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P70999

- SPEB_BACSU

UniProt

P70999 - SPEB_BACSU

Protein

Agmatinase

Gene

speB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      Previous versions | rss
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    Functioni

    Catalyzes the formation of putrescine from agmatine.

    Catalytic activityi

    Agmatine + H2O = putrescine + urea.

    Cofactori

    Manganese.PROSITE-ProRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi112 – 1121ManganesePROSITE-ProRule annotation
    Metal bindingi135 – 1351ManganesePROSITE-ProRule annotation
    Metal bindingi137 – 1371ManganesePROSITE-ProRule annotation
    Metal bindingi139 – 1391ManganesePROSITE-ProRule annotation
    Metal bindingi216 – 2161ManganesePROSITE-ProRule annotation
    Metal bindingi218 – 2181ManganesePROSITE-ProRule annotation

    GO - Molecular functioni

    1. agmatinase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. putrescine biosynthetic process from arginine Source: UniProtKB-UniPathway
    2. spermidine biosynthetic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Polyamine biosynthesis, Putrescine biosynthesis, Spermidine biosynthesis

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU37490-MONOMER.
    MetaCyc:SPEBBACSU-MONOMER.
    UniPathwayiUPA00534; UER00287.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Agmatinase (EC:3.5.3.11)
    Alternative name(s):
    Agmatine ureohydrolase
    Short name:
    AUH
    Gene namesi
    Name:speB
    Synonyms:ywhG
    Ordered Locus Names:BSU37490
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU37490. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 290290AgmatinasePRO_0000173728Add
    BLAST

    Proteomic databases

    PaxDbiP70999.

    Interactioni

    Protein-protein interaction databases

    STRINGi224308.BSU37490.

    Structurei

    3D structure databases

    ProteinModelPortaliP70999.
    SMRiP70999. Positions 18-290.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the arginase family. Agmatinase subfamily.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0010.
    HOGENOMiHOG000204321.
    KOiK01480.
    OMAiKPDYSLY.
    OrthoDBiEOG6R2GW5.
    PhylomeDBiP70999.

    Family and domain databases

    Gene3Di3.40.800.10. 1 hit.
    InterProiIPR005925. Agmatinase-rel.
    IPR006035. Ureohydrolase.
    IPR023696. Ureohydrolase_domain.
    IPR020855. Ureohydrolase_Mn_BS.
    [Graphical view]
    PANTHERiPTHR11358. PTHR11358. 1 hit.
    PfamiPF00491. Arginase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036979. Arginase. 1 hit.
    TIGRFAMsiTIGR01230. agmatinase. 1 hit.
    PROSITEiPS01053. ARGINASE_1. 1 hit.
    PS51409. ARGINASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P70999-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRFDEAYSGK VFIASRPEWE EADAILYGMP MDWTVSYRPG SRFGPSRIRE    50
    VSIGLEEYSP YLDRDLADLN FFDAGDIPLP FGNPQRSLDM IEEYVDSILE 100
    KGKFPMGMGG EHLVSWPVIK AMYKKYPDLA IIHFDAHTDL RVDYEGEPLS 150
    HSTPIRKAAE LIGPHNVYSF GIRSGMKEEF EWAKENGMHI SKFEVLEPLK 200
    EVLPKLAGRP VYVTIDIDVL DPAHAPGTGT VDAGGITSKE LLASVHEIAR 250
    SEVNVKGADL VEVAPVYDHS EQTANTASKI IREMLLGFVK 290
    Length:290
    Mass (Da):32,417
    Last modified:February 1, 1997 - v1
    Checksum:iB14C4AAD1B1BC964
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z80360 Genomic DNA. Translation: CAB02517.1.
    AL009126 Genomic DNA. Translation: CAB15776.1.
    PIRiH70057.
    RefSeqiNP_391629.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB15776; CAB15776; BSU37490.
    GeneIDi937205.
    KEGGibsu:BSU37490.
    PATRICi18979534. VBIBacSub10457_3929.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z80360 Genomic DNA. Translation: CAB02517.1 .
    AL009126 Genomic DNA. Translation: CAB15776.1 .
    PIRi H70057.
    RefSeqi NP_391629.1. NC_000964.3.

    3D structure databases

    ProteinModelPortali P70999.
    SMRi P70999. Positions 18-290.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU37490.

    Proteomic databases

    PaxDbi P70999.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB15776 ; CAB15776 ; BSU37490 .
    GeneIDi 937205.
    KEGGi bsu:BSU37490.
    PATRICi 18979534. VBIBacSub10457_3929.

    Organism-specific databases

    GenoListi BSU37490. [Micado ]

    Phylogenomic databases

    eggNOGi COG0010.
    HOGENOMi HOG000204321.
    KOi K01480.
    OMAi KPDYSLY.
    OrthoDBi EOG6R2GW5.
    PhylomeDBi P70999.

    Enzyme and pathway databases

    UniPathwayi UPA00534 ; UER00287 .
    BioCyci BSUB:BSU37490-MONOMER.
    MetaCyc:SPEBBACSU-MONOMER.

    Family and domain databases

    Gene3Di 3.40.800.10. 1 hit.
    InterProi IPR005925. Agmatinase-rel.
    IPR006035. Ureohydrolase.
    IPR023696. Ureohydrolase_domain.
    IPR020855. Ureohydrolase_Mn_BS.
    [Graphical view ]
    PANTHERi PTHR11358. PTHR11358. 1 hit.
    Pfami PF00491. Arginase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036979. Arginase. 1 hit.
    TIGRFAMsi TIGR01230. agmatinase. 1 hit.
    PROSITEi PS01053. ARGINASE_1. 1 hit.
    PS51409. ARGINASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334 degrees)."
      Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V., Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G., Kunst F., Danchin A., Glaser P.
      Microbiology 143:3313-3328(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    2. "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.
    3. "Characterization of polyamine synthesis pathway in Bacillus subtilis 168."
      Sekowska A., Bertin P., Danchin A.
      Mol. Microbiol. 29:851-858(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF POLYAMINE PATHWAY.

    Entry informationi

    Entry nameiSPEB_BACSU
    AccessioniPrimary (citable) accession number: P70999
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2004
    Last sequence update: February 1, 1997
    Last modified: October 1, 2014
    This is version 89 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