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Protein

Urease subunit beta

Gene

ureB

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

Functioni

Catalytic activityi

Urea + H2O = CO2 + 2 NH3.UniRule annotation9 Publications

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
  1. Vmax=1.9 mmol/min/mg enzyme4 Publications

pH dependencei

Optimum pH is 7.75.4 Publications

Pathwayi: urea degradation

This protein is involved in step 1 of the subpathway that synthesizes CO(2) and NH(3) from urea (urease route).UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Urease subunit beta (ureB), Urease subunit alpha (ureC), Urease subunit beta (ureB), Urease subunit gamma (ureA), Urease subunit beta (ureB), Urease subunit alpha (ureC), Urease subunit gamma (ureA), Urease subunit alpha (ureC)
This subpathway is part of the pathway urea degradation, which is itself part of Nitrogen metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes CO(2) and NH(3) from urea (urease route), the pathway urea degradation and in Nitrogen metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BRENDAi3.5.1.5. 152.
SABIO-RKP18315.
UniPathwayiUPA00258; UER00370.

Protein family/group databases

MEROPSiM38.982.

Names & Taxonomyi

Protein namesi
Recommended name:
Urease subunit betaUniRule annotation (EC:3.5.1.5UniRule annotation)
Alternative name(s):
Urea amidohydrolase subunit betaUniRule annotation
Gene namesi
Name:ureBUniRule annotation
OrganismiEnterobacter aerogenes (Aerobacter aerogenes)
Taxonomic identifieri548 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeKlebsiella

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi39H → A: Reduces activity by 20% and reduces thermal stability above 50 degrees Celsius. 1 Publication1
Mutagenesisi41H → A: Reduces activity by 30% and reduces thermal stability above 50 degrees Celsius. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000675771 – 106Urease subunit betaAdd BLAST106

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.UniRule annotation12 Publications

Protein-protein interaction databases

IntActiP18315. 2 interactors.

Structurei

Secondary structure

1106
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 14Combined sources4
Beta strandi21 – 28Combined sources8
Beta strandi30 – 32Combined sources3
Beta strandi34 – 37Combined sources4
Helixi42 – 44Combined sources3
Beta strandi49 – 51Combined sources3
Turni53 – 58Combined sources6
Beta strandi59 – 61Combined sources3
Beta strandi68 – 71Combined sources4
Beta strandi76 – 83Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A5KX-ray2.20B1-101[»]
1A5LX-ray2.20B1-101[»]
1A5MX-ray2.00B1-101[»]
1A5NX-ray2.40B1-101[»]
1A5OX-ray2.50B1-101[»]
1EF2X-ray2.50B1-101[»]
1EJRX-ray2.00B1-101[»]
1EJSX-ray2.00B1-101[»]
1EJTX-ray2.00B1-101[»]
1EJUX-ray2.00B1-101[»]
1EJVX-ray2.40B1-101[»]
1EJWX-ray1.90B1-101[»]
1EJXX-ray1.60B1-101[»]
1FWAX-ray2.00B1-106[»]
1FWBX-ray2.00B1-106[»]
1FWCX-ray2.00B1-106[»]
1FWDX-ray2.00B1-106[»]
1FWEX-ray2.00B1-106[»]
1FWFX-ray2.00B1-106[»]
1FWGX-ray2.00B1-106[»]
1FWHX-ray2.00B1-106[»]
1FWIX-ray2.00B1-106[»]
1FWJX-ray2.20B1-106[»]
1KRAX-ray2.30B1-106[»]
1KRBX-ray2.50B1-106[»]
1KRCX-ray2.50B1-106[»]
2KAUX-ray2.00B1-106[»]
4EP8X-ray1.55B1-101[»]
4EPBX-ray1.75B1-101[»]
4EPDX-ray1.70B1-101[»]
4EPEX-ray2.05B1-101[»]
ProteinModelPortaliP18315.
SMRiP18315.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18315.

Family & Domainsi

Sequence similaritiesi

Belongs to the urease beta subunit family.UniRule annotation

Family and domain databases

CDDicd00407. Urease_beta. 1 hit.
Gene3Di2.10.150.10. 1 hit.
HAMAPiMF_01954. Urease_beta. 1 hit.
InterProiIPR002019. Urease_beta.
[Graphical view]
PfamiPF00699. Urease_beta. 1 hit.
[Graphical view]
SUPFAMiSSF51278. SSF51278. 1 hit.
TIGRFAMsiTIGR00192. urease_beta. 1 hit.

Sequencei

Sequence statusi: Complete.

P18315-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIPGEYHVKP GQIALNTGRA TCRVVVENHG DRPIQVGSHY HFAEVNPALK
60 70 80 90 100
FDRQQAAGYR LNIPAGTAVR FEPGQKREVE LVAFAGHRAV FGFRGEVMGP

LEVNDE
Length:106
Mass (Da):11,695
Last modified:November 1, 1990 - v1
Checksum:iA232BFCD74864EA6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36068 Genomic DNA. Translation: AAA25150.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36068 Genomic DNA. Translation: AAA25150.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A5KX-ray2.20B1-101[»]
1A5LX-ray2.20B1-101[»]
1A5MX-ray2.00B1-101[»]
1A5NX-ray2.40B1-101[»]
1A5OX-ray2.50B1-101[»]
1EF2X-ray2.50B1-101[»]
1EJRX-ray2.00B1-101[»]
1EJSX-ray2.00B1-101[»]
1EJTX-ray2.00B1-101[»]
1EJUX-ray2.00B1-101[»]
1EJVX-ray2.40B1-101[»]
1EJWX-ray1.90B1-101[»]
1EJXX-ray1.60B1-101[»]
1FWAX-ray2.00B1-106[»]
1FWBX-ray2.00B1-106[»]
1FWCX-ray2.00B1-106[»]
1FWDX-ray2.00B1-106[»]
1FWEX-ray2.00B1-106[»]
1FWFX-ray2.00B1-106[»]
1FWGX-ray2.00B1-106[»]
1FWHX-ray2.00B1-106[»]
1FWIX-ray2.00B1-106[»]
1FWJX-ray2.20B1-106[»]
1KRAX-ray2.30B1-106[»]
1KRBX-ray2.50B1-106[»]
1KRCX-ray2.50B1-106[»]
2KAUX-ray2.00B1-106[»]
4EP8X-ray1.55B1-101[»]
4EPBX-ray1.75B1-101[»]
4EPDX-ray1.70B1-101[»]
4EPEX-ray2.05B1-101[»]
ProteinModelPortaliP18315.
SMRiP18315.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP18315. 2 interactors.

Protein family/group databases

MEROPSiM38.982.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00258; UER00370.
BRENDAi3.5.1.5. 152.
SABIO-RKP18315.

Miscellaneous databases

EvolutionaryTraceiP18315.

Family and domain databases

CDDicd00407. Urease_beta. 1 hit.
Gene3Di2.10.150.10. 1 hit.
HAMAPiMF_01954. Urease_beta. 1 hit.
InterProiIPR002019. Urease_beta.
[Graphical view]
PfamiPF00699. Urease_beta. 1 hit.
[Graphical view]
SUPFAMiSSF51278. SSF51278. 1 hit.
TIGRFAMsiTIGR00192. urease_beta. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiURE2_ENTAE
AccessioniPrimary (citable) accession number: P18315
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: November 2, 2016
This is version 112 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

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 one 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.