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A8A477

- SPEB_ECOHS

UniProt

A8A477 - SPEB_ECOHS

Protein

Agmatinase

Gene

speB

Organism
Escherichia coli O9:H4 (strain HS)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 49 (01 Oct 2014)
      Sequence version 1 (23 Oct 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the formation of putrescine from agmatine.UniRule annotation

    Catalytic activityi

    Agmatine + H2O = putrescine + urea.UniRule annotation

    Cofactori

    Manganese.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi126 – 1261ManganeseUniRule annotation
    Metal bindingi149 – 1491ManganeseUniRule annotation
    Metal bindingi151 – 1511ManganeseUniRule annotation
    Metal bindingi153 – 1531ManganeseUniRule annotation
    Metal bindingi230 – 2301ManganeseUniRule annotation
    Metal bindingi232 – 2321ManganeseUniRule annotation

    GO - Molecular functioni

    1. agmatinase activity Source: UniProtKB-HAMAP
    2. manganese ion binding Source: InterPro

    GO - Biological processi

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

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Polyamine biosynthesis, Putrescine biosynthesis, Spermidine biosynthesis

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciECOL331112:GHHI-3086-MONOMER.
    UniPathwayiUPA00534; UER00287.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    AgmatinaseUniRule annotation (EC:3.5.3.11UniRule annotation)
    Alternative name(s):
    Agmatine ureohydrolaseUniRule annotation
    Short name:
    AUHUniRule annotation
    Gene namesi
    Name:speBUniRule annotation
    Ordered Locus Names:EcHS_A3095
    OrganismiEscherichia coli O9:H4 (strain HS)
    Taxonomic identifieri331112 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000001123: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 306306AgmatinasePRO_1000068495Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi331112.EcHS_A3095.

    Structurei

    3D structure databases

    ProteinModelPortaliA8A477.
    SMRiA8A477. Positions 11-304.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the arginase family. Agmatinase subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0010.
    HOGENOMiHOG000204320.
    KOiK01480.
    OMAiKPDYSLY.
    OrthoDBiEOG6R2GW5.

    Family and domain databases

    Gene3Di3.40.800.10. 1 hit.
    HAMAPiMF_01418. SpeB.
    InterProiIPR023694. Agmatinase.
    IPR005925. 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.

    A8A477-1 [UniParc]FASTAAdd to Basket

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    MSTLGHQYDN SLVSNAFGFL RLPMNFQPYD SDADWVITGV PFDMATSGRA    50
    GGRHGPAAIR QVSTNLAWEH NRFPWNFDMR ERLNVVDCGD LVYAFGDARE 100
    MSEKLQAHAE KLLAAGKRML SFGGDHFVTL PLLRAHAKHF GKMALVHFDA 150
    HTDTYANGCE FDHGTMFYTA PKEGLIDPNH SVQIGIRTEF DKDNGFTVLD 200
    ACQVNDRSVD DVIAQVKQIV GDMSVYLTFD IDCLDPAFAP GTGTPVIGGL 250
    TSDRAIKLVR GLKDLNIVGM DVVEVAPAYD QSEITALAAA TLALEMLYIQ 300
    AAKKGE 306
    Length:306
    Mass (Da):33,547
    Last modified:October 23, 2007 - v1
    Checksum:i8B20899D32873A8D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000802 Genomic DNA. Translation: ABV07331.1.
    RefSeqiWP_000105571.1. NC_009800.1.
    YP_001459714.1. NC_009800.1.

    Genome annotation databases

    EnsemblBacteriaiABV07331; ABV07331; EcHS_A3095.
    GeneIDi5593910.
    KEGGiecx:EcHS_A3095.
    PATRICi18316173. VBIEscCol77814_3026.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000802 Genomic DNA. Translation: ABV07331.1 .
    RefSeqi WP_000105571.1. NC_009800.1.
    YP_001459714.1. NC_009800.1.

    3D structure databases

    ProteinModelPortali A8A477.
    SMRi A8A477. Positions 11-304.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 331112.EcHS_A3095.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABV07331 ; ABV07331 ; EcHS_A3095 .
    GeneIDi 5593910.
    KEGGi ecx:EcHS_A3095.
    PATRICi 18316173. VBIEscCol77814_3026.

    Phylogenomic databases

    eggNOGi COG0010.
    HOGENOMi HOG000204320.
    KOi K01480.
    OMAi KPDYSLY.
    OrthoDBi EOG6R2GW5.

    Enzyme and pathway databases

    UniPathwayi UPA00534 ; UER00287 .
    BioCyci ECOL331112:GHHI-3086-MONOMER.

    Family and domain databases

    Gene3Di 3.40.800.10. 1 hit.
    HAMAPi MF_01418. SpeB.
    InterProi IPR023694. Agmatinase.
    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 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: HS.

    Entry informationi

    Entry nameiSPEB_ECOHS
    AccessioniPrimary (citable) accession number: A8A477
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 5, 2008
    Last sequence update: October 23, 2007
    Last modified: October 1, 2014
    This is version 49 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