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Reviewed, UniProtKB/Swiss-Prot Q8XAG0 (URE1_ECO57)

Last modified November 3, 2009. Version 55. 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: ureC1
Ordered Locus Names: Z1145, ECs1324
AND
Name: ureC2
Ordered Locus Names: Z1584
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

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.

Caution

Neither O157 strain expresses urease due to a truncation of ureD, the last gene of the probable operon. Urease activity is restored in O157 / Sakai upon complementation with wild-type ureD.

This region of the chromosome is duplicated in strain O157:H7 / EDL933 but not in O157:H7 / Sakai.

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_0000234155

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
Q8XAG0-1 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: AC39B7B701481361

FASTA56860,626
        10         20         30         40         50         60 
MMSNISRQAY ADMFGPTTGD KIRLADTELW IEVEDDLTTY GEEVKFGGGK VIRDGMGQGQ 

        70         80         90        100        110        120 
MLSAGCADLV LTNALIIDYW GIVKADIGVK DGRIFAIGKA GNPDIQPNVT IPIGVSTEII 

       130        140        150        160        170        180 
AAEGRIVTAG GVDTHIHWIC PQQAEEALTS GITTMIGGGT GPTAGSNATT CTPGPWYIYQ 

       190        200        210        220        230        240 
MLQAADSLPV NIGLLGKGNC SNPDALREQV AAGVIGLKIH EDWGATPAVI NCALTVADEM 

       250        260        270        280        290        300 
DVQVALHSDT LNESGFVEDT LTAIGGRTIH TFHTEGAGGG HAPDIITACA HPNILPSSTN 

       310        320        330        340        350        360 
PTLPYTVNTI DEHLDMLMVC HHLDPDIAED VAFAESRIRQ ETIAAEDVLH DLGAFSLTSS 

       370        380        390        400        410        420 
DSQAMGRVGE VVLRTWQVAH RMKVQRGPLP EESGDNDNVR VKRYIAKYTI NPALTHGIAH 

       430        440        450        460        470        480 
EVGSIEVGKL ADLVLWSPAF FGVKPATIVK GGMIAMAPMG DINGSIPTPQ PVHYRPMFAA 

       490        500        510        520        530        540 
LGSARHRCRV TFLSQAAAAN GVAEQLNLHS TTAVVKGCRT VQKADMRHNS LLPDITVDSQ 

       550        560 
TYEVRINGEL ITSEPADILP MAQRYFLF 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed: 11206551] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.
[3]"Urease activity of enterohaemorrhagic Escherichia coli depends on a specific one-base substitution in ureD."
Nakano M., Iida T., Honda T.
Microbiology 150:3483-3489(2004) [PubMed: 15470125] [Abstract]
Cited for: ABSENCE OF UREASE.
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases

AE005174 Genomic DNA. Translation: AAG55290.1.
AE005174 Genomic DNA. Translation: AAG55699.1.
BA000007 Genomic DNA. Translation: BAB34747.1.
PIRD90794.
G85654.
RefSeqNP_286680.1.
NP_287088.1.
NP_309351.1.

3D structure databases

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

Protein family/group databases

MEROPSM38.982.

Genome annotation databases

GeneID913507.
958581.
959231.
GenomeReviewsGene locus Z1145 in contig AE005174_GR.
Gene locus Z1584 in contig AE005174_GR.
Gene locus ECs1324 in contig BA000007_GR.
KEGGece:Z1145.
ece:Z1584.
ecs:ECs1324.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8XAG0.
OMAIAGRAIH.

Enzyme and pathway databases

BioCycECOL83334:ECS1324-MON.

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_ECO57
AccessionPrimary (citable) accession number: Q8XAG0
Secondary accession number(s): Q7AFH5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: March 1, 2002
Last modified: November 3, 2009
This is version 55 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