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Reviewed, UniProtKB/Swiss-Prot A5UH45 (URE1_HAEIG)

Last modified November 3, 2009. Version 21. 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: CGSHiGG_05950
OrganismHaemophilus influenzae (strain PittGG) [Complete proteome] [HAMAP]
Taxonomic identifier374931 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

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Protein attributes

Sequence length572 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 – 572572Urease subunit alpha HAMAP MF_01953
PRO_1000070659

Regions

Domain136 – 572437Urease

Sites

Active site3271Proton donor By similarity
Metal binding1411Nickel 2 By similarity
Metal binding1431Nickel 2 By similarity
Metal binding2241Nickel 1; via carbamate group By similarity
Metal binding2241Nickel 2; via carbamate group By similarity
Metal binding2531Nickel 1 By similarity
Metal binding2791Nickel 1 By similarity
Metal binding3671Nickel 2 By similarity
Binding site2261Substrate By similarity

Amino acid modifications

Modified residue2241N6-carboxylysine By similarity

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Sequences

Sequence LengthMass (Da)Tools
A5UH45-1 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 663CAA9AC70713D7

FASTA57261,813
        10         20         30         40         50         60 
MALTISRAQY VATYGPTVGD KVRLGDTNLW ATIEQDLLTK GDECKFGGGK SVRDGMAQSG 

        70         80         90        100        110        120 
TATRDNPNVL DFVITNVMII DARLGIIKAD IGIRDGRIVG IGQAGNPDTM DNVTPNMIIG 

       130        140        150        160        170        180 
ASTEVHNGVH LIATAGGIDT HIHFICPQQA QHAIESGVTT LIGGGTGPAD GTHATTCTPG 

       190        200        210        220        230        240 
AWYMEHMFQA AEALPVNVGF FGKGNCSTLD PLREQIEAGA LGLKIHEDWG ATPAVIDSAL 

       250        260        270        280        290        300 
KVADEMDIQV AIHTDTLNES GFLEDTMKAI DGRVIHTFHT EGAGGGHAPD IIKAAMYSNV 

       310        320        330        340        350        360 
LPASTNPTRP FTKNTIDEHL DMLMVCHHLD KRVPEDVAFA DSRIRPETIA AEDILHDMGV 

       370        380        390        400        410        420 
FSIMSSDSQA MGRIGEVVIR TWQTADKMKM QRGELGNEGN DNFRIKRYIA KYTINPAIAH 

       430        440        450        460        470        480 
GIAEHIGSLE VGKIADIVLW KPMFFGVKPE VVIKKGFISY AKMGDPNASI PTPQPVFYRP 

       490        500        510        520        530        540 
MYGAQGLATA QTAVFFVSQA AEKADIRAKF GLHKETIAVK GCRNVGKKDL VHNDVTPNIT 

       550        560        570 
VDAERYEVRV DGELITCEPV DSVPLGQRYF LF

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References

[1]"Characterization and modeling of the Haemophilus influenzae core and supragenomes based on the complete genomic sequences of Rd and 12 clinical nontypeable strains."
Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C., Ehrlich G.D.
Genome Biol. 8:RESEARCH103.1-RESEARCH103.18(2007) [PubMed: 17550610] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

CP000672 Genomic DNA. Translation: ABR00101.1.
RefSeqYP_001292484.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA5UH45.

Genome annotation databases

GeneID5226503.
GenomeReviewsGene locus CGSHiGG_05950 in contig CP000672_GR.
KEGGhiq:CGSHiGG_05950.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMASHIHFIC.

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_HAEIG
AccessionPrimary (citable) accession number: A5UH45
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 10, 2007
Last modified: November 3, 2009
This is version 21 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