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A4WEJ5 (URE1_ENT38) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 36. 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:Ent638_3466
OrganismEnterobacter sp. (strain 638) [Complete proteome] [HAMAP]
Taxonomic identifier399742 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Enterobacter

Protein attributes

Sequence length567 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.

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: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionnickel cation binding

Inferred from electronic annotation. Source: InterPro

urease activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 567567Urease subunit alpha HAMAP MF_01953
PRO_1000070656

Regions

Domain129 – 567439Urease

Sites

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

Amino acid modifications

Modified residue2171N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A4WEJ5 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: 1C1141C48502D4B7

FASTA56760,232
        10         20         30         40         50         60 
MAEISRQAYA DMFGPTTGDK VRLADTDLWI EVENDLTIYG EEVKFGGGKV IRDGMGQGQM 

        70         80         90        100        110        120 
TAQDCVDLVL TNALIVDHWG IVKADIGVKD 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 DWGSTPATIN CSLSVAEEMD 

       250        260        270        280        290        300 
IQVALHSDTL NEAGFVEDTL AAIDGRTIHT FHTEGAGGGH APDIITACAH PNILPSSTNP 

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

       370        380        390        400        410        420 
SQAMGRVGEV IIRTWQVAHR MKVQRGALAE ESGDNDNFRA KRYVAKYTIN PALTHGIAHE 

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

       490        500        510        520        530        540 
GAARHATRLT FISQAADANR IPQQLNLQSA IAVVKGCRTV KKADMIHNGL QPNITVDAQT 

       550        560 
YEVRIDGELI TSEPADVLPM AQRYFLF

« Hide

References

[1]"Complete sequence of chromosome of Enterobacter sp. 638."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 638.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000653 Genomic DNA. Translation: ABP62125.1.
RefSeqYP_001178176.1. NC_009436.1.

3D structure databases

ProteinModelPortalA4WEJ5.
SMRA4WEJ5. Positions 2-567.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4WEJ5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5110560.
GenomeReviewsGene locus Ent638_3466 in contig CP000653_GR.
KEGGent:Ent638_3466.
NMPDRfig|399742.4.peg.3293.
PATRIC20416657. VBIEntSp101211_3626.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0804.
HOGENOMHBG357507.
OMATIHAFHT.
ProtClustDBPRK13207.

Enzyme and pathway databases

BioCycESP42895:ENT638_3466-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.
IPR017950. Urease_asu_CS.
[Graphical view]
KOK01428.
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_ENT38
AccessionPrimary (citable) accession number: A4WEJ5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 29, 2007
Last modified: January 25, 2012
This is version 36 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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