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Q8PFQ5

- SPEA_XANAC

UniProt

Q8PFQ5 - SPEA_XANAC

Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Xanthomonas axonopodis pv. citri (strain 306)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 2 (29 Mar 2004)
      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

    BioCyciXAXO190486:GH55-3923-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:XAC3923
    OrganismiXanthomonas axonopodis pv. citri (strain 306)
    Taxonomic identifieri190486 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas
    ProteomesiUP000000576: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 628628Biosynthetic arginine decarboxylasePRO_0000149987Add
    BLAST

    Amino acid modifications

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

    Interactioni

    Protein-protein interaction databases

    STRINGi190486.XAC3923.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8PFQ5.
    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.
    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.
    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.

    Q8PFQ5-1 [UniParc]FASTAAdd to Basket

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    MSDWSLDQAR KTYSIPHWAD GYFDVNAAGH VVVTPTADGP AVSLPEVVDA    50
    ARAAGAKLPL LVRFPDILGQ RLGKLQAAFA QAQSEWDYAG GYTAVYPIKV 100
    NQHRGVAGTL ASHHGEGFGL EAGSKPELMA VLALSRPGGL IVCNGYKDRE 150
    YIRLALIGRK LGLQTFIVIE KPSELTLVLE EARALDVKPG LGVRMRLASL 200
    GAGKWQNSGG DKAKFGLSPR QVLDLWKTLR DTEYADSLNL LHFHMGSQIS 250
    NVRDIANGMR EATRYFVELS RLGAKISHVD VGGGLGIDYE GTRSRSYCSI 300
    NYGLHSYASN IVQPLASACE EHGLTPPRIV TECGRAMTAH HAVLIANVSE 350
    VEQAPEGRVP DAHDDEPAAI RHLREIHDEL DVRPAVELFQ EAQHFHAEGL 400
    SAYALGQIDL THRARIDDLF YAIAHGVRAR LSFDEKSHRP VLDELNERLV 450
    DKYFVNFSVF ESIPDVWAID QVFPIVPIER LNEAPQRRGI IADMTCDSDG 500
    MVKTYVENES LDSSLPLHRL NAGESYRIGF FLVGAYQEIL GDIHNLFGDT 550
    DAVEVVVDRD GYRIAQQRRG DTTDVMLDYV GYQLDTLRAT YAERIAAAHL 600
    SPERAQELSA ALEAGLTGYT YLSDEPLG 628
    Length:628
    Mass (Da):69,091
    Last modified:March 29, 2004 - v2
    Checksum:iCF03AC36E3066C05
    GO

    Sequence cautioni

    The sequence AAM38760.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE008923 Genomic DNA. Translation: AAM38760.1. Different initiation.
    RefSeqiNP_644224.2. NC_003919.1.

    Genome annotation databases

    EnsemblBacteriaiAAM38760; AAM38760; XAC3923.
    GeneIDi1157994.
    KEGGixac:XAC3923.
    PATRICi24060012. VBIXanAxo33670_4051.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE008923 Genomic DNA. Translation: AAM38760.1 . Different initiation.
    RefSeqi NP_644224.2. NC_003919.1.

    3D structure databases

    ProteinModelPortali Q8PFQ5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 190486.XAC3923.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAM38760 ; AAM38760 ; XAC3923 .
    GeneIDi 1157994.
    KEGGi xac:XAC3923.
    PATRICi 24060012. VBIXanAxo33670_4051.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci XAXO190486:GH55-3923-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. "Comparison of the genomes of two Xanthomonas pathogens with differing host specificities."
      da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P.
      , Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.
      Nature 417:459-463(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 306.

    Entry informationi

    Entry nameiSPEA_XANAC
    AccessioniPrimary (citable) accession number: Q8PFQ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2004
    Last sequence update: March 29, 2004
    Last modified: October 1, 2014
    This is version 74 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3