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Reviewed, UniProtKB/Swiss-Prot A3MMV2 (URE1_BURM7)

Last modified November 3, 2009. Version 20. 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

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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: BMA10247_2057
OrganismBurkholderia mallei (strain NCTC 10247) [Complete proteome] [HAMAP]
Taxonomic identifier320389 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

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Protein attributes

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

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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.

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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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 568568Urease subunit alpha HAMAP MF_01953
PRO_1000070649

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

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Sequences

Sequence LengthMass (Da)Tools
A3MMV2-1 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: C50CC452A29563CC

FASTA56860,662
        10         20         30         40         50         60 
MTLRLSRRAY AEMYGPTTGD RIRLADTELL IEVERDHTLY GEEVKFGGGK VIRDGMGQSQ 

        70         80         90        100        110        120 
LPAADVADTV ITNAVILDHW GIVKADIAIK HGRIAAIGKA GNPDIQPGVT IAIGAATEII 

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

       190        200        210        220        230        240 
MLQAADGWPI NLGFLGKGNA SRPQPLVEQI EAGAIGLKLH EDWGTTPAAI DNCLTVADDT 

       250        260        270        280        290        300 
DTQVAIHTDT LNEAGFVEAT VAAFKGRTIH TYHTEGAGGG HAPDILKVCG EANVLPSSTN 

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

       370        380        390        400        410        420 
DSQAMGRVGE VIIRTWQTAH KMKVQRGALA GDGARNDNFR AKRYVAKYTI NPALTHGIAH 

       430        440        450        460        470        480 
EVGSIEPGKW ADLVLWEPAF FGVKPAMIVK GGMIAVAQMG DPNASIPTPQ PVHYREMFAT 

       490        500        510        520        530        540 
RGGALARTSL TFVSQLALDA GIGARYGLAK RLVPVRGCRT VTKRDMIHNA WQPAIRVDPE 

       550        560 
TYDVVADGAL LTCEPAAVLP MAQRYFLF

« Hide

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References

[1]DeShazer D., Woods D.E., Nierman W.C.
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

CP000548 Genomic DNA. Translation: ABO04242.1.
RefSeqYP_001081588.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4891555.
GenomeReviewsGene locus BMA10247_2057 in contig CP000548_GR.
KEGGbmn:BMA10247_2057.
TIGRBMA10247_2057.

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...

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Entry information

Entry nameURE1_BURM7
AccessionPrimary (citable) accession number: A3MMV2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: April 3, 2007
Last modified: November 3, 2009
This is version 20 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)

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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