Skip Header

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

Reviewed, UniProtKB/Swiss-Prot Q3M712 (URE1_ANAVT)

Last modified February 9, 2010. Version 37. 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: Ava_3618
OrganismAnabaena variabilis (strain ATCC 29413 / PCC 7937) [Complete proteome] [HAMAP]
Taxonomic identifier240292 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Nostocales › Nostocaceae › Anabaena

Hide | Top

Protein attributes

Sequence length568 AA.
Sequence statusComplete.
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. 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 By similarity. HAMAP MF_01953

Subcellular location

Cytoplasm By similarity HAMAP MF_01953.

Post-translational modification

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

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 – 568568Urease subunit alpha HAMAP MF_01953
PRO_0000239873

Regions

Domain131 – 568438Urease

Sites

Active site3221Proton donor By similarity
Metal binding1361Nickel 2 By similarity
Metal binding1381Nickel 2 By similarity
Metal binding2191Nickel 1; via carbamate group By similarity
Metal binding2191Nickel 2; via carbamate group By similarity
Metal binding2481Nickel 1 By similarity
Metal binding2741Nickel 1 By similarity
Metal binding3621Nickel 2 By similarity
Binding site2211Substrate By similarity

Amino acid modifications

Modified residue2191N6-carboxylysine By similarity

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q3M712-1 [UniParc].

Last modified October 25, 2005. Version 1.
Checksum: 32DBF3391914AC2A

FASTA56861,125
        10         20         30         40         50         60 
MPYRMSRQAY AETYGPTVGD RIRLADTELF IQVEQDFTTY GDEVKFGGGK VIRDGMGQSP 

        70         80         90        100        110        120 
IANADGAVDL VITNALILDW WGIVKADIGI KDGKIFKIGK AGNPYIQDHV DIIIGPGTEA 

       130        140        150        160        170        180 
LAGEGMILTA GGIDTHIHFI CPQQIEVAIA SGITTMIGGG TGPATGTNAT TCTPGPWNMY 

       190        200        210        220        230        240 
RMLQAADAFP MNLGFLGKGN ASQPQGLTEQ IFAGAIGLKL HEDWGTTPAT IDTCLSVADE 

       250        260        270        280        290        300 
YDVQVAIHTD TLNEAGFVED TIAAFKNRAI HTYHTEGAGG GHAPDIIKVC GQANVLPSST 

       310        320        330        340        350        360 
NPTRPYTVNT LDEHLDMLMV CHHLDPAIAE DVAFAESRIR RETIAAEDIL HDLGAFSMIA 

       370        380        390        400        410        420 
SDSQAMGRVG EVIIRTWQTS HKMKVQRGSL AGDGKADNLR AKRYVAKYTI NPAITHGISQ 

       430        440        450        460        470        480 
YVGSVEAGKL ADLCLWRPGF FGVKPEIVIK GGMIAWSQMG DANASIPTPQ PVHMRPMFGS 

       490        500        510        520        530        540 
FAGARNATSL TFVSQAALER DIPQQLGLRK SAVAVSGTRQ LTKQEMKLND ALPHIEVDPE 

       550        560 
TYEVRADGEL LTCEPATVLP MAQRYFLF

« Hide

Hide | Top

References

[1]"Complete sequence of Anabaena variabilis ATCC 29413."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Hide | Top

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000117 Genomic DNA. Translation: ABA23224.1.
RefSeqYP_324119.1.

3D structure databases

SMRQ3M712. Positions 5-568.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3M712.

Genome annotation databases

GeneID3679310.
GenomeReviewsGene locus Ava_3618 in contig CP000117_GR.
KEGGava:Ava_3618.
NMPDRfig|240292.3.peg.4595.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0804.
HOGENOMHBG357507.
OMASHIHFIC.

Enzyme and pathway databases

BioCycAVAR240292:AVA_3618-MONOMER.

Family and domain databases

HAMAPMF_01953. Urease_alpha.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR011059. Metal-dep_hydrolase_composite.
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...

Hide | Top

Entry information

Entry nameURE1_ANAVT
AccessionPrimary (citable) accession number: Q3M712
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: October 25, 2005
Last modified: February 9, 2010
This is version 37 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