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Reviewed, UniProtKB/Swiss-Prot P41020 (URE1_BACPA)

Last modified June 16, 2009. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Urease subunit alpha
    EC=3.5.1.5
Alternative name(s):
    Urea amidohydrolase subunit alpha
Gene names
Name: ureC
OrganismBacillus pasteurii
Taxonomic identifier1474 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Planococcaceae › Sporosarcina

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Protein attributes

Sequence length569 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

Urea + H2O = CO2 + 2 NH3. HAMAP MF_01953

Cofactor

Binds 2 nickel ions per subunit. HAMAP MF_01953

Pathway

Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1. HAMAP MF_01953

Subunit structure

Heterotrimer of ureA (gamma), ureB (beta) and ureC (alpha) subunits. Three heterotrimers associate to form the active enzyme. HAMAP MF_01953

Subcellular location

Cytoplasm By similarity.

Post-translational modification

Carbamylation allows a single lysine to coordinate two nickel ions. HAMAP MF_01953

Sequence similarities

Belongs to the urease family.

Contains 1 urease domain.

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Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
Nickel
   Molecular functionHydrolase
   Technical term3D-structure
Gene Ontology (GO)
   Biological processurea metabolic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionnickel ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

urease activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 569569Urease subunit alpha HAMAP MF_01953
PRO_0000067536

Regions

Domain131 – 569439Urease

Sites

Active site3221Proton donor Probable
Metal binding1361Nickel 2 HAMAP MF_01953
Metal binding1381Nickel 2 HAMAP MF_01953
Metal binding2191Nickel 1; via carbamate group HAMAP MF_01953
Metal binding2191Nickel 2; via carbamate group HAMAP MF_01953
Metal binding2481Nickel 1 HAMAP MF_01953
Metal binding2741Nickel 1 HAMAP MF_01953
Metal binding3621Nickel 2 HAMAP MF_01953
Binding site2211Substrate Probable

Amino acid modifications

Modified residue2191N6-carboxylysine HAMAP MF_01953

Experimental info

Sequence conflict497 – 5015SSIQQ → ELNSE Ref.2

Secondary structure

1 ............................................................................................................ 569
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P41020-1 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: EC55A5C4293F2E5C

FASTA56961,398
        10         20         30         40         50         60 
MKINRQQYAE SYGPTVGDRV RLADTDLGEV EKDYYYLGDE VNFGGGKVLR EGMGENGTYT 

        70         80         90        100        110        120 
RTENVLDLLL TNALILDYTG IYKADIGVKD GYIVGIGKGG NPDIMDGVTP NMIVGTATEV 

       130        140        150        160        170        180 
IAAEGKIVTA GGIDTHVHFI NPDQVDVALA NGITTLFGGG TGPAEGSKAT TVTPGPWNIE 

       190        200        210        220        230        240 
KMLKSTEGLP INVGILGKGH GSSIAPIMEQ IDAGAAGLKI HEDWGATPAS IDRSLTVADE 

       250        260        270        280        290        300 
ADVQVAIHSD TLNEAGFLED TVRAINGRVI HSFHVEGAGG GHAPDIMAMA GHPNVLPSST 

       310        320        330        340        350        360 
NPTRPFTVNT IDEHLDMLMV CHHLKQNIPE DVAFADSRIR PETIAAEDIL HDLGIISMMS 

       370        380        390        400        410        420 
TDALAMGRAG EMVLRTWQTA DKMKKQRGPL AEEKNGSDNF RLKRYVSKYT INPAIAQGMA 

       430        440        450        460        470        480 
HEVGSIEEGK FADLVLWEPK FFGVKADRVI KGGIIAYAQI GDPSASIPTP QPVMGRRMYG 

       490        500        510        520        530        540 
TVGDLIHDTN ITFMSKSSIQ QGVPAKLGLK RRIGTVKNCR NIGKKDMKWN DVTTDIDINP 

       550        560 
ETYEVKVDGE VLTCEPVKEL PMAQRYFLF

« Hide

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References

[1]"Nucleotide sequence of three genes on a urease encoding DNA-fragment from Bacillus pasteurii."
Moersdorf G., Weinmann P., Kaltwasser H.
Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822.
[2]"Genetic organization and nucleotide sequence of the ure gene cluster in Bacillus pasteurii."
You J.-H., Kim J.-G., Song B.-H., Lee M.-H., Kim S.-D.
Mol. Cells 5:359-369(1995)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 497-569.
Strain: ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822.
[3]"Crystallization and preliminary high-resolution X-ray diffraction analysis of native and beta-mercaptoethanol-inhibited urease from Bacillus pasteurii."
Benini S., Ciurli S., Rypniewski W.R., Wilson K.S., Mangani S.
Acta Crystallogr. D 54:409-412(1998) [PubMed: 9761912] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH UREA; UREB; NICKEL IONS AND BETA-MERCAPTOETHANOL, CARBAMYLATION AT LYS-219.
[4]"A new proposal for urease mechanism based on the crystal structures of the native and inhibited enzyme from Bacillus pasteurii: why urea hydrolysis costs two nickels."
Benini S., Rypniewski W.R., Wilson K.S., Miletti S., Ciurli S., Mangani S.
Structure 7:205-216(1999) [PubMed: 10368287] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH UREA; UREB; NICKEL IONS AND DIAMIDOPHOSPHATE, CARBAMYLATION AT LYS-219.
[5]"The complex of Bacillus pasteurii urease with acetohydroxamate anion from X-ray data at 1.55 A resolution."
Benini S., Rypniewski W.R., Wilson K.S., Miletti S., Ciurli S., Mangani S.
J. Biol. Inorg. Chem. 5:110-118(2000) [PubMed: 10766443] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH UREA; UREB; NICKEL IONS AND ACETOHYDROXAMIC ACID, CARBAMYLATION AT LYS-219.
[6]"Structure-based rationalization of urease inhibition by phosphate: novel insights into the enzyme mechanism."
Benini S., Rypniewski W.R., Wilson K.S., Ciurli S., Mangani S.
J. Biol. Inorg. Chem. 6:778-790(2001) [PubMed: 11713685] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH UREA; UREB; NICKEL AND PHOSPHATE IONS, CARBAMYLATION AT LYS-219.
[7]"Molecular details of urease inhibition by boric acid: insights into the catalytic mechanism."
Benini S., Rypniewski W.R., Wilson K.S., Mangani S., Ciurli S.
J. Am. Chem. Soc. 126:3714-3715(2004) [PubMed: 15038715] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH UREA; UREB; NICKEL AND BORATE IONS, CARBAMYLATION AT LYS-219.

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Cross-references

Sequence databases

X78411 Genomic DNA. Translation: CAA55175.1.
U29368 Genomic DNA. Translation: AAA73986.1.
PIRS47104.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1IE7X-ray1.85C1-569[»]
1S3TX-ray2.10C1-569[»]
1UBPX-ray1.65C1-569[»]
2UBPX-ray2.00C1-569[»]
3UBPX-ray2.00C1-569[»]
4UBPX-ray1.55C1-569[»]
ModBaseSearch...

Protein family/group databases

MEROPSM38.982.

Enzyme and pathway databases

BRENDA3.5.1.5. 21619.

Family and domain databases

HAMAPMF_01953.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR011612. Urease_alpha_N.
IPR005848. Urease_asu.
IPR017951. Urease_asu_c.
IPR017952. Urease_asu_core.
IPR017950. Urease_asu_CS.
[Graphical view]
PfamPF01979. Amidohydro_1. 1 hit.
PF00449. Urease_alpha. 1 hit.
[Graphical view]
PRINTSPR01752. UREASE.
TIGRFAMsTIGR01792. urease_alph. 1 hit.
PROSITEPS01120. UREASE_1. 1 hit.
PS00145. UREASE_2. 1 hit.
PS51368. UREASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameURE1_BACPA
AccessionPrimary (citable) accession number: P41020
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 16, 2009
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents