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Q57K30

- SPEA_SALCH

UniProt

Q57K30 - SPEA_SALCH

Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Salmonella choleraesuis (strain SC-B67)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 59 (01 Oct 2014)
      Sequence version 1 (10 May 2005)
      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

    BioCyciSENT321314:GJCS-3160-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:SCH_3026
    OrganismiSalmonella choleraesuis (strain SC-B67)
    Taxonomic identifieri321314 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
    ProteomesiUP000000538: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 632632Biosynthetic arginine decarboxylasePRO_1000024263Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei101 – 1011N6-(pyridoxal phosphate)lysineUniRule annotation

    Proteomic databases

    PaxDbiQ57K30.
    PRIDEiQ57K30.

    Interactioni

    Protein-protein interaction databases

    STRINGi321314.SC3026.

    Structurei

    3D structure databases

    ProteinModelPortaliQ57K30.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni281 – 29111Substrate-bindingUniRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1166.
    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.

    Q57K30-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSQEASKML RTYNIAWWGN NYYDVNELGH ISVCPDPDVP EARVDLAKLV    50
    KAREAQGQRL PALFCFPQIL QHRLRSINAA FKRARESYGY NGDYFLVYPI 100
    KVNQHRRVIE SLIHSGEPLG LEAGSKAELM AVLAHAGMTR SVIVCNGYKD 150
    REYIRLALIG EKMGHKVYLV IEKMSEIAIV LEEAERLNVV PRLGVRARLA 200
    SQGSGKWQSS GGEKSKFGLA ATQVLQLVET LRDAGRLDSL QLLHFHLGSQ 250
    MANIRDIATG VRESARFYVE LHKLGVNIQC FDVGGGLGVD YEGTRSQSDC 300
    SVNYGLNEYA NNIIWAIGDA CEEHGLPHPT VITESGRAVT AHHTVLVSNI 350
    IGVERNEYTD PTAPAEDAPR ALQNLWETWQ EMHKPGTRRS LREWLHDSQM 400
    DLHDIHIGYS SGAFSLQERA WAEQLYLSMC HEVQKQLDPQ NRAHRPIIDE 450
    LQERMADKMY VNFSLFQSMP DAWGIDQLFP VLPLEGLDQV PERRAVLLDI 500
    TCDSDGAIDH YIDGDGIATT MPMPEYDPEN PPMLGFFMVG AYQEILGNMH 550
    NLFGDTEAVD VFVFPDGSVE VELSDEGDTV ADMLQYVQLD PKTLLTHFRD 600
    QVKQTDLDDA LQQQFLEEFE AGLYGYTYLE DE 632
    Length:632
    Mass (Da):71,163
    Last modified:May 10, 2005 - v1
    Checksum:i98BB424D2BC97370
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017220 Genomic DNA. Translation: AAX66932.1.
    RefSeqiYP_218013.1. NC_006905.1.

    Genome annotation databases

    EnsemblBacteriaiAAX66932; AAX66932; SCH_3026.
    PATRICi32327205. VBISalEnt136302_3560.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017220 Genomic DNA. Translation: AAX66932.1 .
    RefSeqi YP_218013.1. NC_006905.1.

    3D structure databases

    ProteinModelPortali Q57K30.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 321314.SC3026.

    Proteomic databases

    PaxDbi Q57K30.
    PRIDEi Q57K30.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAX66932 ; AAX66932 ; SCH_3026 .
    PATRICi 32327205. VBISalEnt136302_3560.

    Phylogenomic databases

    eggNOGi COG1166.
    OMAi IDHYVDG.
    OrthoDBi EOG676Z0R.

    Enzyme and pathway databases

    UniPathwayi UPA00186 ; UER00284 .
    BioCyci SENT321314:GJCS-3160-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. "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly invasive and resistant zoonotic pathogen."
      Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S., Lee Y.-S.
      Nucleic Acids Res. 33:1690-1698(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: SC-B67.

    Entry informationi

    Entry nameiSPEA_SALCH
    AccessioniPrimary (citable) accession number: Q57K30
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: May 10, 2005
    Last modified: October 1, 2014
    This is version 59 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

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3