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Q8FK60 (ALLB_ECOL6) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 77. 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:ybbX
Ordered Locus Names:c0626
OrganismEscherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier199310 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

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_0000317678

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
Q8FK60 [UniParc].

Last modified March 1, 2003. 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

References

[1]"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli."
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014075 Genomic DNA. Translation: AAN79103.1.
RefSeqNP_752559.1. NC_004431.1.

3D structure databases

ProteinModelPortalQ8FK60.
SMRQ8FK60. Positions 2-451.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING199310.c0626.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN79103; AAN79103; c0626.
GeneID1036012.
KEGGecc:c0626.
PATRIC18279295. VBIEscCol75197_0592.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000219146.
KOK01466.
OMACSPWEGH.
OrthoDBEOG6KHFW6.

Enzyme and pathway databases

BioCycECOL199310:C0626-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_ECOL6
AccessionPrimary (citable) accession number: Q8FK60
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: March 1, 2003
Last modified: May 14, 2014
This is version 77 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