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B8G120

- ALLB_DESHD

UniProt

B8G120 - ALLB_DESHD

Protein

Allantoinase

Gene

allB

Organism
Desulfitobacterium hafniense (strain DCB-2 / DSM 10664)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 39 (01 Oct 2014)
      Sequence version 1 (03 Mar 2009)
      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 bindingi61 – 611Zinc 1UniRule annotation
    Metal bindingi63 – 631Zinc 1UniRule annotation
    Metal bindingi148 – 1481Zinc 1; via carbamate groupUniRule annotation
    Metal bindingi148 – 1481Zinc 2; via carbamate groupUniRule annotation
    Metal bindingi184 – 1841Zinc 2UniRule annotation
    Metal bindingi240 – 2401Zinc 2UniRule annotation
    Metal bindingi313 – 3131Zinc 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

    BioCyciDHAF272564:GCV8-1203-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:Dhaf_1177
    OrganismiDesulfitobacterium hafniense (strain DCB-2 / DSM 10664)
    Taxonomic identifieri272564 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesPeptococcaceaeDesulfitobacterium
    ProteomesiUP000007726: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 449449AllantoinasePRO_1000186916Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei148 – 1481N6-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

    STRINGi272564.Dhaf_1177.

    Structurei

    3D structure databases

    ProteinModelPortaliB8G120.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the DHOase family. Allantoinase subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0044.
    HOGENOMiHOG000219146.
    KOiK01466.
    OMAiRWMSTAP.
    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.

    B8G120-1 [UniParc]FASTAAdd to Basket

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    MSHYDLILRN GNVVCPDGVR KADIAVSDGK IVLIAEEIPG DAKEIIDAAG    50
    KHIFPGITDG HVHFNDPGRT EWETITTGSS ALAAGGGVAY FDMPLNCSPC 100
    TLDAVNFNNK LAVAQKDSLV DYGFWGGLTS ANLDKLDELA ECGVIGFKAF 150
    ACHSGIDEFP RMDDYTALVG MEKLAKLGLP LMVHCENAEI TKELTELSLA 200
    NNRTGVRDYF AARPPITEIE NVSRMITFAE ETGCKLIIAH ISTAKAVELV 250
    AQARARGVDV YCETIGHYLY LTGDDVERLG TVAKCSPPIR DGENQLQMWG 300
    RLFNDNIAFV SSDHSPCDPK LKNGEFMRVW GGISACQTTL QGLLTHAYHD 350
    RKFPLVKIAQ LTAQHVNEIF KIKDKGQIAL GYDADFALVD LDHEFTLQAE 400
    DLFYKHKVSP YVGDRFRGSV SQTILRGTTI YKDGKIVSQP IGKHLRPHQ 449
    Length:449
    Mass (Da):49,300
    Last modified:March 3, 2009 - v1
    Checksum:i1FBD355BCE3138D3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001336 Genomic DNA. Translation: ACL19235.1.
    RefSeqiYP_002457671.1. NC_011830.1.

    Genome annotation databases

    EnsemblBacteriaiACL19235; ACL19235; Dhaf_1177.
    GeneIDi7258147.
    KEGGidhd:Dhaf_1177.
    PATRICi21660051. VBIDesHaf15223_1226.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001336 Genomic DNA. Translation: ACL19235.1 .
    RefSeqi YP_002457671.1. NC_011830.1.

    3D structure databases

    ProteinModelPortali B8G120.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272564.Dhaf_1177.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACL19235 ; ACL19235 ; Dhaf_1177 .
    GeneIDi 7258147.
    KEGGi dhd:Dhaf_1177.
    PATRICi 21660051. VBIDesHaf15223_1226.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00395 ; UER00653 .
    BioCyci DHAF272564:GCV8-1203-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. "Genome sequence of Desulfitobacterium hafniense DCB-2, a Gram-positive anaerobe capable of dehalogenation and metal reduction."
      Kim S.H., Harzman C., Davis J.K., Hutcheson R., Broderick J.B., Marsh T.L., Tiedje J.M.
      BMC Microbiol. 12:21-21(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DCB-2 / DSM 10664.

    Entry informationi

    Entry nameiALLB_DESHD
    AccessioniPrimary (citable) accession number: B8G120
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: March 3, 2009
    Last modified: October 1, 2014
    This is version 39 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