqi NP_578405.1. NC_003413.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1E19 X-ray 1.50 A/B 1-314 [» ]
    ProteinModelPortali P95474.
    SMRi P95474. Positions 2-314.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 186497.PF0676.

    Proteomic databases

    PRIDEi P95474.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAL80800 ; AAL80800 ; PF0676 .
    GeneIDi 1468522.
    KEGGi pfu:PF0676.

    Phylogenomic databases

    eggNOGi COG0549.
    HOGENOMi HOG000277403.
    KOi K00926.
    OMAi KGTYEEQ.

    Miscellaneous databases

    EvolutionaryTracei P95474.

    Family and domain databases

    Gene3Di 3.40.1160.10. 1 hit.
    InterProi IPR001048. Asp/Glu/Uridylate_kinase.
    IPR003964. Carb_kinase.
    [Graphical view ]
    Pfami PF00696. AA_kinase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000723. Carbamate_kin. 1 hit.
    PRINTSi PR01469. CARBMTKINASE.
    SUPFAMi SSF53633. SSF53633. 1 hit.
    TIGRFAMsi TIGR00746. arcC. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The carbamate kinase-like carbamoyl phosphate synthetase of the hyperthermophilic archaeon Pyrococcus furiosus, a missing link in the evolution of carbamoyl phosphate biosynthesis."
      Durbecq V., Legrain C., Roovers M., Pierard A., Glansdorff N.
      Proc. Natl. Acad. Sci. U.S.A. 94:12803-12808(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
    2. "Pfu helicase locus."
      Kanai A., Oida H., Yabe T., Hihara S., Doi H.
      Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
    3. "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
      Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
      Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
    4. "The 1.5-A resolution crystal structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic Archaeon Pyrococcus furiosus, bound to ADP, confirms that this thermostable enzyme is a carbamate kinase, and provides insight into substrate binding and stability in carbamate kinases."
      Ramon-Maiques S., Marina A., Uriarte M., Fita I., Rubio V.
      J. Mol. Biol. 299:463-476(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), FUNCTION.
      Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.

    Entry informationi

    Entry nameiCPKA_PYRFU
    AccessioniPrimary (citable) accession number: P95474
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 29, 2001
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 95 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3