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O32137

- ALLB_BACSU

UniProt

O32137 - ALLB_BACSU

Protein

Allantoinase

Gene

allB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      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.1 PublicationUniRule 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 bindingi60 – 601Zinc 1UniRule annotation
    Metal bindingi62 – 621Zinc 1UniRule annotation
    Metal bindingi147 – 1471Zinc 1; via carbamate groupUniRule annotation
    Metal bindingi147 – 1471Zinc 2; via carbamate groupUniRule annotation
    Metal bindingi183 – 1831Zinc 2UniRule annotation
    Metal bindingi239 – 2391Zinc 2UniRule annotation
    Metal bindingi312 – 3121Zinc 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

    BioCyciBSUB:BSU32410-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
    Synonyms:pucHUniRule annotation, yunH
    Ordered Locus Names:BSU32410
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU32410. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 446446AllantoinasePRO_0000165940Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei147 – 1471N6-carboxylysineUniRule annotation

    Post-translational modificationi

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

    Proteomic databases

    PaxDbiO32137.

    Expressioni

    Inductioni

    Expression is very low in excess nitrogen (glutamate plus ammonia) and is induced during limiting-nitrogen conditions (glutamate). Expression is further induced when allantoin or allantoate are added during limiting-nitrogen conditions.1 Publication

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi224308.BSU32410.

    Structurei

    3D structure databases

    ProteinModelPortaliO32137.
    SMRiO32137. Positions 2-432.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the DHOase family. Allantoinase subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0044.
    HOGENOMiHOG000219146.
    KOiK01466.
    OMAiRWMSTAP.
    OrthoDBiEOG6KHFW6.
    PhylomeDBiO32137.

    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.

    O32137-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAYDMVIKGA KAVTPDGVIE ADIVVQNGVI AEIGSDIEAS GTEIIQADGK    50
    YVFPGVIDCH VHFNEPGRED WEGFETGSQM MAAGGCTTYF DMPLNCIPST 100
    VTAEHLLAKA ELGRQKSAVD FALWGGLVPG HIEDIRPMAE AGAIGFKAFL 150
    SKSGTDEFRS VDERTLLKGM AEIAAAGKIL ALHAESDAIT SYLQMVLANK 200
    GKVDADAYAA SRPEEAEVEA VYRTIQYAKV TGCPVHFVHI STAKAVRLIR 250
    EAKQEGLDVS VETCPHYVLF SHDDLRQRGS VAKCAPPLRS RQSKETLIET 300
    LIAGDIDMVS SDHSPCRPSL KREDNMFLSW GGISGGQFTL LGMLELALEH 350
    QIPFETIAEW TAAAPAKRFG LQKKGRLEAG CDADFVLVSM EPYTVTRESM 400
    FAKHKKSIYE GHTFPCSISA TYSKGRCVYN DGEKVTEIDG ALVVPS 446
    Length:446
    Mass (Da):48,331
    Last modified:January 1, 1998 - v1
    Checksum:i48515B6414A5C234
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL009126 Genomic DNA. Translation: CAB15231.1.
    PIRiC70016.
    RefSeqiNP_391121.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB15231; CAB15231; BSU32410.
    GeneIDi936662.
    KEGGibsu:BSU32410.
    PATRICi18978454. VBIBacSub10457_3390.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL009126 Genomic DNA. Translation: CAB15231.1 .
    PIRi C70016.
    RefSeqi NP_391121.1. NC_000964.3.

    3D structure databases

    ProteinModelPortali O32137.
    SMRi O32137. Positions 2-432.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU32410.

    Proteomic databases

    PaxDbi O32137.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB15231 ; CAB15231 ; BSU32410 .
    GeneIDi 936662.
    KEGGi bsu:BSU32410.
    PATRICi 18978454. VBIBacSub10457_3390.

    Organism-specific databases

    GenoListi BSU32410. [Micado ]

    Phylogenomic databases

    eggNOGi COG0044.
    HOGENOMi HOG000219146.
    KOi K01466.
    OMAi RWMSTAP.
    OrthoDBi EOG6KHFW6.
    PhylomeDBi O32137.

    Enzyme and pathway databases

    UniPathwayi UPA00395 ; UER00653 .
    BioCyci BSUB:BSU32410-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 complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    2. "Functional analysis of 14 genes that constitute the purine catabolic pathway in Bacillus subtilis and evidence for a novel regulon controlled by the PucR transcription activator."
      Schultz A.C., Nygaard P., Saxild H.H.
      J. Bacteriol. 183:3293-3302(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
      Strain: 168.

    Entry informationi

    Entry nameiALLB_BACSU
    AccessioniPrimary (citable) accession number: O32137
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 106 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, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3