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Q9CL60

- SPEA_PASMU

UniProt

Q9CL60 - SPEA_PASMU

Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Pasteurella multocida (strain Pm70)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      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

    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. spermidine biosynthetic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Decarboxylase, Lyase

    Keywords - Biological processi

    Polyamine biosynthesis, Spermidine biosynthesis

    Keywords - Ligandi

    Magnesium, Metal-binding, Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciPMUL272843:GC8W-1435-MONOMER.

    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:PM1382
    OrganismiPasteurella multocida (strain Pm70)
    Taxonomic identifieri272843 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaePasteurella
    ProteomesiUP000000809: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 644644Biosynthetic arginine decarboxylasePRO_0000149966Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei113 – 1131N6-(pyridoxal phosphate)lysineUniRule annotation

    Interactioni

    Protein-protein interaction databases

    STRINGi272843.PM1382.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9CL60.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni293 – 30311Substrate-bindingUniRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1166.
    HOGENOMiHOG000029191.
    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.

    Q9CL60-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEQVTLTSDG TSSVFAENTV REVCNINYWG MRYYNVDEKG DIFVCPDPDK    50
    PQNRVSLAAL AEKVQREQGA HLPTLFCFPQ IIQHRLRSIN QAFKRAREDF 100
    GYEGNYFLVY PIKVNQHRRI VESLISSGQP LGLEAGSKAE LMAVLAHAGI 150
    TQTVIVCNGY KDREYVRFAL MGEKLGHKVY LVIEKLSEIQ LVLEEAAKLN 200
    VKPRLGVRAR LASQGSGKWQ SSGGEKSKFG LSASQVLSLV QMLKEHECLD 250
    CLQLLHFHLG SQLGNIRDVA TGVRESARFY VELHKLGVNI QCFDVGGGLG 300
    VDYEGNRTQS DCSVNYGLNE YADTVVWGIG QACREHGLPH PTIITESGRG 350
    VTAHHAVLVS NVIGVERYKF ETLAAPAKDA PSVLHSMWET WVDIQSSREK 400
    RSLRSWIHES QFDLSDVHNQ YNVGLLNLEQ RAWAEQLYLN ICHEVGQLFN 450
    EKHRSHRTII DELQERFADK LYVNFSLFQS LPDAWGIDQL FPVCPISNLN 500
    QPVSRRAVLL DITCDSDGTI DHYIDGDGIT TTMPMPHYEE DNPPLLGFFM 550
    VGAYQEILGN MHNLFGDTST VDVLVHEQDK AYIVDYDEGN TVADMLEYVY 600
    LDPKKLLDRY REQIEHSNLP ASEAIQFLNE LEVGLNGYTY LEDE 644
    Length:644
    Mass (Da):72,707
    Last modified:June 1, 2001 - v1
    Checksum:iF6A7FEB0B8DE3D82
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004439 Genomic DNA. Translation: AAK03466.1.
    RefSeqiNP_246321.1. NC_002663.1.

    Genome annotation databases

    EnsemblBacteriaiAAK03466; AAK03466; PM1382.
    GeneIDi1244729.
    KEGGipmu:PM1382.
    PATRICi22872023. VBIPasMul88067_1394.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004439 Genomic DNA. Translation: AAK03466.1 .
    RefSeqi NP_246321.1. NC_002663.1.

    3D structure databases

    ProteinModelPortali Q9CL60.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272843.PM1382.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAK03466 ; AAK03466 ; PM1382 .
    GeneIDi 1244729.
    KEGGi pmu:PM1382.
    PATRICi 22872023. VBIPasMul88067_1394.

    Phylogenomic databases

    eggNOGi COG1166.
    HOGENOMi HOG000029191.
    KOi K01585.
    OMAi IDHYVDG.
    OrthoDBi EOG676Z0R.

    Enzyme and pathway databases

    BioCyci PMUL272843:GC8W-1435-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Pm70.

    Entry informationi

    Entry nameiSPEA_PASMU
    AccessioniPrimary (citable) accession number: Q9CL60
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2004
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 76 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3