P41020 · URE1_SPOPA

Function

Catalytic activity

Cofactor

Ni cation (UniProtKB | Rhea| CHEBI:25516 )
Note: Binds 2 nickel ions per subunit.

Activity regulation

Inhibited by fluoride.

Pathway

Nitrogen metabolism; urea degradation; CO2 and NH3 from urea (urease route): step 1/1.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site137Ni2+ 1 (UniProtKB | ChEBI)
Binding site139Ni2+ 1 (UniProtKB | ChEBI)
Binding site139substrate
Binding site170substrate
Binding site220Ni2+ 1 (UniProtKB | ChEBI); via carbamate group
Binding site220Ni2+ 2 (UniProtKB | ChEBI); via carbamate group
Binding site222substrate
Binding site249Ni2+ 2 (UniProtKB | ChEBI)
Binding site249substrate
Binding site275Ni2+ 2 (UniProtKB | ChEBI)
Active site323Proton donor
Binding site363Ni2+ 1 (UniProtKB | ChEBI)
Binding site366substrate

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionnickel cation binding
Molecular Functionurease activity
Biological Processurea catabolic process

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Urease subunit alpha
  • EC number
  • Alternative names
    • Urea amidohydrolase subunit alpha

Gene names

    • Name
      ureC
    • ORF names
      NCTC4822_02163

Organism names

Accessions

  • Primary accession
    P41020
  • Secondary accessions
    • A0A0H3YL32

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

Chemistry

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000675361-570Urease subunit alpha
Modified residue220N6-carboxylysine

Post-translational modification

Carboxylation allows a single lysine to coordinate two nickel ions.

Interaction

Subunit

Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha) subunits. Three heterotrimers associate to form the active enzyme.

Chemistry

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain132-570Urease

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    570
  • Mass (Da)
    61,400
  • Last updated
    2021-06-02 v2
  • Checksum
    4F6DC7E2703A7568
MKINRQQYAESYGPTVGDQVRLADTDLWIEVEKDTTYGDEAVNFGGGKVLREGMGENGTYTRTENVLDLLLTNALILDYTGIYKADIGVKDGYIVGIGKGGNPDIMDGVTPNMIVGTATEVIAAEGKIVTAGGIDTHVHFINPDQVDVALANGITTLFGGGTGPAEGSKATTVTPGPWNIEKMLKSTEGLPINVGILGKGHGSSIAPIMEQIDAGAAGLKIHEDWGATPASIDRSLTVADEADVQVAIHSDTLNEAGFLEDTLRAINGRVIHSFHVEGAGGGHAPDIMAMAGHPNVLPSSTNPTRPFTVNTIDEHLDMLMVCHHLKQNIPEDVAFADSRIRPETIAAEDILHDLGIISMMSTDALAMGRAGEMVLRTWQTADKMKKQRGPLAEEKNGSDNFRAKRYVSKYTINPAIAQGIAHEVGSIEEGKFADLVLWEPKFFGVKADRVIKGGIIAYAQIGDPSASIPTPQPVMGRRMYGTVGDLIHDTNITFMSKSSIQQGVPAKLGLKRRIGTVKNCRNIGKKDMKWNDVTTDIDINPETYEVKVDGEVLTCEPVKELPMAQRYFLF

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict19in Ref. 1; CAA55175
Sequence conflict28-29in Ref. 1; CAA55175
Sequence conflict35-41in Ref. 1; CAA55175
Sequence conflict263in Ref. 1; CAA55175
Sequence conflict403in Ref. 1; CAA55175
Sequence conflict420in Ref. 1; CAA55175
Sequence conflict498-502in Ref. 4; AAA73986

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X78411
EMBL· GenBank· DDBJ
CAA55175.1
EMBL· GenBank· DDBJ
Genomic DNA
KR133628
EMBL· GenBank· DDBJ
AKN22164.1
EMBL· GenBank· DDBJ
Genomic DNA
UGYZ01000002
EMBL· GenBank· DDBJ
SUJ11615.1
EMBL· GenBank· DDBJ
Genomic DNA
U29368
EMBL· GenBank· DDBJ
AAA73986.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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