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Reviewed, UniProtKB/Swiss-Prot Q733J6 (URE1_BACC1)

Last modified November 3, 2009. Version 45. 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: BCE_3662
OrganismBacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP]
Taxonomic identifier222523 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

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Protein attributes

Sequence length570 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 – 570570Urease subunit alpha HAMAP MF_01953
PRO_0000234132

Regions

Domain132 – 570439Urease

Sites

Active site3231Proton donor By similarity
Metal binding1371Nickel 2 By similarity
Metal binding1391Nickel 2 By similarity
Metal binding2201Nickel 1; via carbamate group By similarity
Metal binding2201Nickel 2; via carbamate group By similarity
Metal binding2491Nickel 1 By similarity
Metal binding2751Nickel 1 By similarity
Metal binding3631Nickel 2 By similarity
Binding site2221Substrate By similarity

Amino acid modifications

Modified residue2201N6-carboxylysine By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q733J6-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 6BEE8F4748D19122

FASTA57062,058
        10         20         30         40         50         60 
MSFKMSRKQY ADLYGPTTGD SIRLADTQLF AHIERNATVY GDEAVFGGGK SIRDGMGQNS 

        70         80         90        100        110        120 
QLTREQGVVD VVITNAIIID YTGIYKADIG IKDGKISAIG KSGNPSVMDN IDIIIGTSTE 

       130        140        150        160        170        180 
VISGERKIVT AGGIDTHVHF ISPQQIDTAL ASGITTLIGG GTGPAEGTKA TTITPGSWNL 

       190        200        210        220        230        240 
RKMLEAAEAF PINLGFLGKG NSSSLPALEE QIFAGAIGLK IHEDWGATSS AINHSLQIAD 

       250        260        270        280        290        300 
KYDIQVAIHT DTLNECGFVE ETIKAIDNRV IHTYHTEGAG GGHAPDIIKI AALNNILPSS 

       310        320        330        340        350        360 
TNPTLPYTVN TLDEHLDMLM VCHHLKANIP EDVMFADSRI RKETIAAEDI LQDLGVFSMI 

       370        380        390        400        410        420 
SSDSQAMGRV GEVIIRNWQT ADKMKKQIGS LEGDKEYNDN NRIQRYIAKY TINPAITHGI 

       430        440        450        460        470        480 
SEYVGSIEVG KYADLVIWDP QFFGVKPDMV LKNGMVVMAL MGDENASIPT PQPYYEKKMF 

       490        500        510        520        530        540 
GAYGKAVQSS SITFVSKVAY ENNIKDKLGL NKVVLPVKNT REISKQDMKL NNATPEIEVD 

       550        560        570 
PQTYEVKVDG KVITCEAVDV LPMAQRYFLF

« Hide

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References

[1]"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
Nucleic Acids Res. 32:977-988(2004) [PubMed: 14960714] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

AE017194 Genomic DNA. Translation: AAS42567.1.
RefSeqNP_979959.1.

3D structure databases

HSSPHSSP built from PDB template 1A5N based on UniProtKB P18314.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ733J6.

Genome annotation databases

GeneID2750397.
GenomeReviewsGene locus BCE_3662 in contig AE017194_GR.
KEGGbca:BCE_3662.
NMPDRfig|222523.1.peg.3631.
TIGRBCE_3662.

Phylogenomic databases

HOGENOMQ733J6.
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_BACC1
AccessionPrimary (citable) accession number: Q733J6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: July 5, 2004
Last modified: November 3, 2009
This is version 45 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