E6Y5X0 · UREA2_CANEN
- ProteinUrease 2
- GeneJBURE-II
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids840 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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
- 2 H+ + H2O + urea = CO2 + 2 NH4+This reaction proceeds in the forward direction.
Cofactor
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).
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 407 | Ni2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 409 | Ni2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 490 | Ni2+ 1 (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 490 | Ni2+ 2 (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 492 | substrate | ||||
Sequence: H | ||||||
Binding site | 519 | Ni2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 545 | Ni2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 593 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 633 | Ni2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | urease complex | |
Molecular Function | lipid binding | |
Molecular Function | nickel cation binding | |
Molecular Function | urease activity | |
Biological Process | urea catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameUrease 2
- EC number
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > 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 accessionE6Y5X0
- Secondary accessions
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000456907 | 1-840 | Urease 2 | |||
Sequence: MKLSPREVEKISLHNAGFLAQKRLARGVRLNYSESVALIASQILEHARDGEKTVAQLMSIGKHLLGRRQVLPAVPHLLNIIQVEATLPNGTKLVTVHDPIANENGDLEEALYGSFLPVPSLDKFAESKEEHKIPGEIICADGRLTLNPGRKAVFLKVVNHGDRPIQVGSHYHFIEVNPYLTFDRRKAYGMRLNIAAGDSVRFEPGDHKTVNLVSIGGNKIIRGGNAIADGPVNEANCKAAMEIVCRREFGHKEEEDASEGVTTGDPDCPFTKAIPREEYANKYGPTIGDKIRLGDTDLIAEIEKDFALYGDESVFGGGKVIRDGMGQSSGHPPAMSLDTVITSAVIIDYTGIIKADIGIKDGLIASIGKAGNPDIMNGVFPNMIIGVNTEVICGEGLIVTAGGIDCHVHYICPQSLDEAISSGITTVVGGGTGPTDGSRATTCTPAPTQMKLMLQSTDDIPLNFGFTGKGSGSHPDELHEIIKAGAMGLKLHEDWGCTPAAIDNCLAVAEQHDIQVNIHTDTVNESGFVEHTIAAFNGRTIHTYHSEGAGGGHAPDIIKVCSMKNVLPSSTNTTRPLTSNTVDEHLDMLMVCHKLNREIPEDLAFASSRVREQTIAAEDILHDIGGISIISSDAQAVGRIGEVISCTWQTADKMKAERGPLQPDGSDNDNFRIKRYIAKYTINPAIVNGISQYVGSVEVGKLADLVIWKPSFFGAKPDIVIKGGSIAWADMGDPNGSIPTPEPVLMRPMYGTLGKAGSALSIAFVSKAALDLGVKVLYGLNKRVEAVSNVRKLTKLDLKLNNSLPEITVCPETFTVTVDGQALSSEAVTTLPLSQNYFIF | ||||||
Modified residue | 490 | N6-carboxylysine | ||||
Sequence: K |
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.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 402-840 | Urease | ||||
Sequence: GGIDCHVHYICPQSLDEAISSGITTVVGGGTGPTDGSRATTCTPAPTQMKLMLQSTDDIPLNFGFTGKGSGSHPDELHEIIKAGAMGLKLHEDWGCTPAAIDNCLAVAEQHDIQVNIHTDTVNESGFVEHTIAAFNGRTIHTYHSEGAGGGHAPDIIKVCSMKNVLPSSTNTTRPLTSNTVDEHLDMLMVCHKLNREIPEDLAFASSRVREQTIAAEDILHDIGGISIISSDAQAVGRIGEVISCTWQTADKMKAERGPLQPDGSDNDNFRIKRYIAKYTINPAIVNGISQYVGSVEVGKLADLVIWKPSFFGAKPDIVIKGGSIAWADMGDPNGSIPTPEPVLMRPMYGTLGKAGSALSIAFVSKAALDLGVKVLYGLNKRVEAVSNVRKLTKLDLKLNNSLPEITVCPETFTVTVDGQALSSEAVTTLPLSQNYFIF |
Sequence similarities
In the C-terminal section; belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family.
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
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.
- Name1
- SynonymsJBURE-IIB
- Length840
- Mass (Da)90,060
- Last updated2011-03-08 v1
- ChecksumDC6B34EA65BA06B7
E6Y5X0-2
- Name2
- SynonymsJBURE-II
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_061722 | 1-66 | in isoform 2 | |||
Sequence: MKLSPREVEKISLHNAGFLAQKRLARGVRLNYSESVALIASQILEHARDGEKTVAQLMSIGKHLLG → MNHFN | ||||||
Sequence conflict | 256 | in Ref. 1; AAN08919 | ||||
Sequence: D → E | ||||||
Sequence conflict | 623 | in Ref. 1; AAN08919 | ||||
Sequence: D → H | ||||||
Alternative sequence | VSP_061723 | 783-840 | in isoform 2 | |||
Sequence: RVEAVSNVRKLTKLDLKLNNSLPEITVCPETFTVTVDGQALSSEAVTTLPLSQNYFIF → GWNP |
Keywords
- Coding sequence diversity
- Technical term