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B5BD11 (ALLB_SALPK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 39. 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
Ordered Locus Names:SSPA2045
OrganismSalmonella paratyphi A (strain AKU_12601) [Complete proteome] [HAMAP]
Taxonomic identifier554290 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length453 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 – 453453Allantoinase HAMAP-Rule MF_01645
PRO_1000186932

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 binding1861Zinc 2 By similarity
Metal binding2421Zinc 2 By similarity
Metal binding3151Zinc 1 By similarity

Amino acid modifications

Modified residue1461N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B5BD11 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 223BFADF6257891E

FASTA45349,887
        10         20         30         40         50         60 
MSFDLIIKNG TVILENEARV IDIAVQGGKI AAIGENLGEA KNVLDATGLI VSPGMVDAHT 

        70         80         90        100        110        120 
HISEPGRTHW EGYETGTRAA AKGGITTMIE MPLNQLPATV DRETIELKFD AAKGKLTIDA 

       130        140        150        160        170        180 
AQLGGLVSYN LDRLHELDEV GVVGFKCFVA TCGDRGIDND FRDVNDWQFY KGAQKLGEMD 

       190        200        210        220        230        240 
QTVLVHCENA LICDELGEEA KREGRVTAHD YVASRPVFTE VEAIRRVLYL AKAAGCRLHV 

       250        260        270        280        290        300 
CHISSPEGVE EVTRARQEGQ DVTCESCPHY FVLDTDQFEE IGTLAKCSPP IRDQENQKGM 

       310        320        330        340        350        360 
WEKLFNGEID CLVSDHSPCP PEMKAGNIMQ AWGGIAGLQN CMDVMFDEAV QKRGMSLPMF 

       370        380        390        400        410        420 
GKLMATNAAD IFGLKHKGRI APGKDADLVF IQPDSSYVLK NEDLEYRHKV SPYVGRTIGA 

       430        440        450 
RITKTILRGD VIYDIEHGFP VPPKGQFILK HQQ 

« Hide

References

[1]"Pseudogene accumulation in the evolutionary histories of Salmonella enterica serovars Paratyphi A and Typhi."
Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., Bhutta Z.A., Quail M.A., Norbertczak H., Walker D., Simmonds M., White B., Bason N., Mungall K., Dougan G., Parkhill J.
BMC Genomics 10:36-36(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AKU_12601.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM200053 Genomic DNA. Translation: CAR60253.1.
RefSeqYP_002142882.1. NC_011147.1.

3D structure databases

ProteinModelPortalB5BD11.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING554290.SSPA2045.

Proteomic databases

PRIDEB5BD11.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAR60253; CAR60253; SSPA2045.
PATRIC32344257. VBISalEnt134303_2345.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0044.
HOGENOMHOG000219146.
OMAHAEMIPP.
OrthoDBEOG6KHFW6.
ProtClustDBPRK08044.

Enzyme and pathway databases

BioCycSENT554290:GJDA-2192-MONOMER.
UniPathwayUPA00395; UER00653.

Family and domain databases

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

Entry information

Entry nameALLB_SALPK
AccessionPrimary (citable) accession number: B5BD11
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: September 23, 2008
Last modified: April 16, 2014
This is version 39 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