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Q9HUX1

- SPEA_PSEAE

UniProt

Q9HUX1 - SPEA_PSEAE

Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      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: CACAO
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. arginine catabolic process Source: InterPro
    2. putrescine biosynthetic process from arginine Source: PseudoCAP
    3. 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

    BioCyciMetaCyc:MONOMER-12.

    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:PA4839
    OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
    Taxonomic identifieri208964 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    ProteomesiUP000002438: Chromosome

    Organism-specific databases

    PseudoCAPiPA4839.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 636636Biosynthetic arginine decarboxylasePRO_0000149971Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei110 – 1101N6-(pyridoxal phosphate)lysineUniRule annotation

    Interactioni

    Protein-protein interaction databases

    STRINGi208964.PA4839.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9HUX1.
    SMRiQ9HUX1. Positions 20-635.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni290 – 30011Substrate-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.
    PhylomeDBiQ9HUX1.

    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.

    Q9HUX1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAARRTRKDD GSNWTVADSR GVYGIRHWGA GYFAINDGGN VEVRPQGADS    50
    TPIDLYELVG QLREAGLSLP LLVRFPDILQ DRVRKLTGAF DANIERLEYQ 100
    SRYTALYPIK VNQQEAVVEN IIATENVSIG LEAGSKPELM AVLALAPKGG 150
    TIVCNGYKDR EFIKLALMGQ KLGHNVFIVI EKESEVQLVI EEAANVGVQP 200
    QVGLRVRLSS LASSKWADTG GEKAKFGLSA AQLLSVVERF RQAGLDQGVR 250
    LLHFHMGSQI ANLADYQHGF KEAIRYYGEL RALGLPVDHI DVGGGLGVDY 300
    DGTHSRNASS INYDIDDYAG VVVGMLKEFC DAQGLPHPHI FSESGRALTA 350
    HHAVLITQVT DVERHNDDVP KIVDLDEQPE IVRWLAELLG PTDAEMVTET 400
    YWRATHYIGD AAAQYADGKI SLAQKALAEQ CYFAICRRLH NQLKARQRSH 450
    RQVLDELNDK LADKYICNFS VFQSLPDTWA IGQVLPILPL HRLGEEPDRR 500
    AVLQDLTCDS DGKITQYVDE QSIETSLPVH EVKEGEDYLI GVFLVGAYQE 550
    ILGDMHNLFG DTDSVNVYQR ADGGIYHAGI ETHDTIEDML RYVHLSPEEL 600
    MTLYRDKVAG AKLTARERNQ YLDALRLGLT RSAYLS 636
    Length:636
    Mass (Da):70,668
    Last modified:March 1, 2001 - v1
    Checksum:iE7274FD432E0D187
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004091 Genomic DNA. Translation: AAG08224.1.
    PIRiH83040.
    RefSeqiNP_253526.1. NC_002516.2.

    Genome annotation databases

    EnsemblBacteriaiAAG08224; AAG08224; PA4839.
    GeneIDi879594.
    KEGGipae:PA4839.
    PATRICi19844477. VBIPseAer58763_5070.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004091 Genomic DNA. Translation: AAG08224.1 .
    PIRi H83040.
    RefSeqi NP_253526.1. NC_002516.2.

    3D structure databases

    ProteinModelPortali Q9HUX1.
    SMRi Q9HUX1. Positions 20-635.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 208964.PA4839.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAG08224 ; AAG08224 ; PA4839 .
    GeneIDi 879594.
    KEGGi pae:PA4839.
    PATRICi 19844477. VBIPseAer58763_5070.

    Organism-specific databases

    PseudoCAPi PA4839.

    Phylogenomic databases

    eggNOGi COG1166.
    HOGENOMi HOG000029191.
    KOi K01585.
    OMAi IDHYVDG.
    OrthoDBi EOG676Z0R.
    PhylomeDBi Q9HUX1.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-12.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

    Entry informationi

    Entry nameiSPEA_PSEAE
    AccessioniPrimary (citable) accession number: Q9HUX1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2004
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 79 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