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Q8EFU5

- SPEA_SHEON

UniProt

Q8EFU5 - SPEA_SHEON

Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Shewanella oneidensis (strain MR-1)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 1 (01 Mar 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

    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

    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:SO_1870
    OrganismiShewanella oneidensis (strain MR-1)
    Taxonomic identifieri211586 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
    ProteomesiUP000008186: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 637637Biosynthetic arginine decarboxylasePRO_0000149977Add
    BLAST

    Amino acid modifications

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

    Interactioni

    Protein-protein interaction databases

    STRINGi211586.SO_1870.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8EFU5.
    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.
    PhylomeDBiQ8EFU5.

    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.

    Q8EFU5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNDWSIEAAR AGYNVTHWSQ GFYGISDEGE VTVSPDPKNP DHKIGLNELA    50
    KDMVKAGVAL PVLVRFPQIL HHRVNSLCQA FDQAIQKYEY QADYLLVYPI 100
    KVNQQKTVVE EILASQASKE VPQLGLEAGS KPELMAVLAM AQKASSVIVC 150
    NGYKDNEYIR LALIGEKLGH KVYIVLEKLS ELKMVLAESK RLGVKPRLGL 200
    RARLAFQGKG KWQASGGEKS KFGLSAAQIL TVVDQLKQSD MLDSLQLLHF 250
    HLGSQIANIR DIRQGVSEAA RFYCELRELG ASINCFDVGG GLAVDYDGTR 300
    SQSNNSMNYG LSEYANNIVN VLTDICNEYE QPMPRIISES GRHLTAHHAV 350
    LITDVIGTEA YQVEDIQPPE EESPQLLHNM WQSWTELSGR ADQRALIEIY 400
    HDSQSDLQEA QSLFALGQLS LAERAWAEQA NLRVCHEVQG LLSTKNRYHR 450
    PIIDELNEKL ADKFFVNFSL FQSLPDAWGI DQVFPVLPLS GLDKAPERRA 500
    VMLDITCDSD GIVDQYVDGQ GIETTLPVPA WSAESPYLIG FFMVGAYQEI 550
    LGDMHNLFGD TNSAVVSIEE NGMTNIESVL AGDTVADVLR YVNLDAVDFM 600
    RTYEELVNQH IAEDERAQIL EELQVGLKGY TYLEDFS 637
    Length:637
    Mass (Da):71,004
    Last modified:March 1, 2003 - v1
    Checksum:i8EAE2CF59061F7B8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014299 Genomic DNA. Translation: AAN54922.1.
    RefSeqiNP_717478.1. NC_004347.2.
    WP_011071982.1. NC_004347.2.

    Genome annotation databases

    EnsemblBacteriaiAAN54922; AAN54922; SO_1870.
    GeneIDi1169637.
    KEGGison:SO_1870.
    PATRICi23523379. VBISheOne101494_1798.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014299 Genomic DNA. Translation: AAN54922.1 .
    RefSeqi NP_717478.1. NC_004347.2.
    WP_011071982.1. NC_004347.2.

    3D structure databases

    ProteinModelPortali Q8EFU5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 211586.SO_1870.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAN54922 ; AAN54922 ; SO_1870 .
    GeneIDi 1169637.
    KEGGi son:SO_1870.
    PATRICi 23523379. VBISheOne101494_1798.

    Phylogenomic databases

    eggNOGi COG1166.
    HOGENOMi HOG000029191.
    KOi K01585.
    OMAi IDHYVDG.
    OrthoDBi EOG676Z0R.
    PhylomeDBi Q8EFU5.

    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: MR-1.

    Entry informationi

    Entry nameiSPEA_SHEON
    AccessioniPrimary (citable) accession number: Q8EFU5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2004
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 75 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3