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Protein

Urease subunit gamma

Gene

ureA

Organism
Sporosarcina pasteurii (Bacillus pasteurii)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Urea + H2O = CO2 + 2 NH3.UniRule annotation

Pathwayi

GO - Molecular functioni

  1. nickel cation binding Source: InterPro
  2. urease activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. urea catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

UniPathwayiUPA00258; UER00370.

Names & Taxonomyi

Protein namesi
Recommended name:
Urease subunit gammaUniRule annotation (EC:3.5.1.5UniRule annotation)
Alternative name(s):
Urea amidohydrolase subunit gammaUniRule annotation
Gene namesi
Name:ureAUniRule annotation
OrganismiSporosarcina pasteurii (Bacillus pasteurii)
Taxonomic identifieri1474 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesPlanococcaceaeSporosarcina

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 100100Urease subunit gammaPRO_0000097991Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-formylmethionineCurated

Post-translational modificationi

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.

Keywords - PTMi

Formylation

Interactioni

Subunit structurei

Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha) subunits. Three heterotrimers associate to form the active enzyme.UniRule annotation5 Publications

Structurei

Secondary structure

1
100
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 2521Combined sources
Helixi32 – 4918Combined sources
Helixi53 – 597Combined sources
Helixi60 – 623Combined sources
Helixi66 – 683Combined sources
Helixi73 – 764Combined sources
Beta strandi78 – 869Combined sources
Beta strandi89 – 979Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4CEUX-ray1.58A1-100[»]
4CEXX-ray1.59A1-100[»]
4UBPX-ray1.55A1-100[»]
ProteinModelPortaliP41022.
SMRiP41022. Positions 1-100.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP41022.

Family & Domainsi

Sequence similaritiesi

Belongs to the urease gamma subunit family.UniRule annotation

Family and domain databases

Gene3Di3.30.280.10. 1 hit.
HAMAPiMF_00739. Urease_gamma.
InterProiIPR012010. Urease_gamma.
IPR002026. Urease_gamma/gamma-beta_su.
[Graphical view]
PfamiPF00547. Urease_gamma. 1 hit.
[Graphical view]
PIRSFiPIRSF001223. Urease_gamma. 1 hit.
ProDomiPD002319. Urease_gamma_reg. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF54111. SSF54111. 1 hit.
TIGRFAMsiTIGR00193. urease_gam. 1 hit.

Sequencei

Sequence statusi: Complete.

P41022-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHLNPAEKEK LQIFLASELL LRRKARGLKL NYPEAVAIIT SFIMEGARDG
60 70 80 90 100
KTVAMLMEEG KHVLTRDDVM EGVPEMIDDI QAEATFPDGT KLVTVHNPIS
Length:100
Mass (Da):11,146
Last modified:February 1, 1995 - v1
Checksum:i773EC3587BF6CA36
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78411 Genomic DNA. Translation: CAA55173.1.
PIRiS47102.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78411 Genomic DNA. Translation: CAA55173.1.
PIRiS47102.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4CEUX-ray1.58A1-100[»]
4CEXX-ray1.59A1-100[»]
4UBPX-ray1.55A1-100[»]
ProteinModelPortaliP41022.
SMRiP41022. Positions 1-100.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP41022.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00258; UER00370.

Miscellaneous databases

EvolutionaryTraceiP41022.

Family and domain databases

Gene3Di3.30.280.10. 1 hit.
HAMAPiMF_00739. Urease_gamma.
InterProiIPR012010. Urease_gamma.
IPR002026. Urease_gamma/gamma-beta_su.
[Graphical view]
PfamiPF00547. Urease_gamma. 1 hit.
[Graphical view]
PIRSFiPIRSF001223. Urease_gamma. 1 hit.
ProDomiPD002319. Urease_gamma_reg. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF54111. SSF54111. 1 hit.
TIGRFAMsiTIGR00193. urease_gam. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiURE3_SPOPA
AccessioniPrimary (citable) accession number: P41022
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: February 4, 2015
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.