P0CS23 · UREA_CRYNB

Function

function

Plays a nutritional role via nitrogen acquisition in the environment (By similarity).
Contributes to the central nervous system invasion by enhancing yeast sequestration within microcapillary beds (such as within the brain) during hematogenous spread, thereby facilitating blood-to-brain invasion by C.neoformans (By similarity).
Affects fitness within the mammalian phagosome, promoting non-lytic exocytosis while delaying intracellular replication and thus reducing phagolysosomal membrane damage, events that could facilitate cryptococcal dissemination when transported inside macrophages (By similarity).
Urease activity is also associated with the regulation of key intracellular metabolic pathways, including melanin biosynthesis, polyamine biosynthesis, as well as intracellular levels of proline and reactive oxygen species (By similarity).

Catalytic activity

Cofactor

Ni2+ (UniProtKB | Rhea| CHEBI:49786 )

Note: Binds 2 Ni2+ ions per subunit.

Activity regulation

The urease accessory proteins URE4, URE6 and URE7 are required for urease activity, URE7 supplying nickel for the functional urease.

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 site400Ni2+ 1 (UniProtKB | ChEBI)
Binding site402Ni2+ 1 (UniProtKB | ChEBI)
Binding site402urea (UniProtKB | ChEBI)
Binding site433urea (UniProtKB | ChEBI)
Binding site483Ni2+ 1 (UniProtKB | ChEBI); via carbamate group
Binding site483Ni2+ 2 (UniProtKB | ChEBI); via carbamate group
Binding site485urea (UniProtKB | ChEBI)
Binding site512Ni2+ 2 (UniProtKB | ChEBI)
Binding site512urea (UniProtKB | ChEBI)
Binding site538Ni2+ 2 (UniProtKB | ChEBI)
Active site586Proton donor
Binding site626Ni2+ 1 (UniProtKB | ChEBI)
Binding site629urea (UniProtKB | ChEBI)

GO annotations

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

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

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

Gene names

    • Ordered locus names
      CNBL1900

Organism names

Accessions

  • Primary accession
    P0CS23
  • Secondary accessions
    • Q55IZ5
    • Q5KCQ6

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00004103241-833Urease
Modified residue483N6-carboxylysine

Post-translational modification

Carboxylation allows a single lysine to coordinate two nickel ions.

Interaction

Subunit

Homohexamer.

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain395-833Urease

Sequence similarities

In the C-terminal section; belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    833
  • Mass (Da)
    90,455
  • Last updated
    2011-06-28 v1
  • Checksum
    E090343FE3252584
MHLLPRETDKLIVTTLGTLAQRRLARGLILNRAETIALISSQLQEFIRDGRHSVAELMDLGKKMLGRRHVRKGVPESIHTIQVEGTFPDGVFLVTVDDPISSDDGDLNNAFYGSFLPIPSADVFPAAPEPADTLLGALICRKEPIKINASRRRFKLEVKNAGDRPIQVGSHYHFLETNPALIFDRLLSYGYHLDIPAGTAVRFEPGEKKTVTMVEFGGKKIFHGGSGLASGSFDENLRETKVKEMVEKGGFGHKDQEKVEEGPTTEMNREVYASMFGPTTGDKIKLADMDLWIEVEKDYTVYGEECKFGGGKVLRDGGGQASGRHEHEVLDLVITNALIVDWNGIYKADIGVKNGIIVGIGKAGNPDMMDGVTDGMIVGSSTEVIAGEKLIITAGALDVHVHYICPQLMTEALASGITTVVGGGTGPADGSNATTCTSSSFYMQNMIKATDTVPLNFGFTGKGNDSGTNALRDVIEAGACGLKVHEDWGATPEVIDRALSIADEYDVQVNLHSDTLNESGYVESTLAAIKGRTIHSYHTEGAGGGHAPDIIVVCEYENVLPSSTNPTRPYAVNTLDEHLDMLMVCHHLDKSIPEDIAFADSRIRSETVAAEDVLQDTGAISMISSDCQAMGRIGEVITRTWRTAAKMKQFRGPLEGDEPTRDNNRVKRYVAKYTINPAITHGMSHLIGQVAVGCLADLVFWTAESFGARPEMILKGGVIAWAAMGDANASIPTVQPVIGRPMWGSQPEAAALNSIVWVSQASLDKDLVKRFNIKKRAEAVKNCRAIGKKDMKWNDSMPKMTVDPETYDVHADGVLCDVPPADKLPLTKRYFVY

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AAEY01000057
EMBL· GenBank· DDBJ
EAL17675.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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