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A7ZIR8

- ALLB_ECO24

UniProt

A7ZIR8 - ALLB_ECO24

Protein

Allantoinase

Gene

allB

Organism
Escherichia coli O139:H28 (strain E24377A / ETEC)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 51 (01 Oct 2014)
      Sequence version 1 (23 Oct 2007)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

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

    Cofactori

    Binds 2 zinc ions per subunit.UniRule annotation

    Pathwayi

    Sites

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

    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

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Purine metabolism

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciECOL331111:GH7P-545-MONOMER.
    UniPathwayiUPA00395; UER00653.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    AllantoinaseUniRule annotation (EC:3.5.2.5UniRule annotation)
    Alternative name(s):
    Allantoin-utilizing enzymeUniRule annotation
    Gene namesi
    Name:allBUniRule annotation
    Ordered Locus Names:EcE24377A_0548
    OrganismiEscherichia coli O139:H28 (strain E24377A / ETEC)
    Taxonomic identifieri331111 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000001122: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 453453AllantoinasePRO_0000317676Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei146 – 1461N6-carboxylysineUniRule annotation

    Post-translational modificationi

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

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi331111.EcE24377A_0548.

    Structurei

    3D structure databases

    ProteinModelPortaliA7ZIR8.
    SMRiA7ZIR8. Positions 2-451.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the DHOase family. Allantoinase subfamily.UniRule annotation

    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.

    A7ZIR8-1 [UniParc]FASTAAdd to Basket

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    MSFDLIIKNG TVILENEARV VDIAVKGGKI AAIGQDLGDA KEVMDASGLV    50
    VSPGMVDAHT HISEPGRSHW EGYETGTRAA AKGGITTMIE MPLNQLPATV 100
    DRASIELKFD AAKGKLTIDA AQLGGLVSYN IDRLHELDEV GVVGFKCFVA 150
    TCGDRGIDND FRDVNDWQFF KGAQKLGELG QPVLVHCENA LICDALGEEA 200
    KREGRVTAHD YVASRPVFTE VEAIRRVLYL AKVAGCRLHV CHISSPEGVE 250
    EVTRARQEGQ DVTCESCPHY FVLDTDQFEE IGTLAKCSPP IRDLENQKGM 300
    WEKLFNGEID CLVSDHSPCP PEMKAGNIME AWGGIAGLQN CMDVMFDEAV 350
    QKRGMSLPMF GKLMATNAAD IFGLQQKGRI ALGKDADFVF IQPNSSYVLT 400
    NDDLEYRHKV SPYVGRTIGA RITKTILRGD VIYDIEQGFP VAPKGQFILK 450
    HQQ 453
    Length:453
    Mass (Da):49,602
    Last modified:October 23, 2007 - v1
    Checksum:i3EF2096AF5A022B6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000800 Genomic DNA. Translation: ABV17665.1.
    RefSeqiWP_000006885.1. NC_009801.1.
    YP_001461697.1. NC_009801.1.

    Genome annotation databases

    EnsemblBacteriaiABV17665; ABV17665; EcE24377A_0548.
    GeneIDi5586304.
    KEGGiecw:EcE24377A_0548.
    PATRICi18290352. VBIEscCol31211_0856.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000800 Genomic DNA. Translation: ABV17665.1 .
    RefSeqi WP_000006885.1. NC_009801.1.
    YP_001461697.1. NC_009801.1.

    3D structure databases

    ProteinModelPortali A7ZIR8.
    SMRi A7ZIR8. Positions 2-451.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 331111.EcE24377A_0548.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABV17665 ; ABV17665 ; EcE24377A_0548 .
    GeneIDi 5586304.
    KEGGi ecw:EcE24377A_0548.
    PATRICi 18290352. VBIEscCol31211_0856.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00395 ; UER00653 .
    BioCyci ECOL331111:GH7P-545-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. "The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
      Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
      J. Bacteriol. 190:6881-6893(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: E24377A / ETEC.

    Entry informationi

    Entry nameiALLB_ECO24
    AccessioniPrimary (citable) accession number: A7ZIR8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 5, 2008
    Last sequence update: October 23, 2007
    Last modified: October 1, 2014
    This is version 51 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