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Reviewed, UniProtKB/Swiss-Prot Q8FK60 (ALLB_ECOL6)

Last modified November 3, 2009. Version 41. 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

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 [Complete proteome] [HAMAP]
Taxonomic identifier217992 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length453 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

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

Cofactor

Binds 2 zinc ions per subunit By similarity.

Pathway

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

Subunit structure

Homotetramer By similarity.

Post-translational modification

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

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: 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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 453453Allantoinase HAMAP 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
Q8FK60-1 [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: 12471157] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases

AE014075 Genomic DNA. Translation: AAN79103.1.
RefSeqNP_752559.1.

3D structure databases

HSSPHSSP built from PDB template 1GKR based on UniProtKB P81006.
ModBaseSearch...

Genome annotation databases

GeneID1036012.
GenomeReviewsGene locus c0626 in contig AE014075_GR.
KEGGecc:c0626.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8FK60.
OMAFEAWGGI.

Enzyme and pathway databases

BRENDA3.5.2.5. 292881.

Family and domain databases

HAMAPMF_01645.
[Tree]
InterProIPR017593. Allantoinase.
IPR006680. Amidohydro_1.
[Graphical view]
PfamPF01979. Amidohydro_1. 2 hits.
[Graphical view]
ProDomPD000518. DHOase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
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: November 3, 2009
This is version 41 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)

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