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B1LDE8

- SPEA_ECOSM

UniProt

B1LDE8 - SPEA_ECOSM

Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Escherichia coli (strain SMS-3-5 / SECEC)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 49 (01 Oct 2014)
      Sequence version 1 (29 Apr 2008)
      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

    BioCyciECOL439855:GHHB-3078-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:EcSMS35_3081
    OrganismiEscherichia coli (strain SMS-3-5 / SECEC)
    Taxonomic identifieri439855 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000007011: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 632632Biosynthetic arginine decarboxylasePRO_1000145593Add
    BLAST

    Amino acid modifications

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

    Interactioni

    Protein-protein interaction databases

    STRINGi439855.EcSMS35_3081.

    Structurei

    3D structure databases

    ProteinModelPortaliB1LDE8.
    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.
    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.

    B1LDE8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSQEASKML RTYNIAWWGN NYYDVNELGH ISVCPDPDVP EARVDLAQLV    50
    KTREAQGQRL PALFCFPQIL QHRLRSINAA FKRARESYGY NGDYFLVYPI 100
    KVNQHRRVIE SLIHSGEPLG LEAGSKAELM AVLAHAGMTR SVIVCNGYKD 150
    REYIRLALIG EKMGHKVYLV IEKMSEIAIV LDEAERLNVV PRLGVRARLA 200
    SQGSGKWQSS GGEKSKFGLA ATQVLQLVET LREAGRLDSL QLLHFHLGSQ 250
    MANIRDIATG VRESARFYVE LHKLGVNIQC FDVGGGLGVD YEGTRSQSDC 300
    SVNYGLNEYA NNIIWAIGDA CEENGLPHPT VITESGRAVT AHHTVLVSNI 350
    IGVERNEYTV PTAPAEDAPR ALQSMWETWQ EMHEPGTRRS LREWLHDSQM 400
    DLHDIHIGYS SGTFSLQERA WAEQLYLSMC HEVQKQLDPQ NRAHRPIIDE 450
    LQERMADKMY VNFSLFQSMP DAWGIDQLFP VLPLEGLDQV PERRAVLLDI 500
    TCDSDGAIDH YIDGDGIATT MPMPEYDPEN PPMLGFFMVG AYQEILGNMH 550
    NLFGDTEAVD VFVFPDGSVE VELSDEGDTV ADMLQYVQLD PKTLLTQFRD 600
    QVKKTDLDAE LQQQFLEEFE AGLYGYTYLE DE 632
    Length:632
    Mass (Da):71,181
    Last modified:April 29, 2008 - v1
    Checksum:iEE36CC59AF9D2569
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000970 Genomic DNA. Translation: ACB15562.1.
    RefSeqiYP_001745100.1. NC_010498.1.

    Genome annotation databases

    EnsemblBacteriaiACB15562; ACB15562; EcSMS35_3081.
    GeneIDi6142594.
    KEGGiecm:EcSMS35_3081.
    PATRICi18435078. VBIEscCol6161_3234.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000970 Genomic DNA. Translation: ACB15562.1 .
    RefSeqi YP_001745100.1. NC_010498.1.

    3D structure databases

    ProteinModelPortali B1LDE8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 439855.EcSMS35_3081.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACB15562 ; ACB15562 ; EcSMS35_3081 .
    GeneIDi 6142594.
    KEGGi ecm:EcSMS35_3081.
    PATRICi 18435078. VBIEscCol6161_3234.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00186 ; UER00284 .
    BioCyci ECOL439855:GHHB-3078-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. "Insights into the environmental resistance gene pool from the genome sequence of the multidrug-resistant environmental isolate Escherichia coli SMS-3-5."
      Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C., Ravel J., Stepanauskas R.
      J. Bacteriol. 190:6779-6794(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: SMS-3-5 / SECEC.

    Entry informationi

    Entry nameiSPEA_ECOSM
    AccessioniPrimary (citable) accession number: B1LDE8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 14, 2009
    Last sequence update: April 29, 2008
    Last modified: October 1, 2014
    This is version 49 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