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Protein

Carbamate kinase 1

Gene

arcC1

Organism
Enterococcus faecalis (strain ATCC 700802 / V583)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible synthesis of carbamate and ATP from carbamoyl phosphate and ADP. Can also catalyze, although with low efficiency, the phosphorylation of bicarbonate, leading to the formation of carboxyphosphate, an unstable intermediate found in the reactions catalyzed by carbamoyl-phosphate synthase and biotin carboxylase. Can also use acetate.

Catalytic activityi

ATP + NH3 + CO2 = ADP + carbamoyl phosphate.

Enzyme regulationi

Inhibited by adenosine(5')pentaphospho(5')adenosine (Ap5A), Ap6A and to a much lower extent by Ap4A.

Pathwayi: carbamoyl phosphate degradation

This protein is involved in step 1 of the subpathway that synthesizes CO(2) and NH(3) from carbamoyl phosphate.
Proteins known to be involved in this subpathway in this organism are:
  1. Carbamate kinase 1 (arcC1), Carbamate kinase 2 (arcC2)
This subpathway is part of the pathway carbamoyl phosphate degradation, which is itself part of Metabolic intermediate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes CO(2) and NH(3) from carbamoyl phosphate, the pathway carbamoyl phosphate degradation and in Metabolic intermediate metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Arginine metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEFAE226185:GHI1-96-MONOMER.
BRENDAi2.7.2.2. 2096.
SABIO-RKP0A2X7.
UniPathwayiUPA00996; UER00366.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbamate kinase 1 (EC:2.7.2.2)
Gene namesi
Name:arcC1
Synonyms:arcC, arcC-1
Ordered Locus Names:EF_0106
OrganismiEnterococcus faecalis (strain ATCC 700802 / V583)
Taxonomic identifieri226185 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesEnterococcaceaeEnterococcus
Proteomesi
  • UP000001415 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 310309Carbamate kinase 1PRO_0000185122Add
BLAST

Expressioni

Inductioni

By arginine.

Interactioni

Subunit structurei

Homodimer (predominantly) and homotetramer.

Protein-protein interaction databases

STRINGi226185.EF0106.

Structurei

Secondary structure

1
310
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85Combined sources
Helixi11 – 144Combined sources
Beta strandi15 – 173Combined sources
Helixi21 – 4020Combined sources
Beta strandi44 – 485Combined sources
Helixi52 – 6413Combined sources
Beta strandi67 – 704Combined sources
Helixi75 – 10026Combined sources
Beta strandi107 – 1104Combined sources
Beta strandi113 – 1164Combined sources
Helixi121 – 1244Combined sources
Beta strandi128 – 1347Combined sources
Helixi136 – 1438Combined sources
Turni144 – 1463Combined sources
Beta strandi149 – 1513Combined sources
Turni153 – 1553Combined sources
Beta strandi157 – 1615Combined sources
Beta strandi166 – 1694Combined sources
Helixi172 – 1809Combined sources
Beta strandi184 – 1863Combined sources
Helixi189 – 1913Combined sources
Beta strandi193 – 1964Combined sources
Turni197 – 2004Combined sources
Helixi209 – 21911Combined sources
Beta strandi223 – 2286Combined sources
Beta strandi235 – 2373Combined sources
Beta strandi244 – 2463Combined sources
Beta strandi248 – 2503Combined sources
Helixi251 – 2599Combined sources
Turni265 – 2684Combined sources
Helixi269 – 28113Combined sources
Beta strandi286 – 2905Combined sources
Helixi293 – 2975Combined sources
Beta strandi305 – 3095Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WE4X-ray2.02A/B/C/D1-310[»]
2WE5X-ray1.39A/B/C1-310[»]
ProteinModelPortaliP0A2X7.
SMRiP0A2X7. Positions 2-308.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A2X7.

Family & Domainsi

Sequence similaritiesi

Belongs to the carbamate kinase family.Curated

Phylogenomic databases

eggNOGiENOG4105C5B. Bacteria.
COG0549. LUCA.
KOiK00926.
OMAiADIFMIL.
OrthoDBiEOG65QWKX.

Family and domain databases

Gene3Di3.40.1160.10. 1 hit.
InterProiIPR001048. Asp/Glu/Uridylate_kinase.
IPR003964. Carb_kinase.
[Graphical view]
PANTHERiPTHR30409. PTHR30409. 1 hit.
PfamiPF00696. AA_kinase. 1 hit.
[Graphical view]
PIRSFiPIRSF000723. Carbamate_kin. 1 hit.
SUPFAMiSSF53633. SSF53633. 1 hit.
TIGRFAMsiTIGR00746. arcC. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A2X7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKKMVVALG GNAILSNDAS AHAQQQALVQ TSAYLVHLIK QGHRLIVSHG
60 70 80 90 100
NGPQVGNLLL QQQAADSEKN PAMPLDTCVA MTQGSIGYWL SNALNQELNK
110 120 130 140 150
AGIKKQVATV LTQVVVDPAD EAFKNPTKPI GPFLTEAEAK EAMQAGAIFK
160 170 180 190 200
EDAGRGWRKV VPSPKPIDIH EAETINTLIK NDIITISCGG GGIPVVGQEL
210 220 230 240 250
KGVEAVIDKD FASEKLAELV DADALVILTG VDYVCINYGK PDEKQLTNVT
260 270 280 290 300
VAELEEYKQA GHFAPGSMLP KIEAAIQFVE SQPNKQAIIT SLENLGSMSG
310
DEIVGTVVTK
Length:310
Mass (Da):32,927
Last modified:January 23, 2007 - v2
Checksum:iE214B3BA542A89D6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ223332 Genomic DNA. Translation: CAA11271.1.
AJ312276 Genomic DNA. Translation: CAC41343.1.
AE016830 Genomic DNA. Translation: AAO79981.1.
RefSeqiNP_813909.1. NC_004668.1.
WP_002356132.1. NZ_KE136524.1.

Genome annotation databases

EnsemblBacteriaiAAO79981; AAO79981; EF_0106.
GeneIDi1199007.
KEGGiefa:EF0106.
PATRICi21850629. VBIEntFae7065_0096.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ223332 Genomic DNA. Translation: CAA11271.1.
AJ312276 Genomic DNA. Translation: CAC41343.1.
AE016830 Genomic DNA. Translation: AAO79981.1.
RefSeqiNP_813909.1. NC_004668.1.
WP_002356132.1. NZ_KE136524.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WE4X-ray2.02A/B/C/D1-310[»]
2WE5X-ray1.39A/B/C1-310[»]
ProteinModelPortaliP0A2X7.
SMRiP0A2X7. Positions 2-308.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi226185.EF0106.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAO79981; AAO79981; EF_0106.
GeneIDi1199007.
KEGGiefa:EF0106.
PATRICi21850629. VBIEntFae7065_0096.

Phylogenomic databases

eggNOGiENOG4105C5B. Bacteria.
COG0549. LUCA.
KOiK00926.
OMAiADIFMIL.
OrthoDBiEOG65QWKX.

Enzyme and pathway databases

UniPathwayiUPA00996; UER00366.
BioCyciEFAE226185:GHI1-96-MONOMER.
BRENDAi2.7.2.2. 2096.
SABIO-RKP0A2X7.

Miscellaneous databases

EvolutionaryTraceiP0A2X7.

Family and domain databases

Gene3Di3.40.1160.10. 1 hit.
InterProiIPR001048. Asp/Glu/Uridylate_kinase.
IPR003964. Carb_kinase.
[Graphical view]
PANTHERiPTHR30409. PTHR30409. 1 hit.
PfamiPF00696. AA_kinase. 1 hit.
[Graphical view]
PIRSFiPIRSF000723. Carbamate_kin. 1 hit.
SUPFAMiSSF53633. SSF53633. 1 hit.
TIGRFAMsiTIGR00746. arcC. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Carbamate kinase from Enterococcus faecalis and Enterococcus faecium: cloning of the genes, studies on the enzyme expressed in Escherichia coli, and sequence similarity with N-acetyl-L-glutamate kinase."
    Marina A., Uriarte M., Barcelona B., Fresquet V., Cervera J., Rubio V.
    Eur. J. Biochem. 253:280-291(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
    Strain: ATCC 29212 / DSM 2570.
  2. "Gene structure, organization, expression, and potential regulatory mechanisms of arginine catabolism in Enterococcus faecalis."
    Barcelona-Andres B., Marina A., Rubio V.
    J. Bacteriol. 184:6289-6300(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 29212 / DSM 2570.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700802 / V583.

Entry informationi

Entry nameiARCC1_ENTFA
AccessioniPrimary (citable) accession number: P0A2X7
Secondary accession number(s): O54531, P35836
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 83 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

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.