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A5TEZ6 (A5TEZ6_BURMA) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Urease subunit alpha HAMAP MF_01953
EC=3.5.1.5 HAMAP MF_01953
Alternative name(s):
Urea amidohydrolase subunit alpha HAMAP MF_01953
Gene names
Name:ureC HAMAP MF_01953 EMBL EDK83465.1
ORF Names:BMA721280_B0231 EMBL EDK83465.1
OrganismBurkholderia mallei 2002721280 EMBL EDK83465.1
Taxonomic identifier370895 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length568 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Urea + H2O = CO2 + 2 NH3. HAMAP MF_01953 RuleBase RU000510 SAAS SAAS005848

Cofactor

Binds 2 nickel ions per subunit By similarity. HAMAP MF_01953 RuleBase RU000510 SAAS SAAS005848

Pathway

Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1. HAMAP MF_01953 SAAS SAAS005848

Subunit structure

Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha) subunits. Three heterotrimers associate to form the active enzyme By similarity. HAMAP MF_01953

Subcellular location

Cytoplasm By similarity HAMAP MF_01953 SAAS SAAS005848.

Post-translational modification

Carbamylation allows a single lysine to coordinate two nickel ions By similarity. HAMAP MF_01953

Sequence similarities

Belongs to the urease family. HAMAP MF_01953 RuleBase RU004158

Contains 1 urease domain. HAMAP MF_01953

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Domain130 – 568439Urease By similarity HAMAP MF_01953

Sites

Active site3211Proton donor By similarity HAMAP MF_01953
Metal binding1351Nickel 1 By similarity HAMAP MF_01953
Metal binding1371Nickel 1 By similarity HAMAP MF_01953
Metal binding2181Nickel 1; via carbamate group By similarity HAMAP MF_01953
Metal binding2181Nickel 2; via carbamate group By similarity HAMAP MF_01953
Metal binding2471Nickel 2 By similarity HAMAP MF_01953
Metal binding2731Nickel 2 By similarity HAMAP MF_01953
Metal binding3611Nickel 1 By similarity HAMAP MF_01953
Binding site2201Substrate By similarity HAMAP MF_01953

Amino acid modifications

Modified residue2181N6-carboxylysine By similarity HAMAP MF_01953

Sequences

Sequence LengthMass (Da)Tools
A5TEZ6 [UniParc].

Last modified July 10, 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

References

[1]"Annotation of Burkholderia mallei 2002721280."
DeShazer D., Woods D.E., Nierman W.C.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: 2002721280 EMBL EDK83465.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CH899691 Genomic DNA. Translation: EDK83465.1.

3D structure databases

ProteinModelPortalA5TEZ6.
SMRA5TEZ6. Positions 5-568.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

PATRIC26888323. VBIBurMal4978_0936.

Phylogenomic databases

OMATIHAFHT.

Family and domain databases

HAMAPMF_01953. Urease_alpha.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR011059. Metal-dep_hydrolase_composite.
IPR011612. Urease_alpha_N.
IPR005848. Urease_asu.
IPR017951. Urease_asu_c.
IPR017950. Urease_asu_CS.
[Graphical view]
PfamPF01979. Amidohydro_1. 1 hit.
PF00449. Urease_alpha. 1 hit.
[Graphical view]
PRINTSPR01752. UREASE.
SUPFAMSSF51338. Metalo_hydrolase. 2 hits.
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 nameA5TEZ6_BURMA
AccessionPrimary (citable) accession number: A5TEZ6
Entry history
Integrated into UniProtKB/TrEMBL: July 10, 2007
Last sequence update: July 10, 2007
Last modified: December 14, 2011
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info