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P95474 (CPKA_PYRFU) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carbamate kinase

EC=2.7.2.2
Alternative name(s):
Carbamate kinase-like carbamoylphosphate synthase
Gene names
Name:cpkA
Synonyms:cpa
Ordered Locus Names:PF0676
OrganismPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) [Reference proteome] [HAMAP]
Taxonomic identifier186497 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length314 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Carbamate kinase that plays a biosynthetic role in that it produces carbamoyl-phosphate. Ref.4

Catalytic activity

ATP + NH3 + CO2 = ADP + carbamoyl phosphate.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the carbamate kinase family.

Biophysicochemical properties

Temperature dependence:

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

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processarginine metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

carbamate kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 314314Carbamate kinase
PRO_0000185149

Secondary structure

......................................................... 314
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P95474 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: B4496B827581EF42

FASTA31434,429
        10         20         30         40         50         60 
MGKRVVIALG GNALQQRGQK GSYEEMMDNV RKTARQIAEI IARGYEVVIT HGNGPQVGSL 

        70         80         90        100        110        120 
LLHMDAGQAT YGIPAQPMDV AGAMSQGWIG YMIQQALKNE LRKRGMEKKV VTIITQTIVD 

       130        140        150        160        170        180 
KNDPAFQNPT KPVGPFYDEE TAKRLAREKG WIVKEDSGRG WRRVVPSPDP KGHVEAETIK 

       190        200        210        220        230        240 
KLVERGVIVI ASGGGGVPVI LEDGEIKGVE AVIDKDLAGE KLAEEVNADI FMILTDVNGA 

       250        260        270        280        290        300 
ALYYGTEKEQ WLREVKVEEL RKYYEEGHFK AGSMGPKVLA AIRFIEWGGE RAIIAHLEKA 

       310 
VEALEGKTGT QVLP 

« Hide

References

« Hide 'large scale' references
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y09829 Genomic DNA. Translation: CAA70972.1.
AB016521 Genomic DNA. Translation: BAA32017.1.
AE009950 Genomic DNA. Translation: AAL80800.1.
PIRT43855.
RefSeqNP_578405.1. NC_003413.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E19X-ray1.50A/B1-314[»]
ProteinModelPortalP95474.
SMRP95474. Positions 2-314.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING186497.PF0676.

Proteomic databases

PRIDEP95474.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL80800; AAL80800; PF0676.
GeneID1468522.
KEGGpfu:PF0676.

Phylogenomic databases

eggNOGCOG0549.
HOGENOMHOG000277403.
KOK00926.
OMAADIFMIL.
ProtClustDBPRK12454.

Family and domain databases

Gene3D3.40.1160.10. 1 hit.
InterProIPR001048. Asp/Glu/Uridylate_kinase.
IPR003964. Bac_carb_kinase.
[Graphical view]
PfamPF00696. AA_kinase. 1 hit.
[Graphical view]
PIRSFPIRSF000723. Carbamate_kin. 1 hit.
PRINTSPR01469. CARBMTKINASE.
SUPFAMSSF53633. SSF53633. 1 hit.
TIGRFAMsTIGR00746. arcC. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP95474.

Entry information

Entry nameCPKA_PYRFU
AccessionPrimary (citable) accession number: P95474
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: May 1, 1997
Last modified: December 11, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references