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Q0TKD0

- ALLB_ECOL5

UniProt

Q0TKD0 - ALLB_ECOL5

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Protein
Allantoinase
Gene
allB, ECP_0572
Organism
Escherichia coli O6:K15:H31 (strain 536 / UPEC)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

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

Catalytic activityi

(S)-allantoin + H2O = allantoate.UniRule annotation

Cofactori

Binds 2 zinc ions per subunit By similarity.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi59 – 591Zinc 1 By similarity
Metal bindingi61 – 611Zinc 1 By similarity
Metal bindingi146 – 1461Zinc 1; via carbamate group By similarity
Metal bindingi146 – 1461Zinc 2; via carbamate group By similarity
Metal bindingi186 – 1861Zinc 2 By similarity
Metal bindingi242 – 2421Zinc 2 By similarity
Metal bindingi315 – 3151Zinc 1 By similarity

GO - Molecular functioni

  1. allantoinase activity Source: UniProtKB-HAMAP
  2. cobalt ion binding Source: InterPro
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. allantoin catabolic process Source: UniProtKB-HAMAP
  2. purine nucleobase metabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Purine metabolism

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciECOL362663:GIY5-573-MONOMER.
UniPathwayiUPA00395; UER00653.

Names & Taxonomyi

Protein namesi
Recommended name:
Allantoinase (EC:3.5.2.5)
Alternative name(s):
Allantoin-utilizing enzyme
Gene namesi
Name:allB
Ordered Locus Names:ECP_0572
OrganismiEscherichia coli O6:K15:H31 (strain 536 / UPEC)
Taxonomic identifieri362663 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000009182: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 453453AllantoinaseUniRule annotation
PRO_0000317679Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei146 – 1461N6-carboxylysine By similarity

Post-translational modificationi

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

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi362663.ECP_0572.

Structurei

3D structure databases

ProteinModelPortaliQ0TKD0.
SMRiQ0TKD0. Positions 2-451.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0044.
HOGENOMiHOG000219146.
KOiK01466.
OMAiCSPWEGH.
OrthoDBiEOG6KHFW6.

Family and domain databases

Gene3Di2.30.40.10. 1 hit.
HAMAPiMF_01645. Hydantoinase.
InterProiIPR017593. Allantoinase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
TIGRFAMsiTIGR03178. allantoinase. 1 hit.

Sequencei

Sequence statusi: Complete.

Q0TKD0-1 [UniParc]FASTAAdd to Basket

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MSFDLIIKNG TVILENEARV VDIAVKDGKI AAIGQDLGDA KDVMDASGLV    50
VSPGMVDAHT HISEPGRSHW EGYETGTRAA AKGGITTMIE MPLNQLPATV 100
DRASIELKFD AAKGKLTIDA AQLGGLVSYN IDRLHELDEV GVVGFKCFVA 150
TCGDRGIDND FRDVNDWQFF KGAQKLGELG QPVLVHCENA LICDALGEEA 200
KREGRVTAHD YVASRPVFTE VEAIRRVLYL AKVAGCRLHV CHVSSPEGVE 250
EVTRARQEGQ DVTCESCPHY FVLDTDQFEE IGTLAKCSPP IRDLENQKGM 300
WEKLFNGEID CLVSDHSPCP PEMKAGNIMK AWGGIAGLQS CMDVMFDEAV 350
QKRGMSLPMF GKLMATNAAD IFGLQQKGRI APGKDADFVF IQPNSSYVLT 400
NDDLEYRHKV SPYVGRTIGA RITKTILRGD VIYDIEQGFP VAPKGQFILK 450
HQQ 453
Length:453
Mass (Da):49,588
Last modified:September 5, 2006 - v1
Checksum:iBB588074A32118B0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000247 Genomic DNA. Translation: ABG68601.1.
RefSeqiYP_668500.1. NC_008253.1.

Genome annotation databases

EnsemblBacteriaiABG68601; ABG68601; ECP_0572.
GeneIDi4189510.
KEGGiecp:ECP_0572.
PATRICi18191803. VBIEscCol77757_0575.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000247 Genomic DNA. Translation: ABG68601.1 .
RefSeqi YP_668500.1. NC_008253.1.

3D structure databases

ProteinModelPortali Q0TKD0.
SMRi Q0TKD0. Positions 2-451.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 362663.ECP_0572.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABG68601 ; ABG68601 ; ECP_0572 .
GeneIDi 4189510.
KEGGi ecp:ECP_0572.
PATRICi 18191803. VBIEscCol77757_0575.

Phylogenomic databases

eggNOGi COG0044.
HOGENOMi HOG000219146.
KOi K01466.
OMAi CSPWEGH.
OrthoDBi EOG6KHFW6.

Enzyme and pathway databases

UniPathwayi UPA00395 ; UER00653 .
BioCyci ECOL362663:GIY5-573-MONOMER.

Family and domain databases

Gene3Di 2.30.40.10. 1 hit.
HAMAPi MF_01645. Hydantoinase.
InterProi IPR017593. Allantoinase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view ]
SUPFAMi SSF51338. SSF51338. 2 hits.
TIGRFAMsi TIGR03178. allantoinase. 1 hit.
ProtoNeti Search...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 536 / UPEC.

Entry informationi

Entry nameiALLB_ECOL5
AccessioniPrimary (citable) accession number: Q0TKD0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: September 5, 2006
Last modified: July 9, 2014
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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