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G8LEN1 (G8LEN1_ENTCL) Unreviewed, UniProtKB/TrEMBL

Last modified April 3, 2013. Version 9. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Urease subunit alpha HAMAP-Rule MF_01953
EC=3.5.1.5 HAMAP-Rule MF_01953
Alternative name(s):
Urea amidohydrolase subunit alpha HAMAP-Rule MF_01953
Gene names
Name:ureC HAMAP-Rule MF_01953 EMBL AEW75273.1
ORF Names:EcWSU1_03845 EMBL AEW75273.1
OrganismEnterobacter cloacae EcWSU1 EMBL AEW75273.1
Taxonomic identifier1045856 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Enterobacter › Enterobacter cloacae complex ›

Protein attributes

Sequence length567 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Urea + H2O = CO2 + 2 NH3. HAMAP-Rule MF_01953 RuleBase RU000510 SAAS SAAS017950

Cofactor

Binds 14 nickel ions per subunit By similarity. HAMAP-Rule MF_01953

Binds 2 nickel ions per subunit By similarity. HAMAP-Rule MF_01953 SAAS SAAS017950 RuleBase RU000510

Pathway

Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1. HAMAP-Rule MF_01953 SAAS SAAS017950

Subunit structure

Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha) subunits. Three heterotrimers associate to form the active enzyme By similarity. HAMAP-Rule MF_01953

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01953 SAAS SAAS017950.

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. HAMAP-Rule MF_01953 RuleBase RU004158

Contains 1 urease domain. HAMAP-Rule MF_01953

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Domain129 – 567439Urease By similarity HAMAP-Rule MF_01953

Sites

Active site3201Proton donor By similarity HAMAP-Rule MF_01953
Metal binding1341Nickel 2 By similarity HAMAP-Rule MF_01953
Metal binding1361Nickel 2 By similarity HAMAP-Rule MF_01953
Metal binding2171Nickel 1; via carbamate group By similarity HAMAP-Rule MF_01953
Metal binding2171Nickel 2; via carbamate group By similarity HAMAP-Rule MF_01953
Metal binding2461Nickel 1 By similarity HAMAP-Rule MF_01953
Metal binding2721Nickel 1 By similarity HAMAP-Rule MF_01953
Metal binding3601Nickel 2 By similarity HAMAP-Rule MF_01953
Binding site2191Substrate By similarity HAMAP-Rule MF_01953

Amino acid modifications

Modified residue2171N6-carboxylysine By similarity HAMAP-Rule MF_01953

Sequences

Sequence LengthMass (Da)Tools
G8LEN1 [UniParc].

Last modified February 22, 2012. Version 1.
Checksum: F27C8F12918282D3

FASTA56760,102
        10         20         30         40         50         60 
MAEISRQAYA DMFGPTTGDK VRLADSELWI EVENDLTVYG EEVKFGGGKV IRDGMGQGQM 

        70         80         90        100        110        120 
TSDGCVDLVL TNALIIDHWG IVKADIGIKN GRIFAVGKAG NPDIQPGVTI PIGAATEVIA 

       130        140        150        160        170        180 
AEGKIVTAGG IDTHIHWICP QQAEEALVSG VTTMIGGGTG PAAGTNATTC TPGPWYIARM 

       190        200        210        220        230        240 
LQAADTLPVN IGLLGKGNGS NPDALREQIA AGAIGLKIHE DWGATPAAIN CSLAVAEEMD 

       250        260        270        280        290        300 
IQVALHSDTL NESGFVEDTL AAIGGRTIHT FHTEGAGGGH APDIITACAH PNILPSSTNP 

       310        320        330        340        350        360 
TLPYTVNTID EHLDMLMVCH HLDPDIAEDV AFAESRIRRE TIAAEDVLHD IGAFSLTSSD 

       370        380        390        400        410        420 
SQAMGRVGEV IIRTWQVAHR MKVQRGALPE ETGNNDNYRV KRYIAKYTIN PALTHGIAHE 

       430        440        450        460        470        480 
VGSIETGKLA DLVVWSPAFF GVKPATIVKG GMIACAPMGD INASIPTPQP VHYRPMFGSL 

       490        500        510        520        530        540 
GAARHATRLT FVSQAADAKG ISHQLSLQSG IAVVKGCRTV KKADMIHNSL QPNITVDAQT 

       550        560 
YEVRVDGELI TSEPADVLPM AQRYFLF

« Hide

References

[1]"Complete genome of the onion pathogen Enterobacter cloacae EcWSU1."
Humann J.L., Wildung M., Cheng C.-H., Lee T., Drew J.C., Triplett E.W., Main D., Schroeder B.K.
Stand. Genomic Sci. 0:0-0(2011)
Cited for: NUCLEOTIDE SEQUENCE.
Strain: EcWSU1 EMBL AEW75273.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002886 Genomic DNA. Translation: AEW75273.1.
RefSeqYP_004953694.1. NC_016514.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEW75273; AEW75273; EcWSU1_03845.
GeneID11488633.
KEGGeec:EcWSU1_03845.

Phylogenomic databases

KOK01428.

Enzyme and pathway databases

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 nameG8LEN1_ENTCL
AccessionPrimary (citable) accession number: G8LEN1
Entry history
Integrated into UniProtKB/TrEMBL: February 22, 2012
Last sequence update: February 22, 2012
Last modified: April 3, 2013
This is version 9 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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