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Q5WBJ6 (ALLB_BACSK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Allantoinase

EC=3.5.2.5
Alternative name(s):
Allantoin-utilizing enzyme
Gene names
Name:allB
Synonyms:pucH
Ordered Locus Names:ABC3732
OrganismBacillus clausii (strain KSM-K16) [Complete proteome] [HAMAP]
Taxonomic identifier66692 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length448 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring By similarity. HAMAP-Rule MF_01645

Catalytic activity

(S)-allantoin + H2O = allantoate. HAMAP-Rule MF_01645

Cofactor

Binds 2 zinc ions per subunit By similarity. HAMAP-Rule MF_01645

Pathway

Nitrogen metabolism; (S)-allantoin degradation; allantoate from (S)-allantoin: step 1/1. HAMAP-Rule MF_01645

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_01645

Post-translational modification

Carbamylation allows a single lysine to coordinate two zinc ions By similarity. HAMAP-Rule MF_01645

Sequence similarities

Belongs to the DHOase family. Allantoinase subfamily.

Ontologies

Keywords
   Biological processPurine metabolism
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processallantoin catabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

purine nucleobase metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionallantoinase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

cobalt ion binding

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 448448Allantoinase HAMAP-Rule MF_01645
PRO_0000317669

Sites

Metal binding591Zinc 1 By similarity
Metal binding611Zinc 1 By similarity
Metal binding1461Zinc 1; via carbamate group By similarity
Metal binding1461Zinc 2; via carbamate group By similarity
Metal binding1851Zinc 2 By similarity
Metal binding2391Zinc 2 By similarity
Metal binding3121Zinc 1 By similarity

Amino acid modifications

Modified residue1461N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5WBJ6 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 903BD489E7C7ACF5

FASTA44848,711
        10         20         30         40         50         60 
MLDLCITGGR VVLPSGVEET DVGIQAGKIA RIGPINKKEA RCIMNANGQY VFPGAVDTHV 

        70         80         90        100        110        120 
HFSEPGRTEW EGFFTGSRSL AAGGTTTYVE MPLNALPATT NRANLQRKLE AAKGQNYVDY 

       130        140        150        160        170        180 
SFYGGLVPTN LHELADLSAS GVVAFKCFLS PCGSDIPGDF RNVDLNGLRA GMRLLAEKGQ 

       190        200        210        220        230        240 
LLCVHAEDPS MISQLEAKLL SPVGADAYVA SRPVEAEVKA VCDTLAAARE TGCRIHFVHI 

       250        260        270        280        290        300 
SSAAAIEAIE RAKEEGVDVT VESCPHYFLL SAEELAELGP LAKCQPPLRP KQEQAKLWAC 

       310        320        330        340        350        360 
LLDGQIDWLA SDHSPCTPDL KDGDFLTAWG GISGCQNNID IMFDAAVKRR GMPPEQLARL 

       370        380        390        400        410        420 
IATNPAKRMN LREKGEIAIG KDADFAFVDD RQSYTLTKEQ LYYKNKHSPY VGRTIGCKVR 

       430        440 
RVLLRGQTIY TEEKGIIGKP SGELLHIH 

« Hide

References

[1]"The complete genome sequence of the alkaliphilic Bacillus clausii KSM-K16."
Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., Kawai S., Ito S., Horikoshi K.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KSM-K16.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006627 Genomic DNA. Translation: BAD66264.1.
RefSeqYP_177225.1. NC_006582.1.

3D structure databases

ProteinModelPortalQ5WBJ6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING66692.ABC3732.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD66264; BAD66264; ABC3732.
GeneID3202800.
KEGGbcl:ABC3732.
PATRIC18927260. VBIBacCla58185_3978.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0044.
HOGENOMHOG000219146.
KOK01466.
OMACSPWEGH.
OrthoDBEOG6KHFW6.

Enzyme and pathway databases

BioCycBCLA66692:GHMP-3813-MONOMER.
UniPathwayUPA00395; UER00653.

Family and domain databases

Gene3D2.30.40.10. 1 hit.
HAMAPMF_01645. Hydantoinase.
InterProIPR017593. Allantoinase.
IPR013108. Amidohydro_3.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
PfamPF07969. Amidohydro_3. 1 hit.
[Graphical view]
SUPFAMSSF51338. SSF51338. 2 hits.
TIGRFAMsTIGR03178. allantoinase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameALLB_BACSK
AccessionPrimary (citable) accession number: Q5WBJ6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 23, 2004
Last modified: May 14, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways