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Reviewed, UniProtKB/Swiss-Prot Q47G55 (URE1_DECAR)

Last modified February 9, 2010. Version 38. 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: Daro_1427
OrganismDechloromonas aromatica (strain RCB) [Complete proteome] [HAMAP]
Taxonomic identifier159087 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeDechloromonas

Protein attributes

Sequence length569 AA.
Sequence statusComplete.
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. HAMAP MF_01953

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. HAMAP MF_01953

Subcellular location

Cytoplasm By similarity HAMAP MF_01953.

Post-translational modification

Carbamylation allows a single lysine to coordinate two nickel ions By similarity. HAMAP MF_01953

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_0000234153

Regions

Domain132 – 569438Urease

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
Q47G55-1 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: B10702E8BE43CABC

FASTA56960,409
        10         20         30         40         50         60 
MMANKITRQA YAEMFGPTTG DRMRLADTEL IIEVEKDYTI YGEEVKFGGG KVIRDGMGQG 

        70         80         90        100        110        120 
QRLSAETVDT VITNALIVDA VTGIVKADIG LKEGRIAAIG KAGNPDIQPG VTIVIGPGTE 

       130        140        150        160        170        180 
VIAGEGMIVT AGGIDSHIHF ICPQQIDEAL YSGVTTMIGG GTGPATGTFA TTCTPGPWHI 

       190        200        210        220        230        240 
HRMLEAADAF PMNLGFLGKG NASLPEALRE QVEAGVMGLK LHEDWGTTPA AIDCCLTVAD 

       250        260        270        280        290        300 
EMDVQVAIHS DTLNESGFVE ATLGAFKGRT IHTFHTEGAG GGHAPDIIKA AGLPNVLPSS 

       310        320        330        340        350        360 
TNPTMPYTVN TIDEHLDMLM VCHHLDPSIA EDIAFAESRI RRETIAAEDI LHDLGAFSMM 

       370        380        390        400        410        420 
SSDSQAMGRV GEVIIRTWQA AHKMKLQRGA LPEDSARNDN FRVKRYIAKY TINPALTHGI 

       430        440        450        460        470        480 
AHTVGSVEVG KLADLVLWKP AFFGVKPSLI LKGGMIAAAA MGDPNASIPT PQPVHYRPMF 

       490        500        510        520        530        540 
GSFGKALKTS VTFISQAALN NPAIAALGLS KPLVAVSGTR TLTKADMVHN GATPEITVDP 

       550        560 
ETYVVKADGV HLVCEPATEL PLAQRYFLF 

« Hide

References

[1]"Complete sequence of Dechloromonas aromatica RCB."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Di Bartolo G., Trong S., Kellar K., Schmutz J., Larimer F., Land M., Ivanova N., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000089 Genomic DNA. Translation: AAZ46176.1.
RefSeqYP_284646.1.

3D structure databases

SMRQ47G55. Positions 4-569.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ47G55.

Genome annotation databases

GeneID3569073.
GenomeReviewsGene locus Daro_1427 in contig CP000089_GR.
KEGGdar:Daro_1427.
NMPDRfig|159087.4.peg.1280.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0804.
HOGENOMHBG357507.
OMASHIHFIC.

Enzyme and pathway databases

BioCycDARO159087:DARO_1427-MONOMER.

Family and domain databases

HAMAPMF_01953. Urease_alpha.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR011059. Metal-dep_hydrolase_composite.
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_DECAR
AccessionPrimary (citable) accession number: Q47G55
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: September 13, 2005
Last modified: February 9, 2010
This is version 38 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