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Reviewed, UniProtKB/Swiss-Prot A0JRH4 (URE1_ARTS2)

Last modified November 3, 2009. Version 26. 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: Arth_0243
OrganismArthrobacter sp. (strain FB24) [Complete proteome] [HAMAP]
Taxonomic identifier290399 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeArthrobacter

Protein attributes

Sequence length576 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 – 576576Urease subunit alpha HAMAP MF_01953
PRO_1000070647

Regions

Domain132 – 576445Urease

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

Sequences

Sequence LengthMass (Da)Tools
A0JRH4-1 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 58BC841B6AE59E84

FASTA57661,668
        10         20         30         40         50         60 
MSFELTRRQY ADLYGPTTGD SIRLADTELF LEIEKDLTVY GEEVVFGGGK VIRDGMGQNG 

        70         80         90        100        110        120 
QVTRDEDVPD TVITNAVILD YTGIYKADVA IRDGHIIKIG KAGNPQITDG VDIVIGASTE 

       130        140        150        160        170        180 
IIAGERKILT AGGVDTHIHF ISPDQVPTAL TSGVTTMVGG GTGPAEGTKA TTVTPGKWHI 

       190        200        210        220        230        240 
QRMLQATEGM PINIGLFGKG HASAVEPLAE QIRAGAIGLK VHEDWGSTTS SIDNSLKVAD 

       250        260        270        280        290        300 
EYDVQVAIHT DTLNECGFVE DTIRAIGGRV IHTFHTEGAG GGHAPDIIKI AGLPNVLPAS 

       310        320        330        340        350        360 
TNPTLPYTRN TIEEHLDMLM VCHHLNPDIP EDVAFADSRI RAETIAAEDV LQDLGIFAIT 

       370        380        390        400        410        420 
SSDSQAMGRV GEVITRTWQV ADKMKKQRGV LKDPAGGAHG SEDSDNFRLK RYVAKYTINA 

       430        440        450        460        470        480 
AIAQGMADSI GSVEEGKFAD LVLWDPAFFG VKPELVLKGG QIAYALMGDA NASIPTPQPR 

       490        500        510        520        530        540 
TMRPMFAAFG KAVQQSSITF LSQAAIDAGV PEELGLQKVI RAVSGIRSLS KADLKYNDAT 

       550        560        570 
PDIQVDPETY KVTVDGEDVT CEPADVLPMA QRYFLF 

« Hide

References

[1]"Complete sequence of chromosome 1 of Arthrobacter sp. FB24."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Thompson S., Brettin T., Bruce D., Han C., Tapia R., Gilna P. expand/collapse author list , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Beasley F., Chen W., Jerke K., Nakatsu C.H., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000454 Genomic DNA. Translation: ABK01644.1.
RefSeqYP_829744.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA0JRH4.

Genome annotation databases

GeneID4447299.
GenomeReviewsGene locus Arth_0243 in contig CP000454_GR.
KEGGart:Arth_0243.
TIGRArth_0243.

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...

Entry information

Entry nameURE1_ARTS2
AccessionPrimary (citable) accession number: A0JRH4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: December 12, 2006
Last modified: November 3, 2009
This is version 26 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