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Reviewed, UniProtKB/Swiss-Prot P94669 (URE1_CLOPE)

Last modified June 16, 2009. Version 67. 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

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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
Encoded onPlasmid
OrganismClostridium perfringens
Taxonomic identifier1502 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

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Protein attributes

Sequence length587 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

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Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
Nickel
   Molecular functionHydrolase
   Technical termPlasmid
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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 587587Urease subunit alpha HAMAP MF_01953
PRO_0000067540

Regions

Domain134 – 572439Urease

Sites

Active site3251Proton donor By similarity
Metal binding1391Nickel 2 By similarity
Metal binding1411Nickel 2 By similarity
Metal binding2221Nickel 1; via carbamate group By similarity
Metal binding2221Nickel 2; via carbamate group By similarity
Metal binding2511Nickel 1 By similarity
Metal binding2771Nickel 1 By similarity
Metal binding3651Nickel 2 By similarity
Binding site2241Substrate By similarity

Amino acid modifications

Modified residue2221N6-carboxylysine By similarity

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Sequences

Sequence LengthMass (Da)Tools
P94669-1 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: F4EE2EFAE32318AC

FASTA58763,838
        10         20         30         40         50         60 
MSFEISREQY AGMFGPTTGD SIRLGDTNLF AKIEKDMTVY GDESKFGGGK CLRDGMGQSA 

        70         80         90        100        110        120 
TELRRDNPKV VDLIITSAVI LDYTGIYKAD IGIRDGKIVA IGNGGNPSIM DNVDFIVGSS 

       130        140        150        160        170        180 
TEALSGEGLI VTAGGIDTHV HFITPAIAYS ALENGTTTII GGGTGPADGT NSATSTPGAW 

       190        200        210        220        230        240 
NIHQMLRAAE GMPVNMGIQG KAGGAIMDTT AEQIEAGAMA LKVHEDWGAT LSCIDHALET 

       250        260        270        280        290        300 
ADKYDVQVSL HSDTLNETGF VEDTIKSIGG RCIHSYHTEG AGGGHAPDLM KVASKNNIIP 

       310        320        330        340        350        360 
SSTSPTNPYT VDILPEHLDM LMVCHHLDPK IPEDVRFADS RIRKQTIAAE DVLQDMGALS 

       370        380        390        400        410        420 
IMSSDTMAMG RIGEVIMRSW QLADKMKKQR GPLEGDSEYI DNNRIKRYIS KYTINPAIAE 

       430        440        450        460        470        480 
GISDYVGSIE EGKYADLVLW EPAMFGAKPK MILKSGMIAY GVMGDSNASI PTTQPRTMRE 

       490        500        510        520        530        540 
LFGLTGKSRQ HVNMTFVSTY AYEHNIKEEL GLERNVLPVH NVRTVTKKDM KFNSETPKIE 

       550        560        570        580 
IDPLTYDVTV DGKLITCDPA RELPLAQRYL YTNLDKINIL VYYKKIT

« Hide

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References

[1]"Clostridium perfringens urease genes are plasmid borne."
Dupuy B., Daube G., Popoff M.R., Cole S.T.
Infect. Immun. 65:2313-2320(1997) [PubMed: 9169769] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: CP76.

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Cross-references

Sequence databases

Y10356 Genomic DNA. Translation: CAA71385.1.

3D structure databases

HSSPHSSP built from PDB template 1E9Z based on UniProtKB P14917.
ModBaseSearch...

Protein family/group databases

MEROPSM38.982.

Enzyme and pathway databases

BRENDA3.5.1.5. 2406.

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...

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Entry information

Entry nameURE1_CLOPE
AccessionPrimary (citable) accession number: P94669
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: June 16, 2009
This is version 67 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)

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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