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P41022 (URE3_SPOPA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Urease subunit gamma

EC=3.5.1.5
Alternative name(s):
Urea amidohydrolase subunit gamma
Gene names
Name:ureA
OrganismSporosarcina pasteurii (Bacillus pasteurii)
Taxonomic identifier1474 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesPlanococcaceaeSporosarcina

Protein attributes

Sequence length100 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Urea + H2O = CO2 + 2 NH3. HAMAP-Rule MF_00739

Pathway

Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1. HAMAP-Rule MF_00739

Subunit structure

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

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00739.

Post-translational modification

Although not discussed in the published references, Met-1 is represented in the submitted PDB entries as being modified by either a formyl, a carboxyl, or an acetyl group. The N-terminal is probably N-(dihydroxymethyl)methionine, the hydrated form of N-formylmethionine. HAMAP-Rule MF_00739

Sequence similarities

Belongs to the urease gamma subunit family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionHydrolase
   PTMFormylation
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processurea catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionnickel cation binding

Inferred from electronic annotation. Source: InterPro

urease activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 100100Urease subunit gamma HAMAP-Rule MF_00739
PRO_0000097991

Amino acid modifications

Modified residue11N-formylmethionine Probable

Secondary structure

................ 100
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P41022 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 773EC3587BF6CA36

FASTA10011,146
        10         20         30         40         50         60 
MHLNPAEKEK LQIFLASELL LRRKARGLKL NYPEAVAIIT SFIMEGARDG KTVAMLMEEG 

        70         80         90        100 
KHVLTRDDVM EGVPEMIDDI QAEATFPDGT KLVTVHNPIS 

« Hide

References

[1]"Nucleotide sequence of three genes on a urease encoding DNA-fragment from Bacillus pasteurii."
Moersdorf G., Weinmann P., Kaltwasser H.
Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822.
[2]"Crystallization and preliminary high-resolution X-ray diffraction analysis of native and beta-mercaptoethanol-inhibited urease from Bacillus pasteurii."
Benini S., Ciurli S., Rypniewski W.R., Wilson K.S., Mangani S.
Acta Crystallogr. D 54:409-412(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH UREB; UREC AND BETA-MERCAPTOETHANOL.
[3]"A new proposal for urease mechanism based on the crystal structures of the native and inhibited enzyme from Bacillus pasteurii: why urea hydrolysis costs two nickels."
Benini S., Rypniewski W.R., Wilson K.S., Miletti S., Ciurli S., Mangani S.
Structure 7:205-216(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH UREB; UREC AND DIAMIDOPHOSPHATE.
[4]"The complex of Bacillus pasteurii urease with acetohydroxamate anion from X-ray data at 1.55 A resolution."
Benini S., Rypniewski W.R., Wilson K.S., Miletti S., Ciurli S., Mangani S.
J. Biol. Inorg. Chem. 5:110-118(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH UREB; UREC AND ACETOHYDROXAMIC ACID.
[5]"Structure-based rationalization of urease inhibition by phosphate: novel insights into the enzyme mechanism."
Benini S., Rypniewski W.R., Wilson K.S., Ciurli S., Mangani S.
J. Biol. Inorg. Chem. 6:778-790(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH UREB; UREC AND PHOSPHATE.
[6]"Molecular details of urease inhibition by boric acid: insights into the catalytic mechanism."
Benini S., Rypniewski W.R., Wilson K.S., Mangani S., Ciurli S.
J. Am. Chem. Soc. 126:3714-3715(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH UREB; UREC AND BORATE IONS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X78411 Genomic DNA. Translation: CAA55173.1.
PIRS47102.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IE7X-ray1.85A1-100[»]
1S3TX-ray2.10A1-100[»]
1UBPX-ray1.65A1-100[»]
2UBPX-ray2.00A1-100[»]
3UBPX-ray2.00A1-100[»]
4AC7X-ray1.50A1-100[»]
4UBPX-ray1.55A1-100[»]
ProteinModelPortalP41022.
SMRP41022. Positions 1-100.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP41022.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00258; UER00370.

Family and domain databases

Gene3D3.30.280.10. 1 hit.
HAMAPMF_00739. Urease_gamma.
InterProIPR002026. Urease_gamma/gamma-beta_su.
IPR012010. Urease_gamma_su.
[Graphical view]
PfamPF00547. Urease_gamma. 1 hit.
[Graphical view]
PIRSFPIRSF001223. Urease_gamma. 1 hit.
ProDomPD002319. Urease_gamma_reg. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF54111. SSF54111. 1 hit.
TIGRFAMsTIGR00193. urease_gam. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP41022.

Entry information

Entry nameURE3_SPOPA
AccessionPrimary (citable) accession number: P41022
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: February 19, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways