E6Y5X0 · UREA2_CANEN

Function

function

Urea hydrolase involved in recycling metabolically derived urea generated internally or externally (By similarity).
Is able to impair growth of the phytopathogenic fungus Penicillium herguei, and shows entomotoxic activity by inhibiting diuresis in Malpighian tubules isolated from Rhodnius prolixus (PubMed:21893219).

Catalytic activity

Cofactor

Ni2+ (UniProtKB | Rhea| CHEBI:49786 )

Note: Binds 2 nickel ions per subunit.

Biotechnology

Canatoxin, a urease isoform derived from Canavalia ensiformis seeds, shows insecticidal activity against different insect species (PubMed:17875343).
Its toxicity relies on an internal 10 kDa peptide (pepcanatox), released by hydrolysis of canatoxin by cathepsins in the digestive system of susceptible insects (PubMed:17875343).
In laboratory feeding experiments is 100% effective against larvae of Dysdercus peruvianus and Spodoptera frugiperda (PubMed:17875343).

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 site407Ni2+ 1 (UniProtKB | ChEBI)
Binding site409Ni2+ 1 (UniProtKB | ChEBI)
Binding site490Ni2+ 1 (UniProtKB | ChEBI); via carbamate group
Binding site490Ni2+ 2 (UniProtKB | ChEBI); via carbamate group
Binding site492substrate
Binding site519Ni2+ 2 (UniProtKB | ChEBI)
Binding site545Ni2+ 2 (UniProtKB | ChEBI)
Active site593Proton donor
Binding site633Ni2+ 1 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componenturease complex
Molecular Functionlipid binding
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 2
  • EC number
  • Alternative names
    • Jaburetox
    • Jack bean urease II
    • Urea amidohydrolase

Gene names

    • Name
      JBURE-II

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fabales > Fabaceae > Papilionoideae > 50 kb inversion clade > NPAAA clade > indigoferoid/millettioid clade > Phaseoleae > Canavalia

Accessions

  • Primary accession
    E6Y5X0
  • Secondary accessions
    • Q8H6V8

Subcellular Location

Phenotypes & Variants

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00004569071-840Urease 2
Modified residue490N6-carboxylysine

Post-translational modification

Carboxylation allows a single lysine to coordinate two nickel ions.

Expression

Tissue specificity

Expressed in flower buds and young developing seeds.

Induction

Induced in leaves treated with abscisic acid (ABA).

Interaction

Subunit

Homohexamer. Other oligomeric forms may exist depending on pH and presence of salts.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain402-840Urease

Sequence similarities

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

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

E6Y5X0-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Name
    1
  • Synonyms
    JBURE-IIB
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    840
  • Mass (Da)
    90,060
  • Last updated
    2011-03-08 v1
  • Checksum
    DC6B34EA65BA06B7
MKLSPREVEKISLHNAGFLAQKRLARGVRLNYSESVALIASQILEHARDGEKTVAQLMSIGKHLLGRRQVLPAVPHLLNIIQVEATLPNGTKLVTVHDPIANENGDLEEALYGSFLPVPSLDKFAESKEEHKIPGEIICADGRLTLNPGRKAVFLKVVNHGDRPIQVGSHYHFIEVNPYLTFDRRKAYGMRLNIAAGDSVRFEPGDHKTVNLVSIGGNKIIRGGNAIADGPVNEANCKAAMEIVCRREFGHKEEEDASEGVTTGDPDCPFTKAIPREEYANKYGPTIGDKIRLGDTDLIAEIEKDFALYGDESVFGGGKVIRDGMGQSSGHPPAMSLDTVITSAVIIDYTGIIKADIGIKDGLIASIGKAGNPDIMNGVFPNMIIGVNTEVICGEGLIVTAGGIDCHVHYICPQSLDEAISSGITTVVGGGTGPTDGSRATTCTPAPTQMKLMLQSTDDIPLNFGFTGKGSGSHPDELHEIIKAGAMGLKLHEDWGCTPAAIDNCLAVAEQHDIQVNIHTDTVNESGFVEHTIAAFNGRTIHTYHSEGAGGGHAPDIIKVCSMKNVLPSSTNTTRPLTSNTVDEHLDMLMVCHKLNREIPEDLAFASSRVREQTIAAEDILHDIGGISIISSDAQAVGRIGEVISCTWQTADKMKAERGPLQPDGSDNDNFRIKRYIAKYTINPAIVNGISQYVGSVEVGKLADLVIWKPSFFGAKPDIVIKGGSIAWADMGDPNGSIPTPEPVLMRPMYGTLGKAGSALSIAFVSKAALDLGVKVLYGLNKRVEAVSNVRKLTKLDLKLNNSLPEITVCPETFTVTVDGQALSSEAVTTLPLSQNYFIF

E6Y5X0-2

  • Name
    2
  • Synonyms
    JBURE-II
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-66: MKLSPREVEKISLHNAGFLAQKRLARGVRLNYSESVALIASQILEHARDGEKTVAQLMSIGKHLLG → MNHFN
    • 783-840: RVEAVSNVRKLTKLDLKLNNSLPEITVCPETFTVTVDGQALSSEAVTTLPLSQNYFIF → GWNP

Features

Showing features for alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Alternative sequenceVSP_0617221-66in isoform 2
Sequence conflict256in Ref. 1; AAN08919
Sequence conflict623in Ref. 1; AAN08919
Alternative sequenceVSP_061723783-840in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF468788
EMBL· GenBank· DDBJ
AAN08919.1
EMBL· GenBank· DDBJ
mRNA
EU938655
EMBL· GenBank· DDBJ
ACL14297.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

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