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Protein

Urease subunit alpha

Gene

ureC

Organism
Enterobacter aerogenes (Aerobacter aerogenes)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

Enzyme 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 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.

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

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Nickel

Enzyme and pathway databases

BRENDAi3.5.1.5. 152.
SABIO-RKP18314.
UniPathwayiUPA00258; 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
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
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

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
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 5Combined sources3
Helixi6 – 13Combined sources8
Beta strandi20 – 22Combined sources3
Beta strandi29 – 31Combined sources3
Beta strandi50 – 53Combined sources4
Turni54 – 56Combined sources3
Helixi62 – 64Combined sources3
Beta strandi67 – 77Combined sources11
Beta strandi80 – 89Combined sources10
Beta strandi92 – 97Combined sources6
Turni102 – 104Combined sources3
Beta strandi105 – 107Combined sources3
Beta strandi109 – 111Combined sources3
Beta strandi117 – 120Combined sources4
Beta strandi125 – 128Combined sources4
Beta strandi130 – 136Combined sources7
Helixi142 – 149Combined sources8
Beta strandi151 – 157Combined sources7
Beta strandi159 – 162Combined sources4
Helixi163 – 167Combined sources5
Helixi173 – 184Combined sources12
Beta strandi187 – 196Combined sources10
Helixi202 – 211Combined sources10
Beta strandi214 – 219Combined sources6
Helixi220 – 222Combined sources3
Helixi226 – 239Combined sources14
Beta strandi242 – 246Combined sources5
Helixi256 – 263Combined sources8
Beta strandi268 – 270Combined sources3
Turni271 – 274Combined sources4
Beta strandi278 – 280Combined sources3
Turni281 – 283Combined sources3
Helixi284 – 289Combined sources6
Beta strandi293 – 297Combined sources5
Helixi299 – 301Combined sources3
Beta strandi305 – 307Combined sources3
Helixi308 – 320Combined sources13
Beta strandi324 – 326Combined sources3
Helixi327 – 336Combined sources10
Helixi339 – 350Combined sources12
Beta strandi356 – 358Combined sources3
Beta strandi363 – 365Combined sources3
Helixi370 – 385Combined sources16
Beta strandi393 – 395Combined sources3
Helixi397 – 404Combined sources8
Helixi405 – 407Combined sources3
Helixi409 – 414Combined sources6
Turni418 – 420Combined sources3
Beta strandi421 – 424Combined sources4
Beta strandi432 – 435Combined sources4
Helixi437 – 439Combined sources3
Turni440 – 442Combined sources3
Beta strandi445 – 449Combined sources5
Beta strandi452 – 458Combined sources7
Beta strandi463 – 466Combined sources4
Beta strandi472 – 475Combined sources4
Helixi477 – 479Combined sources3
Helixi481 – 487Combined sources7
Beta strandi489 – 492Combined sources4
Helixi494 – 498Combined sources5
Helixi501 – 504Combined sources4
Beta strandi509 – 513Combined sources5
Turni517 – 519Combined sources3
Helixi522 – 524Combined sources3
Beta strandi534 – 536Combined sources3
Turni538 – 540Combined sources3
Beta strandi543 – 545Combined sources3
Beta strandi548 – 550Combined sources3
Beta strandi555 – 557Combined sources3
Beta strandi559 – 561Combined sources3
Turni562 – 564Combined sources3

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...

Miscellaneous databases

EvolutionaryTraceiP18314.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Belongs to the urease family.UniRule annotation
Contains 1 urease domain.UniRule annotation

Family and domain databases

CDDicd00375. Urease_alpha. 1 hit.
Gene3Di2.30.40.10. 1 hit.
HAMAPiMF_01953. Urease_alpha. 1 hit.
InterProiIPR006680. 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.
[Graphical view]
PfamiPF01979. Amidohydro_1. 1 hit.
PF00449. Urease_alpha. 1 hit.
[Graphical view]
PRINTSiPR01752. UREASE.
SUPFAMiSSF51338. SSF51338. 2 hits.
SSF51556. SSF51556. 2 hits.
TIGRFAMsiTIGR01792. urease_alph. 1 hit.
PROSITEiPS01120. UREASE_1. 1 hit.
PS00145. UREASE_2. 1 hit.
PS51368. UREASE_3. 1 hit.
[Graphical view]

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.

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.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00258; UER00370.
BRENDAi3.5.1.5. 152.
SABIO-RKP18314.

Miscellaneous databases

EvolutionaryTraceiP18314.

Family and domain databases

CDDicd00375. Urease_alpha. 1 hit.
Gene3Di2.30.40.10. 1 hit.
HAMAPiMF_01953. Urease_alpha. 1 hit.
InterProiIPR006680. 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.
[Graphical view]
PfamiPF01979. Amidohydro_1. 1 hit.
PF00449. Urease_alpha. 1 hit.
[Graphical view]
PRINTSiPR01752. UREASE.
SUPFAMiSSF51338. SSF51338. 2 hits.
SSF51556. SSF51556. 2 hits.
TIGRFAMsiTIGR01792. urease_alph. 1 hit.
PROSITEiPS01120. UREASE_1. 1 hit.
PS00145. UREASE_2. 1 hit.
PS51368. UREASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiURE1_ENTAE
AccessioniPrimary (citable) accession number: P18314
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: November 2, 2016
This is version 136 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.