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Q12LW6

- SPEA_SHEDO

UniProt

Q12LW6 - SPEA_SHEDO

Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 62 (01 Oct 2014)
      Sequence version 1 (22 Aug 2006)
      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. 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

    BioCyciSDEN318161:GHKQ-2356-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:Sden_2280
    OrganismiShewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013)
    Taxonomic identifieri318161 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
    ProteomesiUP000001982: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 636636Biosynthetic arginine decarboxylasePRO_1000024267Add
    BLAST

    Amino acid modifications

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

    Interactioni

    Protein-protein interaction databases

    STRINGi318161.Sden_2280.

    Structurei

    3D structure databases

    ProteinModelPortaliQ12LW6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni286 – 29611Substrate-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.
    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.
    SUPFAMiSSF51419. SSF51419. 1 hit.
    TIGRFAMsiTIGR01273. speA. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q12LW6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNDWTIEDAR AGYNVTHWSQ GFYGIGEAGE VTVSPDPLNP SNKVALDTLA    50
    QDLVQAGIAL PVLVRFPQIL HHRVESLCDA FNQAIQKYEY QNDYLLVYPI 100
    KVNQQKTVVE EILASQVSKE VPQLGLEAGS KPELMAVLAM AQKASSVIVC 150
    NGYKDKEYVR LALIGEKLGH KVYIVLEKMS ELKMVLEEAR ELGVTPRLGL 200
    RTRLAFQGKG KWQASGGEKS KFGLSAAQVL KVVDELKEAN MLESLQLLHF 250
    HLGSQIANIR DIRQGVSEAG RFYCELRQLG ASINCFDVGG GLAVDYDGTR 300
    SQSNNSMNYG LTEYANNIVN VLTDLCNEYE QPMPRIISES GRHLTAHHAV 350
    LITDVIGTEA YMPENIQAPA EDAPQLLHNM WQSWTEISGR HDQRAIIEIY 400
    HDSQSDIAEA HSLFAVGQLS LMDRAWAEQT NLRVCHEVKG LLSNNNRYHR 450
    PVIDELNEKL ADKLFVNFSL FQSLPDAWGI DQVFPVLPLT CLDKAPERRA 500
    VMLDITCDSD GIVDQYVDGQ GIETTLPVPA WDPANPYLIG FFMVGAYQEI 550
    LGDMHNLFGD TNSAVVFVED NGKARIESTL DGDTVADVLR YVNLDADEFM 600
    HTYEELVEQH IVEDERASIL EELQLGLKGY TYLEDF 636
    Length:636
    Mass (Da):71,065
    Last modified:August 22, 2006 - v1
    Checksum:i67F1E19B36DD55CA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000302 Genomic DNA. Translation: ABE55560.1.
    RefSeqiYP_563283.1. NC_007954.1.

    Genome annotation databases

    EnsemblBacteriaiABE55560; ABE55560; Sden_2280.
    GeneIDi4018772.
    KEGGisdn:Sden_2280.
    PATRICi23490479. VBISheDen79529_2399.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000302 Genomic DNA. Translation: ABE55560.1 .
    RefSeqi YP_563283.1. NC_007954.1.

    3D structure databases

    ProteinModelPortali Q12LW6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 318161.Sden_2280.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABE55560 ; ABE55560 ; Sden_2280 .
    GeneIDi 4018772.
    KEGGi sdn:Sden_2280.
    PATRICi 23490479. VBISheDen79529_2399.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00186 ; UER00284 .
    BioCyci SDEN318161:GHKQ-2356-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.
    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 SSF51419. SSF51419. 1 hit.
    TIGRFAMsi TIGR01273. speA. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: OS217 / ATCC BAA-1090 / DSM 15013.

    Entry informationi

    Entry nameiSPEA_SHEDO
    AccessioniPrimary (citable) accession number: Q12LW6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: August 22, 2006
    Last modified: October 1, 2014
    This is version 62 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