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Reviewed, UniProtKB/Swiss-Prot Q28RJ3 (URE1_JANSC)

Last modified November 3, 2009. Version 28. 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: ureC
Ordered Locus Names: Jann_1752
OrganismJannaschia sp. (strain CCS1) [Complete proteome] [HAMAP]
Taxonomic identifier290400 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeJannaschia

Protein attributes

Sequence length569 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.

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 – 569569Urease subunit alpha HAMAP MF_01953
PRO_0000239877

Regions

Domain131 – 569439Urease

Sites

Active site3221Proton donor By similarity
Metal binding1361Nickel 2 By similarity
Metal binding1381Nickel 2 By similarity
Metal binding2191Nickel 1; via carbamate group By similarity
Metal binding2191Nickel 2; via carbamate group By similarity
Metal binding2481Nickel 1 By similarity
Metal binding2741Nickel 1 By similarity
Metal binding3621Nickel 2 By similarity
Binding site2211Substrate By similarity

Amino acid modifications

Modified residue2191N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q28RJ3-1 [UniParc].

Last modified April 4, 2006. Version 1.
Checksum: 3B58F0DF91AAAF21

FASTA56961,338
        10         20         30         40         50         60 
MPTKIPRNDY AAMYGPTTGD RVRLADTDLI IEVERDLTTY GEEVKFGGGK VIRDGMGQSQ 

        70         80         90        100        110        120 
VTRAQCAVDT VITNALIVDH SGIYKADVGL KDGRIHKIGK AGNPDTQPNV DIIIGPGTEA 

       130        140        150        160        170        180 
IAGEGRILTA GGFDAHIHFI CPQQIEDSLH SGITTMLGGG TGPAHGTLAT TCTPGPWHIG 

       190        200        210        220        230        240 
RMLQSLDAFP MNFGLSCKGN ASQPEALVEM VSAGACAMKL HEDWGTTPGA IDCCLSVADE 

       250        260        270        280        290        300 
MDVQVMIHTD TLNESGFVEN TLAAIGDRTI HAFHTEGAGG GHAPDIMKVV GYENILPSST 

       310        320        330        340        350        360 
NPTMPYTVNT LEEHLDMLMV CHHLDKSIPE DVAFAESRIR KETIAAEDIL HDMGAFSVMA 

       370        380        390        400        410        420 
SDSQAMGRVG EVIIRTWQTA DKMKKQRGRL AEETGDNDNA RVMRYIAKYT INPALVHGMS 

       430        440        450        460        470        480 
REIGSIEEGK RADLVLWSPA FFGVKPEMSL IGGTIVMAQM GDPNASIPTP QPVYSRPMFG 

       490        500        510        520        530        540 
AFGRAVERSA VLFVSEAAQA AGIGDQLGLA KDTLAVKSTR DIRKSDMIHN SFRPDIHVDP 

       550        560 
ETYDVRANGE LLTCEPATDL PLAQRYFMY 

« Hide

References

[1]"Complete sequence of chromosome of Jannaschia sp. CCS1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Chertkov O., Saunders E., Schmutz J., Larimer F. expand/collapse author list , Land M., Kyrpides N., Lykidis A., Moran M.A., Belas R., Ye W., Buchan A., Gonzalez J.M., Schell M.A., Richardson P.
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000264 Genomic DNA. Translation: ABD54669.1.
RefSeqYP_509694.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ28RJ3.

Genome annotation databases

GeneID3934200.
GenomeReviewsGene locus Jann_1752 in contig CP000264_GR.
KEGGjan:Jann_1752.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ28RJ3.
OMASHIHFIC.

Enzyme and pathway databases

BioCycJSP290400:JANN_1752-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_JANSC
AccessionPrimary (citable) accession number: Q28RJ3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: April 4, 2006
Last modified: November 3, 2009
This is version 28 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