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Q9RXR4

- SPEA_DEIRA

UniProt

Q9RXR4 - SPEA_DEIRA

Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      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

    BioCyciDRAD243230:GH46-249-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:DR_0243
    OrganismiDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
    Taxonomic identifieri243230 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus
    ProteomesiUP000002524: Chromosome I

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 662662Biosynthetic arginine decarboxylasePRO_0000149959Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei126 – 1261N6-(pyridoxal phosphate)lysineUniRule annotation

    Proteomic databases

    PRIDEiQ9RXR4.

    Interactioni

    Protein-protein interaction databases

    STRINGi243230.DR_0243.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9RXR4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni308 – 31811Substrate-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.
    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.

    Q9RXR4-1 [UniParc]FASTAAdd to Basket

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    MCPARLRTPR TASLPTHRRS AMTTANPLNT SFTSADAAEL YQVPNWSGGW    50
    FRVSDKGLME ATPAPGLHAS LRAIVDEIVD RGESLPVILR FPQVLAGRVK 100
    HLNEAFQAAI NEYNYSGHYQ GVFPIKVNQR RAVVETVAAA GYDYAHGLEA 150
    GSKAELALCL AQKMHPDALL CCNGFKDDGF IKLALWGRTL GKNVVITIEK 200
    FTELDRILKQ AKALGVKPAV GVRFKLHARG SGQWEESGGD QAKFGLNAYE 250
    LLRVVERLKE ENMLDSLVML HTHIGSQITD IRRVKVAVRE AAQTYAGLIA 300
    AGADLKYLNV GGGLGVDYDG SKTTFYASMN YTVKEYAADI VYTVQEVCKA 350
    REVPEPVIVS ESGRALTAHH AVLILPVVDV TGPTRNLEDQ ELTVPGEDSH 400
    QIVRDMYETL ENISMRNYRE SYNDAVGDKQ TLHNLFDLGY VTLEDRARGE 450
    ALFNAILRKI AKLIQGEKYV PDELEDLQKV LADKFICNFS LFQSLPDNWA 500
    IGALFPIVPL DRLNEQPTRQ ATLVDITCDS DGKVEKFIDL RDVKATLPLH 550
    EPGDRPYYLG AFLMGAYQDV LGSAHNLFGK VSEAHVTVRP GGRFNIDLFV 600
    RGQKARRMIE SMGYEEPMLR DAIEDQADAA IGRGTLTQEQ EHELLEDYGE 650
    ELLGYTYLEY ES 662
    Length:662
    Mass (Da):73,528
    Last modified:May 1, 2000 - v1
    Checksum:i88DDA5636BD83E6A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000513 Genomic DNA. Translation: AAF09826.1.
    PIRiB75544.
    RefSeqiNP_293967.1. NC_001263.1.
    WP_010886889.1. NC_001263.1.

    Genome annotation databases

    EnsemblBacteriaiAAF09826; AAF09826; DR_0243.
    GeneIDi1799241.
    KEGGidra:DR_0243.
    PATRICi21627969. VBIDeiRad64572_0407.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000513 Genomic DNA. Translation: AAF09826.1 .
    PIRi B75544.
    RefSeqi NP_293967.1. NC_001263.1.
    WP_010886889.1. NC_001263.1.

    3D structure databases

    ProteinModelPortali Q9RXR4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243230.DR_0243.

    Proteomic databases

    PRIDEi Q9RXR4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAF09826 ; AAF09826 ; DR_0243 .
    GeneIDi 1799241.
    KEGGi dra:DR_0243.
    PATRICi 21627969. VBIDeiRad64572_0407.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci DRAD243230:GH46-249-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.
    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: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.

    Entry informationi

    Entry nameiSPEA_DEIRA
    AccessioniPrimary (citable) accession number: Q9RXR4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2004
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 88 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