Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q6FD83 (URE1_ACIAD)

Last modified November 3, 2009. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Hide | Top

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
Ordered Locus Names: ACIAD1091
OrganismAcinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]
Taxonomic identifier62977 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

Hide | Top

Protein attributes

Sequence length566 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

Hide | Top

General annotation (Comments)

Catalytic activity

Urea + H2O = CO2 + 2 NH3. HAMAP MF_01953

Cofactor

Binds 2 nickel ions per subunit By similarity.

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 By similarity.

Subcellular location

Cytoplasm By similarity.

Post-translational modification

Carbamylation allows a single lysine to coordinate two nickel ions By similarity.

Sequence similarities

Belongs to the urease family.

Contains 1 urease domain.

Hide | Top

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
Nickel
   Molecular functionHydrolase
   Technical termComplete proteome
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...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 566566Urease subunit alpha HAMAP MF_01953
PRO_0000234129

Regions

Domain128 – 566439Urease

Sites

Active site3191Proton donor By similarity
Metal binding1331Nickel 2 By similarity
Metal binding1351Nickel 2 By similarity
Metal binding2161Nickel 1; via carbamate group By similarity
Metal binding2161Nickel 2; via carbamate group By similarity
Metal binding2451Nickel 1 By similarity
Metal binding2711Nickel 1 By similarity
Metal binding3591Nickel 2 By similarity
Binding site2181Substrate By similarity

Amino acid modifications

Modified residue2161N6-carboxylysine By similarity

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q6FD83-1 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 75691EE2513D67CA

FASTA56661,192
        10         20         30         40         50         60 
MKMSRRAYAE MFGPTVGDRV RLADTELFIE VEQDLTTYGE EVKFGGGKVI RDGMGQSQLL 

        70         80         90        100        110        120 
ADEVADTVIT NALIVDWWGI VKADVGLKNG RIWKIGKAGN PDIQPDITIP LGAATEVIAG 

       130        140        150        160        170        180 
EGQILTAGGI DTHIHWICPQ QVETALMSGV TTMVGGGTGP AAGTSATTVT PGPWHIGTML 

       190        200        210        220        230        240 
QAIDDLPMNI GLLGKGNLSL PDPIREQIKA GVVGLKLHED WGSTPAAIDN CLSVADEFDV 

       250        260        270        280        290        300 
QVAIHTDTLN ESGFLEETLA AFKNRTIHTY HTEGAGGGHA PDILKAIGQA NVLPSSTNPT 

       310        320        330        340        350        360 
RPYTINTIDE HLDMLMVCHH LDPAIAEDVA FAESRIRRET IAAEDILQDL GAIAMMSSDS 

       370        380        390        400        410        420 
QAMGRVGEVI IRTWQTAHKM KVQRGALQGD ETSHDNSRVK RYIAKYTINP AITHGLSHEI 

       430        440        450        460        470        480 
GSVEEGKLAD LVLWKPAFFG VKPSMIIKGG MIAAAPMGDI NASIPTPQPV HYRPMFGAYP 

       490        500        510        520        530        540 
RGVHNTCITF LSQAAIDDGV AEKLKLKKLI SPCKNTRQIT KADMKHNTYC PVMDVHPETY 

       550        560 
EVRADGELLT CEPADVLPMA QRYFLF

« Hide

Hide | Top

References

[1]"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium."
Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.
Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Hide | Top

Cross-references

Sequence databases

CR543861 Genomic DNA. Translation: CAG67976.1.
RefSeqYP_045798.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ6FD83.

Genome annotation databases

GeneID2879202.
GenomeReviewsGene locus ACIAD1091 in contig CR543861_GR.
KEGGaci:ACIAD1091.
NMPDRfig|62977.3.peg.1236.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ6FD83.
OMASHIHFIC.

Enzyme and pathway databases

BioCycASP62977:ACIAD1091-MON.

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.
ProDomPD001248. Amidohydro_like. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01792. urease_alph. 1 hit.
PROSITEPS01120. UREASE_1. 1 hit.
PS00145. UREASE_2. 1 hit.
PS51368. UREASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry nameURE1_ACIAD
AccessionPrimary (citable) accession number: Q6FD83
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: July 19, 2004
Last modified: November 3, 2009
This is version 44 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)

Hide | Top

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

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