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Q5KYM1 (URE1_GEOKA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:GK1930
OrganismGeobacillus kaustophilus (strain HTA426) [Complete proteome] [HAMAP]
Taxonomic identifier235909 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Geobacillus ›

Protein attributes

Sequence length569 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Urea + H2O = CO2 + 2 NH3. HAMAP-Rule 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-Rule 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. HAMAP-Rule 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 catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionnickel cation binding

Inferred from electronic annotation. Source: HAMAP

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-Rule MF_01953
PRO_0000234156

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
Q5KYM1 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: 42FC32C3B4F41BDD

FASTA56961,400
        10         20         30         40         50         60 
MSFSMSRRQY ADMFGPTTGD CIRLADTDLW IEIEHDYTVY GDEVKFGGGK VIRDGMGQHP 

        70         80         90        100        110        120 
LATRDEAVDL VLTNAVIVDY TGIYKADIGI KDGNIAAIGK AGNPLLMDGV NIVIGASTEV 

       130        140        150        160        170        180 
IAAEGKIVTA GGVDAHIHFI CPQQIETALS SGITTMIGGG TGPATGTNAT TCTPGEWNIY 

       190        200        210        220        230        240 
RMLEAAEAFP MNIGFLGKGN ASAKEPIAEQ VRAGAIGLKL HEDWGTTAAA IDACLRVADE 

       250        260        270        280        290        300 
YDVQVAIHTD TLNEGGFVEH TLKAINGRVI HTYHTEGAGG GHAPDIMKVA SFPNILPSST 

       310        320        330        340        350        360 
NPTRPYTKNT LDEHLDMLMV CHHLDPSVPE DIAFADSRIR KETIAAEDIL HDIGAFSMIS 

       370        380        390        400        410        420 
SDSQAMGRVG EVILRTWQTA DKMKKQFGRL PEETGRGDNV RVKRYVAKYT INPAITHGIA 

       430        440        450        460        470        480 
EYVGSVEVGK FADLVVWHPA FFGVKPELVI KGGMIAYSVM GDPNASIPTP QPALYRPMFA 

       490        500        510        520        530        540 
SYGAAIAKTS ITFLSKAAFE RGIPDKLGLH KIVKPVGNIR SLTKNDMVFN NAMLQIDVDP 

       550        560 
QTYEVKVDGR LITCEPAEVV AMAQRYFLF

« Hide

References

[1]"Thermoadaptation trait revealed by the genome sequence of thermophilic Geobacillus kaustophilus."
Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H., Matsui S., Uchiyama I.
Nucleic Acids Res. 32:6292-6303(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HTA426.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000043 Genomic DNA. Translation: BAD76215.1.
RefSeqYP_147783.1. NC_006510.1.

3D structure databases

ProteinModelPortalQ5KYM1.
SMRQ5KYM1. Positions 4-569.
ModBaseSearch...

Protein-protein interaction databases

STRING235909.GK1930.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD76215; BAD76215; GK1930.
GeneID3184685.
KEGGgka:GK1930.
PATRIC21965231. VBIGeoKau81518_2071.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0804.
HOGENOMHOG000075064.
KOK01428.
OMATIHAFHT.
ProtClustDBPRK13207.

Enzyme and pathway databases

BioCycGKAU235909:GJO7-2018-MONOMER.
UniPathwayUPA00258; UER00370.

Family and domain databases

HAMAPMF_01953. Urease_alpha.
InterProIPR006680. Amidohydro_1.
IPR011059. Metal-dep_hydrolase_composite.
IPR011612. Urease_alpha_N.
IPR005848. Urease_asu.
IPR017951. Urease_asu_c.
IPR017950. Urease_asu_CS.
[Graphical view]
PfamPF01979. Amidohydro_1. 1 hit.
PF00449. Urease_alpha. 1 hit.
[Graphical view]
PRINTSPR01752. UREASE.
SUPFAMSSF51338. Metalo_hydrolase. 2 hits.
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_GEOKA
AccessionPrimary (citable) accession number: Q5KYM1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: February 1, 2005
Last modified: May 1, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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