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Protein

Urease subunit alpha

Gene

ureC

Organism
Klebsiella aerogenes (Enterobacter aerogenes)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Ni cationUniRule annotation3 PublicationsNote: Binds 2 nickel ions per subunit.UniRule annotation3 Publications

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

The apoenzyme can be activated in vitro in the presence of nickel ions and carbon dioxide, which promotes carbamylation of Lys-217.4 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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 alpha (ureC), Urease subunit alpha (ureC_2), Urease subunit alpha (ureC), Urease subunit beta (ureB), Urease subunit beta (ureB_1), Urease subunit beta (ureB), Urease subunit beta (ureB), Urease subunit alpha (ureC), Urease subunit alpha (ureC_1), Urease subunit beta (ureB_2), Urease subunit gamma (ureA_1), Urease subunit gamma (ureA), Urease subunit gamma (ureA), Urease subunit gamma (ureA), Urease subunit beta (ureB), 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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi134Nickel 1; via tele nitrogen1
Metal bindingi136Nickel 1; via tele nitrogen1
Metal bindingi217Nickel 1; via carbamate group1
Metal bindingi217Nickel 2; via carbamate group1
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei219Substrate1
Metal bindingi246Nickel 2; via pros nitrogen1
Metal bindingi272Nickel 2; via tele nitrogen1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei320Proton donor1
Metal bindingi360Nickel 11

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase
LigandMetal-binding, Nickel

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.5.1.5 152

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P18314

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00258;UER00370

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M38.982

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Urease subunit alphaUniRule annotation (EC:3.5.1.5UniRule annotation)
Alternative name(s):
Urea amidohydrolase subunit alphaUniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ureCUniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiKlebsiella aerogenes (Enterobacter aerogenes)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri548 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeKlebsiella

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi134H → A: Abrogates activity and reduces binding to nickel ions. 1 Publication1
Mutagenesisi136H → A: Abrogates activity and reduces binding to nickel ions. 1 Publication1
Mutagenesisi217K → A, C or E: Reduces activity 8000-fold and abrogates binding to nickel ions. 1 Publication1
Mutagenesisi219H → A: Reduces activity 500-fold and increases KM 1000-fold. Resistant to inactivation by diethylpyrocarbonate and iodoacetamide. 2 Publications1
Mutagenesisi219H → N or Q: Increases KM 100-fold; optimum pH is 6. 2 Publications1
Mutagenesisi221D → A: Reduces activity 1000-fold and increases KM 10-fold. 1 Publication1
Mutagenesisi221D → N: Reduces activity 50-fold. 1 Publication1
Mutagenesisi246H → A: Abrogates activity and reduces binding to nickel ions. 1 Publication1
Mutagenesisi312H → A: Enhances thermal stability above 50 degrees Celsius. 1
Mutagenesisi319C → A: Reduces activity 2-fold, but increases KM only 1.7-fold; optimum pH is 6.7. Reduces binding of nickel ions. Resistant to inactivation by iodoacetamide. 2 Publications1
Mutagenesisi319C → D: Reduces activity 20-fold, but increases KM only 1.9-fold; optimum pH is 5.2. Reduces binding of nickel ions. Resistant to inactivation by iodoacetamide. 2 Publications1
Mutagenesisi319C → S: Reduces activity 3000-fold, but increases KM only 3.9-fold; optimum pH is 5.2. Reduces binding of nickel ions. Resistant to inactivation by iodoacetamide. 2 Publications1
Mutagenesisi319C → Y: Abrogates activity. 2 Publications1
Mutagenesisi320H → A: Reduces activity 100000-fold, but increases KM only 3-fold; optimum pH is 6.75. Resistant to inactivation by diethylpyrocarbonate and iodoacetamide. 2 Publications1
Mutagenesisi320H → N or Q: Reduces activity 100000-fold, but increases KM only 3-fold. 2 Publications1
Mutagenesisi336R → Q: Reduces activity 10000-fold, but has no effect on KM. 1 Publication1

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB00551 Acetohydroxamic Acid
DB05265 Ecabet

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000675431 – 567Urease subunit alphaAdd BLAST567

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei217N6-carboxylysineUniRule annotation4 Publications1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Carbamylation allows a single lysine to coordinate two nickel ions.UniRule annotation4 Publications

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P18314

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
ureAP1831611EBI-1028571,EBI-1028581

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P18314, 3 interactors

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1567
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P18314

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P18314

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P18314

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini129 – 567UreaseUniRule annotationAdd BLAST439

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family.UniRule annotation

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00375 Urease_alpha, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.30.40.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01953 Urease_alpha, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006680 Amidohydro-rel
IPR011059 Metal-dep_hydrolase_composite
IPR032466 Metal_Hydrolase
IPR011612 Urease_alpha_N_dom
IPR017950 Urease_AS
IPR005848 Urease_asu
IPR017951 Urease_asu_c
IPR029754 Urease_Ni-bd

The PANTHER Classification System

More...
PANTHERi
PTHR43440 PTHR43440, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01979 Amidohydro_1, 1 hit
PF00449 Urease_alpha, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01752 UREASE

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51338 SSF51338, 2 hits
SSF51556 SSF51556, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01792 urease_alph, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01120 UREASE_1, 1 hit
PS00145 UREASE_2, 1 hit
PS51368 UREASE_3, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P18314-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSNISRQAYA DMFGPTVGDK VRLADTELWI EVEDDLTTYG EEVKFGGGKV
60 70 80 90 100
IRDGMGQGQM LAADCVDLVL TNALIVDHWG IVKADIGVKD GRIFAIGKAG
110 120 130 140 150
NPDIQPNVTI PIGAATEVIA AEGKIVTAGG IDTHIHWICP QQAEEALVSG
160 170 180 190 200
VTTMVGGGTG PAAGTHATTC TPGPWYISRM LQAADSLPVN IGLLGKGNVS
210 220 230 240 250
QPDALREQVA AGVIGLKIHE DWGATPAAID CALTVADEMD IQVALHSDTL
260 270 280 290 300
NESGFVEDTL AAIGGRTIHT FHTEGAGGGH APDIITACAH PNILPSSTNP
310 320 330 340 350
TLPYTLNTID EHLDMLMVCH HLDPDIAEDV AFAESRIRRE TIAAEDVLHD
360 370 380 390 400
LGAFSLTSSD SQAMGRVGEV ILRTWQVAHR MKVQRGALAE ETGDNDNFRV
410 420 430 440 450
KRYIAKYTIN PALTHGIAHE VGSIEVGKLA DLVVWSPAFF GVKPATVIKG
460 470 480 490 500
GMIAIAPMGD INASIPTPQP VHYRPMFGAL GSARHHCRLT FLSQAAAANG
510 520 530 540 550
VAERLNLRSA IAVVKGCRTV QKADMVHNSL QPNITVDAQT YEVRVDGELI
560
TSEPADVLPM AQRYFLF
Length:567
Mass (Da):60,305
Last modified:November 1, 1990 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i2ECF3C4268A2E2C7
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M36068 Genomic DNA Translation: AAA25151.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36068 Genomic DNA Translation: AAA25151.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A5KX-ray2.20C2-567[»]
1A5LX-ray2.20C2-567[»]
1A5MX-ray2.00C2-567[»]
1A5NX-ray2.40C2-567[»]
1A5OX-ray2.50C2-567[»]
1EF2X-ray2.50A2-567[»]
1EJRX-ray2.00C1-567[»]
1EJSX-ray2.00C1-567[»]
1EJTX-ray2.00C1-567[»]
1EJUX-ray2.00C1-567[»]
1EJVX-ray2.40C1-567[»]
1EJWX-ray1.90C1-567[»]
1EJXX-ray1.60C1-567[»]
1FWAX-ray2.00C1-567[»]
1FWBX-ray2.00C1-567[»]
1FWCX-ray2.00C1-567[»]
1FWDX-ray2.00C1-567[»]
1FWEX-ray2.00C1-567[»]
1FWFX-ray2.00C1-567[»]
1FWGX-ray2.00C1-567[»]
1FWHX-ray2.00C1-567[»]
1FWIX-ray2.00C1-567[»]
1FWJX-ray2.20C1-567[»]
1KRAX-ray2.30C1-567[»]
1KRBX-ray2.50C1-567[»]
1KRCX-ray2.50C1-567[»]
2KAUX-ray2.00C1-567[»]
4EP8X-ray1.55C2-567[»]
4EPBX-ray1.75C2-567[»]
4EPDX-ray1.70C2-567[»]
4EPEX-ray2.05C2-567[»]
ProteinModelPortaliP18314
SMRiP18314
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP18314, 3 interactors

Chemistry databases

DrugBankiDB00551 Acetohydroxamic Acid
DB05265 Ecabet

Protein family/group databases

MEROPSiM38.982

Proteomic databases

PRIDEiP18314

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayi
UPA00258;UER00370

BRENDAi3.5.1.5 152
SABIO-RKiP18314

Miscellaneous databases

EvolutionaryTraceiP18314

Family and domain databases

CDDicd00375 Urease_alpha, 1 hit
Gene3Di2.30.40.10, 1 hit
HAMAPiMF_01953 Urease_alpha, 1 hit
InterProiView protein in InterPro
IPR006680 Amidohydro-rel
IPR011059 Metal-dep_hydrolase_composite
IPR032466 Metal_Hydrolase
IPR011612 Urease_alpha_N_dom
IPR017950 Urease_AS
IPR005848 Urease_asu
IPR017951 Urease_asu_c
IPR029754 Urease_Ni-bd
PANTHERiPTHR43440 PTHR43440, 1 hit
PfamiView protein in Pfam
PF01979 Amidohydro_1, 1 hit
PF00449 Urease_alpha, 1 hit
PRINTSiPR01752 UREASE
SUPFAMiSSF51338 SSF51338, 2 hits
SSF51556 SSF51556, 1 hit
TIGRFAMsiTIGR01792 urease_alph, 1 hit
PROSITEiView protein in PROSITE
PS01120 UREASE_1, 1 hit
PS00145 UREASE_2, 1 hit
PS51368 UREASE_3, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiURE1_KLEAE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P18314
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: December 5, 2018
This is version 146 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

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