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Reviewed, UniProtKB/Swiss-Prot Q8FQX2 (URE1_COREF)

Last modified November 3, 2009. Version 48. 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

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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
Ordered Locus Names: CE0995
OrganismCorynebacterium efficiens [Complete proteome] [HAMAP]
Taxonomic identifier152794 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

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Protein attributes

Sequence length571 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

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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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 571571Urease subunit alpha HAMAP MF_01953
PRO_0000234151

Regions

Domain133 – 571439Urease

Sites

Active site3241Proton donor By similarity
Metal binding1381Nickel 2 By similarity
Metal binding1401Nickel 2 By similarity
Metal binding2211Nickel 1; via carbamate group By similarity
Metal binding2211Nickel 2; via carbamate group By similarity
Metal binding2501Nickel 1 By similarity
Metal binding2761Nickel 1 By similarity
Metal binding3641Nickel 2 By similarity
Binding site2231Substrate By similarity

Amino acid modifications

Modified residue2211N6-carboxylysine By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q8FQX2-1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 55C06EF074E7B7F8

FASTA57160,969
        10         20         30         40         50         60 
MFSMSRKQHA SMYGPTTGDR LRLADTGLFA EIEEDLTIAG EEAVFGGGKV VRVGMGQNGH 

        70         80         90        100        110        120 
RTREEDPDIP DTVITNVIVL DWSGIYKADI GIRDGIITGI GHAGNPDTMD GGTIPIGVST 

       130        140        150        160        170        180 
DIIAGEGKVL TAGGIDTHIH FISPEQIEAA LVSGITTMIG GGTGPSESTK ATTITPGPWH 

       190        200        210        220        230        240 
IHQMLRSLDG FPMNIGLLGK GHATASAPLI DQIRAGAIGL KVHEDWGATP ATIDLSLSVA 

       250        260        270        280        290        300 
DEFDIQVAVH TDTLNEAGFV ESTREAIGGR VIHTFHTEGA GGGHAPDIIA LAGEPNVLPA 

       310        320        330        340        350        360 
STNPTLPYTV NTVEEHLDML MVCHHLNPDV PEDVAFADSR IRTETIAAED VLHDMGIFSI 

       370        380        390        400        410        420 
TSSDSQAMGR VGEVIIRTWQ VADSMKRQRG PLEGDTADSD NNRIKRYVAK YTINPALAQG 

       430        440        450        460        470        480 
ISHVVGSVET GKFADLVLWE PKFFGVKPFM ILKGGQVVNS IMGDAGASIP TPQPELYRPM 

       490        500        510        520        530        540 
FGSYGSATSS NSITFLPRVA IAAGIPEQLG LNRRIEECHG IRTLTKQSLK LNGETPSIHV 

       550        560        570 
DPETYEVRID GALITCEPAE KLPLAQRYFL F

« Hide

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References

[1]"Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
Genome Res. 13:1572-1579(2003) [PubMed: 12840036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

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Cross-references

Sequence databases

BA000035 Genomic DNA. Translation: BAC17805.1.
RefSeqNP_737605.1.

3D structure databases

HSSPHSSP built from PDB template 1EJW based on UniProtKB P18314.
ModBaseSearch...

Genome annotation databases

GeneID1031957.
GenomeReviewsGene locus CE0995 in contig BA000035_GR.
KEGGcef:CE0995.
NMPDRfig|196164.1.peg.995.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8FQX2.
OMASHIHFIC.

Enzyme and pathway databases

BioCycCEFF196164:CE0995-MON.
BRENDA3.5.1.5. 277326.

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_COREF
AccessionPrimary (citable) accession number: Q8FQX2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: March 1, 2003
Last modified: November 3, 2009
This is version 48 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

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