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Q7NU27

- SPEA_CHRVO

UniProt

Q7NU27 - SPEA_CHRVO

Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (15 Dec 2003)
      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

    BioCyciCVIO243365:GHUD-2935-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:CV_2876
    OrganismiChromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
    Taxonomic identifieri243365 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesChromobacteriaceaeChromobacterium
    ProteomesiUP000001424: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 626626Biosynthetic arginine decarboxylasePRO_0000149958Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei99 – 991N6-(pyridoxal phosphate)lysineUniRule annotation

    Interactioni

    Protein-protein interaction databases

    STRINGi243365.CV_2876.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7NU27.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni279 – 28911Substrate-bindingUniRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1166.
    HOGENOMiHOG000029191.
    KOiK01585.
    OMAiDSEDMVE.
    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.
    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.
    PROSITEiPS00879. ODR_DC_2_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q7NU27-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAWSVADSRS LYGIRHWGAG YFDVGDSGNI VVRPNVRQRK EIDLYRLVRD    50
    LGGKGLDLPL LVRFPDILQD RVTRLCGAFD KAIAEQGYGN RYTAIYPIKV 100
    NQQEAVVKSI IATQDVSIGL EAGSKPELMA VLALAPKGCT IVCNGYKDRE 150
    FIRLALIGER LGHQVFIVIE KESEVDLVIE ESRKLEVRPN IGLRVRLSSL 200
    ASSKWSDTGG EKGKFGLSAG QLISATDKLI AAGLGDCVRL MHFHMGSQIA 250
    NIADYRLGFR EAIRYFAELR ALGLPVDHVD VGGGLGVDYD GTHSRNDSSI 300
    NYDMAEYAHV IVSMLSEFCA ENGIPHPRIL SESGRAMTAH HAVLLMNVTD 350
    VERLPDTVAP IDKAEELSLP LRKLVELANL NDEELVTEIY YRASHCVSEV 400
    SEMYAEGRLS LQEKALAEDL HATLCRRLHN QLQASQRSQR QVYDELTDRL 450
    ADKYFCNFSV FQSLPDTWAI DQVLPIMPVH RLAEQPTRRA VLQDLTCDSD 500
    GKLKQYVDQQ SIESSMSVHE VKQGDEYLIA VFLVGAYQEI LGDMHNLFGD 550
    TDSVNVYVRE GGELEISGIE EHDTIEDMLR YVHLSPEDLL NRYEAKTREC 600
    DLNPEERSLY FAEFCRGLKQ SSYLAV 626
    Length:626
    Mass (Da):70,119
    Last modified:December 15, 2003 - v1
    Checksum:i98A2CC60BACFB3F3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016825 Genomic DNA. Translation: AAQ60544.1.
    RefSeqiNP_902546.1. NC_005085.1.
    WP_011136423.1. NC_005085.1.

    Genome annotation databases

    EnsemblBacteriaiAAQ60544; AAQ60544; CV_2876.
    GeneIDi2548774.
    KEGGicvi:CV_2876.
    PATRICi21440494. VBIChrVio67196_2799.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016825 Genomic DNA. Translation: AAQ60544.1 .
    RefSeqi NP_902546.1. NC_005085.1.
    WP_011136423.1. NC_005085.1.

    3D structure databases

    ProteinModelPortali Q7NU27.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243365.CV_2876.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAQ60544 ; AAQ60544 ; CV_2876 .
    GeneIDi 2548774.
    KEGGi cvi:CV_2876.
    PATRICi 21440494. VBIChrVio67196_2799.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00186 ; UER00284 .
    BioCyci CVIO243365:GHUD-2935-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.
    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 PS00879. ODR_DC_2_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
      Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A.
      , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
      Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757.

    Entry informationi

    Entry nameiSPEA_CHRVO
    AccessioniPrimary (citable) accession number: Q7NU27
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2004
    Last sequence update: December 15, 2003
    Last modified: October 1, 2014
    This is version 81 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