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Reviewed, UniProtKB/Swiss-Prot A4JC42 (URE1_BURVG)

Last modified November 3, 2009. Version 22. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Urease subunit alpha
    EC=3.5.1.5
Alternative name(s):
    Urea amidohydrolase subunit alpha
Gene names
Name: ureC
Ordered Locus Names: Bcep1808_0833
OrganismBurkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia (strain R1808)) [Complete proteome] [HAMAP]
Taxonomic identifier269482 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length568 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

Urea + H2O = CO2 + 2 NH3. HAMAP MF_01953

Cofactor

Binds 2 nickel ions per subunit By similarity.

Pathway

Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1. HAMAP MF_01953

Subunit structure

Heterotrimer of ureA (gamma), ureB (beta) and ureC (alpha) subunits. Three heterotrimers associate to form the active enzyme By similarity.

Subcellular location

Cytoplasm By similarity.

Post-translational modification

Carbamylation allows a single lysine to coordinate two nickel ions By similarity.

Sequence similarities

Belongs to the urease family.

Contains 1 urease domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
Nickel
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processurea metabolic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionnickel ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

urease activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 568568Urease subunit alpha HAMAP MF_01953
PRO_1000073701

Regions

Domain130 – 568439Urease

Sites

Active site3211Proton donor By similarity
Metal binding1351Nickel 2 By similarity
Metal binding1371Nickel 2 By similarity
Metal binding2181Nickel 1; via carbamate group By similarity
Metal binding2181Nickel 2; via carbamate group By similarity
Metal binding2471Nickel 1 By similarity
Metal binding2731Nickel 1 By similarity
Metal binding3611Nickel 2 By similarity
Binding site2201Substrate By similarity

Amino acid modifications

Modified residue2181N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A4JC42-1 [UniParc].

Last modified May 1, 2007. Version 1.
Checksum: 73EF5C10FCF33794

FASTA56861,031
        10         20         30         40         50         60 
MTLRLSRRAY AEMFGPTTGD RVRLADTELL IEIERDYTIY GEEVKFGGGK VIRDGMGQSQ 

        70         80         90        100        110        120 
RVAADVPDTI ITNAVILDHW GIVKADIAIK HGRIAAIGKA GNPDIQPGVT IAIGAATEVI 

       130        140        150        160        170        180 
AGEGLIVTAG GIDTHIHFIS PQQIDEALAS GVTTMLGGGT GPATGTNATT CTPGPWHMER 

       190        200        210        220        230        240 
MLQAADGWPI NLGFLGKGNV SVPQPLVEQI AAGAIGLKLH EDWGTTPAAI DNCLSVADDT 

       250        260        270        280        290        300 
DTQVAIHTDT LNEGGFVEST VAAFKGRTIH TYHTEGAGGG HAPDILKVCG ESNVLPSSTN 

       310        320        330        340        350        360 
PTRPYTINTL DEHLDMLMVC HHLDPSIAED LAFAESRIRR ETIAAEDILH DLGALSMLSS 

       370        380        390        400        410        420 
DSQAMGRVGE VIIRTWQTAH KMKVQRGALP EDNARNDNFR AKRYVAKYTI NPAITHGIAH 

       430        440        450        460        470        480 
EVGSIEPGKW ADLVLWEPAF FGIKPSMILK GGMIAMAQMG DPNASIPTPQ PVHYREMFAT 

       490        500        510        520        530        540 
RGGALARTSL TFVSQMAADA GIAERYGLAK WIVPVRNCRN VTKADMIHNA WRPSISVDPE 

       550        560 
TYDVIADGQL LTCEPATVLP MAQRYFLF 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia vietnamiensis G4."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Tiedje J., Richardson P.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000614 Genomic DNA. Translation: ABO53845.1.
RefSeqYP_001118680.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA4JC42.

Protein family/group databases

MEROPSM38.982.

Genome annotation databases

GeneID4952529.
GenomeReviewsGene locus Bcep1808_0833 in contig CP000614_GR.
KEGGbvi:Bcep1808_0833.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMASHIHFIC.

Family and domain databases

HAMAPMF_01953.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR011612. Urease_alpha_N.
IPR005848. Urease_asu.
IPR017951. Urease_asu_c.
IPR017952. Urease_asu_core.
IPR017950. Urease_asu_CS.
[Graphical view]
PfamPF01979. Amidohydro_1. 1 hit.
PF00449. Urease_alpha. 1 hit.
[Graphical view]
PRINTSPR01752. UREASE.
TIGRFAMsTIGR01792. urease_alph. 1 hit.
PROSITEPS01120. UREASE_1. 1 hit.
PS00145. UREASE_2. 1 hit.
PS51368. UREASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameURE1_BURVG
AccessionPrimary (citable) accession number: A4JC42
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: May 1, 2007
Last modified: November 3, 2009
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents