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Reviewed, UniProtKB/Swiss-Prot A8APV0 (URE1_CITK8)

Last modified November 3, 2009. Version 17. 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: CKO_04457
OrganismCitrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696) [Complete proteome] [HAMAP]
Taxonomic identifier290338 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Citrobacter

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Protein attributes

Sequence length567 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 – 567567Urease subunit alpha HAMAP MF_01953
PRO_1000070654

Regions

Domain129 – 567439Urease

Sites

Active site3201Proton donor By similarity
Metal binding1341Nickel 2 By similarity
Metal binding1361Nickel 2 By similarity
Metal binding2171Nickel 1; via carbamate group By similarity
Metal binding2171Nickel 2; via carbamate group By similarity
Metal binding2461Nickel 1 By similarity
Metal binding2721Nickel 1 By similarity
Metal binding3601Nickel 2 By similarity
Binding site2191Substrate By similarity

Amino acid modifications

Modified residue2171N6-carboxylysine By similarity

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Sequences

Sequence LengthMass (Da)Tools
A8APV0-1 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: B9CAE08BFA390FE5

FASTA56760,475
        10         20         30         40         50         60 
MTEISRQAYA DMFGPTTGDR VRLADTELWI EVENDLTAYG EEVKFGGGKV IRDGMGQGQM 

        70         80         90        100        110        120 
RARACVDLVI TNALIVDHWG IVKADIGIKD GRIFAIGKAG NPDIQPNVTI PIGVGTEAIA 

       130        140        150        160        170        180 
GEGKIVTAGG VDTHIHWICP QQAEEALVSG VTTMIGGGTG PAAGTNATTC TPGPWYIARM 

       190        200        210        220        230        240 
LQAADSLPVN IGFLGKGNGS NPDALREQIA AGAIGLKIHE DWGATPAAID CALTVAEEMD 

       250        260        270        280        290        300 
IQVALHSDTL NESGFVEDTL AAIGDRTIHT FHTEGAGGGH APDIITACAH PHILPSSTNP 

       310        320        330        340        350        360 
TLPYTVNTID EHLDMLMVCH HLDPDIAEDV AFAESRIRRE TIAAEDVLHD LGAFSLTSSD 

       370        380        390        400        410        420 
SQAMGRVGEV ILRTWQVAHR MKVQRGPLAE ETGDNDNQRV KRYIAKYTIN PALTHGIAHE 

       430        440        450        460        470        480 
VGSVEAGKLA DLVLWSPAFF GVKPATLIKG GMIVCAPMGD INASIPTPQP VHYRPMFGAL 

       490        500        510        520        530        540 
GAARHHCRLT FLSQAAVENG IAQQLNLRSA TAVVKGCRTV KKADMIHNSL QPNITVDAQT 

       550        560 
YEVRIDGEPI TSEPADVLPM AQRYFLF

« Hide

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References

[1]McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W., Johnson M., Thiruvilangam P., Wilson R.
Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

CP000822 Genomic DNA. Translation: ABV15513.1.
RefSeqYP_001455949.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA8APV0.

Protein family/group databases

MEROPSM38.982.

Genome annotation databases

GeneID5585479.
GenomeReviewsGene locus CKO_04457 in contig CP000822_GR.
KEGGcko:CKO_04457.

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...

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Entry information

Entry nameURE1_CITK8
AccessionPrimary (citable) accession number: A8APV0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: November 3, 2009
This is version 17 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