B5YUX3 · URE1_ECO5E

Function

Catalytic activity

Cofactor

Ni cation (UniProtKB | Rhea| CHEBI:25516 )

Note: Binds 2 nickel ions per subunit.

Pathway

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

Features

Showing features for binding site, active site.

156750100150200250300350400450500550
TypeIDPosition(s)Description
Binding site134Ni2+ 1 (UniProtKB | ChEBI)
Binding site136Ni2+ 1 (UniProtKB | ChEBI)
Binding site217Ni2+ 1 (UniProtKB | ChEBI); via carbamate group
Binding site217Ni2+ 2 (UniProtKB | ChEBI); via carbamate group
Binding site219substrate
Binding site246Ni2+ 2 (UniProtKB | ChEBI)
Binding site272Ni2+ 2 (UniProtKB | ChEBI)
Active site320Proton donor
Binding site360Ni2+ 1 (UniProtKB | ChEBI)

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
    • Ordered locus names
      ECH74115_1323

Organism names

Accessions

  • Primary accession
    B5YUX3

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_10001888721-567Urease subunit alpha
Modified residue217N6-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.

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain129-567Urease

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    567
  • Mass (Da)
    60,495
  • Last updated
    2008-11-25 v1
  • Checksum
    5501063E39E51374
MSNISRQAYADMFGPTTGDKIRLADTELWIEVEDDLTTYGEEVKFGGGKVIRDGMGQGQMLSAGCADLVLTNALIIDYWGIVKADIGVKDGRIFAIGKAGNPDIQPNVTIPIGVSTEIIAAEGRIVTAGGVDTHIHWICPQQAEEALTSGITTMIGGGTGPTAGSNATTCTPGPWYIYQMLQAADSLPVNIGLLGKGNCSNPDALREQVAAGVIGLKIHEDWGATPAVINCALTVADEMDVQVALHSDTLNESGFVEDTLTAIGGRTIHTFHTEGAGGGHAPDIITACAHPNILPSSTNPTLPYTVNTIDEHLDMLMVCHHLDPDIAEDVAFAESRIRQETIAAEDVLHDLGAFSLTSSDSQAMGRVGEVVLRTWQVAHRMKVQRGPLPEESGDNDNVRVKRYIAKYTINPALTHGIAHEVGSIEVGKLADLVLWSPAFFGVKPATIVKGGMIAMAPMGDINGSIPTPQPVHYRPMFAALGSARHRCRVTFLSQAAAANGVAEQLNLHSTTAVVKGCRTVQKADMRHNSLLPDITVDSQTYEVRINGELITSEPADILPMAQRYFLF

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP001164
EMBL· GenBank· DDBJ
ACI35641.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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