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Protein

Urease subunit alpha

Gene

ureC

Organism
Klebsiella aerogenes (Enterobacter aerogenes)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

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

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

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 gamma (ureA), Urease subunit alpha (ureC), Urease subunit beta (ureB), Urease subunit gamma (ureA), Urease subunit beta (ureB), Urease subunit alpha (ureC), Urease subunit alpha (ureC), Urease subunit beta (ureB)
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
Metal bindingi134Nickel 1; via tele nitrogen1
Metal bindingi136Nickel 1; via tele nitrogen1
Metal bindingi217Nickel 1; via carbamate group1
Metal bindingi217Nickel 2; via carbamate group1
Binding sitei219Substrate1
Metal bindingi246Nickel 2; via pros nitrogen1
Metal bindingi272Nickel 2; via tele nitrogen1
Active sitei320Proton donor1
Metal bindingi360Nickel 11

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
LigandMetal-binding, Nickel

Enzyme and pathway databases

BRENDAi3.5.1.5 152
SABIO-RKiP18314
UniPathwayi
UPA00258;UER00370

Protein family/group databases

MEROPSiM38.982

Names & Taxonomyi

Protein namesi
Recommended name:
Urease subunit alphaUniRule annotation (EC:3.5.1.5UniRule annotation)
Alternative name(s):
Urea amidohydrolase subunit alphaUniRule annotation
Gene namesi
Name:ureCUniRule annotation
OrganismiKlebsiella aerogenes (Enterobacter aerogenes)
Taxonomic identifieri548 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeKlebsiella

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

DrugBankiDB00551 Acetohydroxamic Acid
DB05265 Ecabet

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000675431 – 567Urease subunit alphaAdd BLAST567

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei217N6-carboxylysineUniRule annotation4 Publications1

Post-translational modificationi

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

Proteomic databases

PRIDEiP18314

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

Binary interactionsi

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

Protein-protein interaction databases

IntActiP18314, 3 interactors

Structurei

Secondary structure

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

3D structure databases

ProteinModelPortaliP18314
SMRiP18314
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18314

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini129 – 567UreaseUniRule annotationAdd BLAST439

Sequence similaritiesi

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

Family and domain databases

CDDicd00375 Urease_alpha, 1 hit
Gene3Di2.30.40.10, 2 hits
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, 2 hits
TIGRFAMsiTIGR01792 urease_alph, 1 hit
PROSITEiView protein in PROSITE
PS01120 UREASE_1, 1 hit
PS00145 UREASE_2, 1 hit
PS51368 UREASE_3, 1 hit

Sequencei

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
Checksum:i2ECF3C4268A2E2C7
GO

Sequence databases

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

Similar proteinsi

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:
PDBei
RCSB PDBi
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, 2 hits
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, 2 hits
TIGRFAMsiTIGR01792 urease_alph, 1 hit
PROSITEiView protein in PROSITE
PS01120 UREASE_1, 1 hit
PS00145 UREASE_2, 1 hit
PS51368 UREASE_3, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiURE1_KLEAE
AccessioniPrimary (citable) accession number: P18314
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: October 10, 2018
This is version 144 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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