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Reviewed, UniProtKB/Swiss-Prot Q0TKD0 (ALLB_ECOL5)

Last modified February 9, 2010. Version 28. 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:
    Allantoinase
    EC=3.5.2.5
Alternative name(s):
    Allantoin-utilizing enzyme
Gene names
Name: allB
Ordered Locus Names: ECP_0572
OrganismEscherichia coli O6:K15:H31 (strain 536 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier362663 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length453 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

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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 MF_01645

Catalytic activity

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

Cofactor

Binds 2 zinc ions per subunit By similarity. HAMAP MF_01645

Pathway

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

Subunit structure

Homotetramer By similarity. HAMAP MF_01645

Post-translational modification

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

Sequence similarities

Belongs to the DHOase family. Allantoinase subfamily.

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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: HAMAP

purine base metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionallantoinase activity

Inferred from electronic annotation. Source: HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 453453Allantoinase HAMAP MF_01645
PRO_0000317679

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

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Sequences

Sequence LengthMass (Da)Tools
Q0TKD0-1 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: BB588074A32118B0

FASTA45349,588
        10         20         30         40         50         60 
MSFDLIIKNG TVILENEARV VDIAVKDGKI AAIGQDLGDA KDVMDASGLV VSPGMVDAHT 

        70         80         90        100        110        120 
HISEPGRSHW EGYETGTRAA AKGGITTMIE MPLNQLPATV DRASIELKFD AAKGKLTIDA 

       130        140        150        160        170        180 
AQLGGLVSYN IDRLHELDEV GVVGFKCFVA TCGDRGIDND FRDVNDWQFF KGAQKLGELG 

       190        200        210        220        230        240 
QPVLVHCENA LICDALGEEA KREGRVTAHD YVASRPVFTE VEAIRRVLYL AKVAGCRLHV 

       250        260        270        280        290        300 
CHVSSPEGVE EVTRARQEGQ DVTCESCPHY FVLDTDQFEE IGTLAKCSPP IRDLENQKGM 

       310        320        330        340        350        360 
WEKLFNGEID CLVSDHSPCP PEMKAGNIMK AWGGIAGLQS CMDVMFDEAV QKRGMSLPMF 

       370        380        390        400        410        420 
GKLMATNAAD IFGLQQKGRI APGKDADFVF IQPNSSYVLT NDDLEYRHKV SPYVGRTIGA 

       430        440        450 
RITKTILRGD VIYDIEQGFP VAPKGQFILK HQQ

« Hide

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References

[1]"Role of pathogenicity island-associated integrases in the genome plasticity of uropathogenic Escherichia coli strain 536."
Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.
Mol. Microbiol. 61:584-595(2006) [PubMed: 16879640] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000247 Genomic DNA. Translation: ABG68601.1.
RefSeqYP_668500.1.

3D structure databases

SMRQ0TKD0. Positions 3-449.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0TKD0.

Genome annotation databases

GeneID4189510.
GenomeReviewsGene locus ECP_0572 in contig CP000247_GR.
KEGGecp:ECP_0572.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0044.
HOGENOMHBG724623.
OMAHICHISS.
PhylomeDBQ0TKD0.

Enzyme and pathway databases

BioCycECOL362663:ECP_0572-MONOMER.

Family and domain databases

HAMAPMF_01645. Hydantoinase.
[Tree]
InterProIPR017593. Allantoinase.
IPR006680. Amidohydro_1.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
TIGRFAMsTIGR03178. allantoinase. 1 hit.
ProtoNetSearch...

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Entry information

Entry nameALLB_ECOL5
AccessionPrimary (citable) accession number: Q0TKD0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: September 5, 2006
Last modified: February 9, 2010
This is version 28 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