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P18316

- URE3_ENTAE

UniProt

P18316 - URE3_ENTAE

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Protein

Urease subunit gamma

Gene

ureA

Organism
Enterobacter aerogenes (Aerobacter aerogenes)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

Urea + H2O = CO2 + 2 NH3.9 PublicationsUniRule annotation

Enzyme regulationi

The apoenzyme can be activated in vitro in the presence of nickel ions and carbon dioxide, which promotes carbamylation of 'Lys-217' of the UreC (alpha) subunit.4 Publications

Kineticsi

  1. KM=2.3 mM for urea4 Publications

Vmax=1.9 mmol/min/mg enzyme4 Publications

pH dependencei

Optimum pH is 7.75.4 Publications

Pathwayi

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

SABIO-RKP18316.
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
OrganismiEnterobacter aerogenes (Aerobacter aerogenes)
Taxonomic identifieri548 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEnterobacter

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 100100Urease subunit gammaPRO_0000098015Add
BLAST

Interactioni

Subunit structurei

Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha) subunits. Three heterotrimers associate to form the active enzyme. The apoenzyme interacts with an accessory complex composed of UreD, UreF and UreG, which is required for the assembly of the nickel containing metallocenter of UreC. The UreE protein may also play a direct role as a metallochaperone in nickel transfer to the urease apoprotein.12 PublicationsUniRule annotation

Binary interactionsi

WithEntry#Exp.IntActNotes
ureCP1831411EBI-1028581,EBI-1028571

Protein-protein interaction databases

IntActiP18316. 2 interactions.

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
1A5KX-ray2.20A1-100[»]
1A5LX-ray2.20A1-100[»]
1A5MX-ray2.00A1-100[»]
1A5NX-ray2.40A1-100[»]
1A5OX-ray2.50A1-100[»]
1EF2X-ray2.50C1-100[»]
1EJRX-ray2.00A1-100[»]
1EJSX-ray2.00A1-100[»]
1EJTX-ray2.00A1-100[»]
1EJUX-ray2.00A1-100[»]
1EJVX-ray2.40A1-100[»]
1EJWX-ray1.90A1-100[»]
1EJXX-ray1.60A1-100[»]
1FWAX-ray2.00A1-100[»]
1FWBX-ray2.00A1-100[»]
1FWCX-ray2.00A1-100[»]
1FWDX-ray2.00A1-100[»]
1FWEX-ray2.00A1-100[»]
1FWFX-ray2.00A1-100[»]
1FWGX-ray2.00A1-100[»]
1FWHX-ray2.00A1-100[»]
1FWIX-ray2.00A1-100[»]
1FWJX-ray2.20A1-100[»]
1KRAX-ray2.30A1-100[»]
1KRBX-ray2.50A1-100[»]
1KRCX-ray2.50A1-100[»]
2KAUX-ray2.00A1-100[»]
4EP8X-ray1.55A1-100[»]
4EPBX-ray1.75A1-100[»]
4EPDX-ray1.70A1-100[»]
4EPEX-ray2.05A1-100[»]
ProteinModelPortaliP18316.
SMRiP18316. Positions 1-100.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18316.

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.

P18316-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MELTPREKDK LLLFTAALVA ERRLARGLKL NYPESVALIS AFIMEGARDG
60 70 80 90 100
KSVASLMEEG RHVLTREQVM EGVPEMIPDI QVEATFPDGS KLVTVHNPII
Length:100
Mass (Da):11,087
Last modified:November 1, 1990 - v1
Checksum:iC5B9E7FAF615C04D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36068 Genomic DNA. Translation: AAA25149.1.
PIRiA36138.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36068 Genomic DNA. Translation: AAA25149.1 .
PIRi A36138.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A5K X-ray 2.20 A 1-100 [» ]
1A5L X-ray 2.20 A 1-100 [» ]
1A5M X-ray 2.00 A 1-100 [» ]
1A5N X-ray 2.40 A 1-100 [» ]
1A5O X-ray 2.50 A 1-100 [» ]
1EF2 X-ray 2.50 C 1-100 [» ]
1EJR X-ray 2.00 A 1-100 [» ]
1EJS X-ray 2.00 A 1-100 [» ]
1EJT X-ray 2.00 A 1-100 [» ]
1EJU X-ray 2.00 A 1-100 [» ]
1EJV X-ray 2.40 A 1-100 [» ]
1EJW X-ray 1.90 A 1-100 [» ]
1EJX X-ray 1.60 A 1-100 [» ]
1FWA X-ray 2.00 A 1-100 [» ]
1FWB X-ray 2.00 A 1-100 [» ]
1FWC X-ray 2.00 A 1-100 [» ]
1FWD X-ray 2.00 A 1-100 [» ]
1FWE X-ray 2.00 A 1-100 [» ]
1FWF X-ray 2.00 A 1-100 [» ]
1FWG X-ray 2.00 A 1-100 [» ]
1FWH X-ray 2.00 A 1-100 [» ]
1FWI X-ray 2.00 A 1-100 [» ]
1FWJ X-ray 2.20 A 1-100 [» ]
1KRA X-ray 2.30 A 1-100 [» ]
1KRB X-ray 2.50 A 1-100 [» ]
1KRC X-ray 2.50 A 1-100 [» ]
2KAU X-ray 2.00 A 1-100 [» ]
4EP8 X-ray 1.55 A 1-100 [» ]
4EPB X-ray 1.75 A 1-100 [» ]
4EPD X-ray 1.70 A 1-100 [» ]
4EPE X-ray 2.05 A 1-100 [» ]
ProteinModelPortali P18316.
SMRi P18316. Positions 1-100.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P18316. 2 interactions.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00258 ; UER00370 .
SABIO-RK P18316.

Miscellaneous databases

EvolutionaryTracei P18316.

Family and domain databases

Gene3Di 3.30.280.10. 1 hit.
HAMAPi MF_00739. Urease_gamma.
InterProi IPR012010. Urease_gamma.
IPR002026. Urease_gamma/gamma-beta_su.
[Graphical view ]
Pfami PF00547. Urease_gamma. 1 hit.
[Graphical view ]
PIRSFi PIRSF001223. Urease_gamma. 1 hit.
ProDomi PD002319. Urease_gamma_reg. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF54111. SSF54111. 1 hit.
TIGRFAMsi TIGR00193. urease_gam. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Sequence of the Klebsiella aerogenes urease genes and evidence for accessory proteins facilitating nickel incorporation."
    Mulrooney S.B., Hausinger R.P.
    J. Bacteriol. 172:5837-5843(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY.
    Strain: CG253.
  2. "Site-directed mutagenesis of the active site cysteine in Klebsiella aerogenes urease."
    Martin P.R., Hausinger R.P.
    J. Biol. Chem. 267:20024-20027(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  3. "Site-directed mutagenesis of Klebsiella aerogenes urease: identification of histidine residues that appear to function in nickel ligation, substrate binding, and catalysis."
    Park I.-S., Hausinger R.P.
    Protein Sci. 2:1034-1041(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  4. "In vitro activation of urease apoprotein and role of UreD as a chaperone required for nickel metallocenter assembly."
    Park I.-S., Carr M.B., Hausinger R.P.
    Proc. Natl. Acad. Sci. U.S.A. 91:3233-3237(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, INTERACTION WITH UREB; UREC AND URED.
  5. "Evidence for the presence of urease apoprotein complexes containing UreD, UreF, and UreG in cells that are competent for in vivo enzyme activation."
    Park I.-S., Hausinger R.P.
    J. Bacteriol. 177:1947-1951(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, INTERACTION WITH UREB; UREC; URED; UREF AND UREG.
  6. "Requirement of carbon dioxide for in vitro assembly of the urease nickel metallocenter."
    Park I.-S., Hausinger R.P.
    Science 267:1156-1158(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION.
  7. "Purification and activation properties of UreD-UreF-urease apoprotein complexes."
    Moncrief M.B.C., Hausinger R.P.
    J. Bacteriol. 178:5417-5421(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, INTERACTION WITH UREB; UREC; URED AND UREF.
  8. "GTP-dependent activation of urease apoprotein in complex with the UreD, UreF, and UreG accessory proteins."
    Soriano A., Hausinger R.P.
    Proc. Natl. Acad. Sci. U.S.A. 96:11140-11144(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, INTERACTION WITH UREB; UREC; URED; UREF AND UREG.
  9. "UreE stimulation of GTP-dependent urease activation in the UreD-UreF-UreG-urease apoprotein complex."
    Soriano A., Colpas G.J., Hausinger R.P.
    Biochemistry 39:12435-12440(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, ACTIVATION OF THE APOPROTEIN BY UREE.
  10. "Dual effects of ionic strength on Klebsiella aerogenes urease: pH-dependent activation and inhibition."
    Mulrooney S.B., Zakharian T., Schaller R.A., Hausinger R.P.
    Arch. Biochem. Biophys. 394:280-282(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
  11. "Chemical cross-linking and mass spectrometric identification of sites of interaction for UreD, UreF, and urease."
    Chang Z., Kuchar J., Hausinger R.P.
    J. Biol. Chem. 279:15305-15313(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UREB; UREC; URED AND UREF, IDENTIFICATION BY MASS SPECTROMETRY.
  12. "The crystal structure of urease from Klebsiella aerogenes."
    Jabri E., Carr M.B., Hausinger R.P., Karplus P.A.
    Science 268:998-1004(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH UREB AND UREC.
  13. "Structures of the Klebsiella aerogenes urease apoenzyme and two active-site mutants."
    Jabri E., Karplus P.A.
    Biochemistry 35:10616-10626(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH UREB AND UREC.
  14. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH UREB AND UREC.
  15. "Structures of Cys319 variants and acetohydroxamate-inhibited Klebsiella aerogenes urease."
    Pearson M.A., Michel L.O., Hausinger R.P., Karplus P.A.
    Biochemistry 36:8164-8172(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH UREB; UREC AND ACETOHYDROXAMIC ACID.
  16. "Chemical rescue of Klebsiella aerogenes urease variants lacking the carbamylated-lysine nickel ligand."
    Pearson M.A., Schaller R.A., Michel L.O., Karplus P.A., Hausinger R.P.
    Biochemistry 37:6214-6220(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH UREB; UREC AND FORMATE.
  17. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH UREB AND UREC.
  18. "Kinetic and structural characterization of urease active site variants."
    Pearson M.A., Park I.-S., Schaller R.A., Michel L.O., Karplus P.A., Hausinger R.P.
    Biochemistry 39:8575-8584(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH UREB AND UREC, BIOPHYSICOCHEMICAL PROPERTIES.

Entry informationi

Entry nameiURE3_ENTAE
AccessioniPrimary (citable) accession number: P18316
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: November 26, 2014
This is version 102 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