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C4K6F4

- SPEA_HAMD5

UniProt

C4K6F4 - SPEA_HAMD5

Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Hamiltonella defensa subsp. Acyrthosiphon pisum (strain 5AT)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 36 (01 Oct 2014)
      Sequence version 1 (07 Jul 2009)
      Previous versions | rss
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    Functioni

    Catalyzes the biosynthesis of agmatine from arginine.UniRule annotation

    Catalytic activityi

    L-arginine = agmatine + CO2.UniRule annotation

    Cofactori

    Magnesium.UniRule annotation
    Pyridoxal phosphate.UniRule annotation

    Pathwayi

    GO - Molecular functioni

    1. arginine decarboxylase activity Source: UniProtKB-HAMAP
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. arginine catabolic process Source: InterPro
    2. putrescine biosynthetic process Source: UniProtKB-HAMAP
    3. spermidine biosynthetic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Decarboxylase, Lyase

    Keywords - Biological processi

    Polyamine biosynthesis, Putrescine biosynthesis, Spermidine biosynthesis

    Keywords - Ligandi

    Magnesium, Metal-binding, Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciHDEF572265:GJAB-1543-MONOMER.
    UniPathwayiUPA00186; UER00284.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Biosynthetic arginine decarboxylaseUniRule annotation (EC:4.1.1.19UniRule annotation)
    Short name:
    ADCUniRule annotation
    Gene namesi
    Name:speAUniRule annotation
    Ordered Locus Names:HDEF_1524
    OrganismiHamiltonella defensa subsp. Acyrthosiphon pisum (strain 5AT)
    Taxonomic identifieri572265 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeaphid secondary symbiontsCandidatus Hamiltonella
    ProteomesiUP000002334: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 633633Biosynthetic arginine decarboxylasePRO_1000215248Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei102 – 1021N6-(pyridoxal phosphate)lysineUniRule annotation

    Interactioni

    Protein-protein interaction databases

    STRINGi572265.HDEF_1524.

    Structurei

    3D structure databases

    ProteinModelPortaliC4K6F4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni282 – 29211Substrate-bindingUniRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1166.
    KOiK01585.
    OMAiIDHYVDG.
    OrthoDBiEOG676Z0R.

    Family and domain databases

    Gene3Di2.40.37.10. 2 hits.
    3.20.20.10. 1 hit.
    HAMAPiMF_01417. SpeA.
    InterProiIPR009006. Ala_racemase/Decarboxylase_C.
    IPR002985. Arg_decrbxlase.
    IPR022643. De-COase2_C.
    IPR022657. De-COase2_CS.
    IPR022644. De-COase2_N.
    IPR022653. De-COase2_pyr-phos_BS.
    IPR000183. Orn/DAP/Arg_de-COase.
    IPR029066. PLP-binding_barrel.
    [Graphical view]
    PfamiPF02784. Orn_Arg_deC_N. 1 hit.
    PF00278. Orn_DAP_Arg_deC. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001336. Arg_decrbxlase. 1 hit.
    PRINTSiPR01180. ARGDCRBXLASE.
    PR01179. ODADCRBXLASE.
    SUPFAMiSSF50621. SSF50621. 1 hit.
    SSF51419. SSF51419. 1 hit.
    TIGRFAMsiTIGR01273. speA. 1 hit.
    PROSITEiPS00878. ODR_DC_2_1. 1 hit.
    PS00879. ODR_DC_2_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    C4K6F4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNDRHAEKIR RAYNVAYWGN DYFYINDLGH ICVRPNPEVS QSSIDLAELL    50
    KEKEGKNPQP LPALFFFPQI LQHRLHAINK AFKSARDSFG YQGDYCLVYP 100
    IKVNQHRRVI ESLLKSGESL GLEAGSKAEM VAVLAYAGGT RSLIVCNGYK 150
    DREYIRLALM GEKLGYKVYL VIEKMSEIKM VLEEAKRLNV VPRLGVRARL 200
    ASEGSGKWQA SGGEKSKFGL SATQVLQLVE ILKSADCLSG LQLLHFHLGS 250
    QLSNIHDIAT GVRESARFYV ELHKLGVKIS CFDVGGGLGV DYEGTRSQSD 300
    CSVNYGLKEY ANNVIWGIGE ICNENHLPHP TVISESGRAL TAHHTVLISN 350
    VIGVERNEFS PPQAPEKHSP RALESLWYTW QEMQKPDHRH SLRECLHDSQ 400
    RDLQDVHTQY THGILDLKQR AWAEQLYLQI CHHIQKELDP SDRAHRTMID 450
    NLQERMADKL YVNFSLFQSL PDAWGINQLF PILPLEGLNQ RPERRAVLLD 500
    ITCDSDGIIE HYVDGDGVAN TLPIPPYDAE NPPILGFFMV GAYQEILGNM 550
    HNLFGDTAVV EVSLDEQEKI SVKIDNPGNT VSDMLKYVKL DPKALLAYFA 600
    QKIKKTDLNA QLQMAFLEEF EASLYGYTYL EHD 633
    Length:633
    Mass (Da):71,505
    Last modified:July 7, 2009 - v1
    Checksum:i444A0217E53529B2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001277 Genomic DNA. Translation: ACQ68147.1.
    RefSeqiYP_002924295.1. NC_012751.1.

    Genome annotation databases

    EnsemblBacteriaiACQ68147; ACQ68147; HDEF_1524.
    GeneIDi7951124.
    KEGGihde:HDEF_1524.
    PATRICi31974509. VBICanHam112931_1522.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001277 Genomic DNA. Translation: ACQ68147.1 .
    RefSeqi YP_002924295.1. NC_012751.1.

    3D structure databases

    ProteinModelPortali C4K6F4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 572265.HDEF_1524.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACQ68147 ; ACQ68147 ; HDEF_1524 .
    GeneIDi 7951124.
    KEGGi hde:HDEF_1524.
    PATRICi 31974509. VBICanHam112931_1522.

    Phylogenomic databases

    eggNOGi COG1166.
    KOi K01585.
    OMAi IDHYVDG.
    OrthoDBi EOG676Z0R.

    Enzyme and pathway databases

    UniPathwayi UPA00186 ; UER00284 .
    BioCyci HDEF572265:GJAB-1543-MONOMER.

    Family and domain databases

    Gene3Di 2.40.37.10. 2 hits.
    3.20.20.10. 1 hit.
    HAMAPi MF_01417. SpeA.
    InterProi IPR009006. Ala_racemase/Decarboxylase_C.
    IPR002985. Arg_decrbxlase.
    IPR022643. De-COase2_C.
    IPR022657. De-COase2_CS.
    IPR022644. De-COase2_N.
    IPR022653. De-COase2_pyr-phos_BS.
    IPR000183. Orn/DAP/Arg_de-COase.
    IPR029066. PLP-binding_barrel.
    [Graphical view ]
    Pfami PF02784. Orn_Arg_deC_N. 1 hit.
    PF00278. Orn_DAP_Arg_deC. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001336. Arg_decrbxlase. 1 hit.
    PRINTSi PR01180. ARGDCRBXLASE.
    PR01179. ODADCRBXLASE.
    SUPFAMi SSF50621. SSF50621. 1 hit.
    SSF51419. SSF51419. 1 hit.
    TIGRFAMsi TIGR01273. speA. 1 hit.
    PROSITEi PS00878. ODR_DC_2_1. 1 hit.
    PS00879. ODR_DC_2_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Hamiltonella defensa, genome evolution of protective bacterial endosymbiont from pathogenic ancestors."
      Degnan P.H., Yu Y., Sisneros N., Wing R.A., Moran N.A.
      Proc. Natl. Acad. Sci. U.S.A. 106:9063-9068(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 5AT.

    Entry informationi

    Entry nameiSPEA_HAMD5
    AccessioniPrimary (citable) accession number: C4K6F4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 22, 2009
    Last sequence update: July 7, 2009
    Last modified: October 1, 2014
    This is version 36 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3