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Protein

Pyruvoyl-dependent arginine decarboxylase AaxB

Gene

aaxB

Organism
Chlamydia pneumoniae (Chlamydophila pneumoniae)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Part of the AaxABC system, catalyzes the decarboxylation of L-arginine. The arginine uptake by the bacterium in the macrophage may be a virulence factor against the host innate immune response.1 Publication

Catalytic activityi

L-arginine = agmatine + CO2.

Cofactori

pyruvateNote: Binds 1 pyruvoyl group covalently per subunit.

Enzyme regulationi

Inhibited by argininamide.

Kineticsi

  1. KM=5.0 mM for L-arginine1 Publication

    pH dependencei

    Optimum pH is 3.4.1 Publication

    Temperature dependencei

    Thermostable. Retains 48% activity at 50 degrees Celsius, and 13% activity at 100 degrees Celsius.1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionDecarboxylase, Lyase
    Biological processVirulence
    LigandPyruvate

    Enzyme and pathway databases

    SABIO-RKQ9Z6M7

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyruvoyl-dependent arginine decarboxylase AaxB (EC:4.1.1.19)
    Short name:
    PvlArgDC
    Alternative name(s):
    Biodegradative arginine decarboxylase
    Cleaved into the following 2 chains:
    Gene namesi
    Name:aaxB
    Ordered Locus Names:CPn_1032, CP_0820, CPj1032, CpB1072
    OrganismiChlamydia pneumoniae (Chlamydophila pneumoniae)
    Taxonomic identifieri83558 [NCBI]
    Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
    Proteomesi
    • UP000000583 Componenti: Chromosome
    • UP000000801 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi52T → S: 70% loss of activity. Significantly impaired in ability to self-cleave. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00003640331 – 52Pyruvoyl-dependent arginine decarboxylase subunit betaAdd BLAST52
    ChainiPRO_000036403453 – 195Pyruvoyl-dependent arginine decarboxylase subunit alphaAdd BLAST143

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei53Pyruvic acid (Ser)1 Publication1

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sitei52 – 53Cleavage (non-hydrolytic)2

    Interactioni

    Subunit structurei

    Trimer of an alpha-beta dimer.

    Protein-protein interaction databases

    STRINGi182082.CpB1072

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z6M7
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4108PHJ Bacteria
    COG1945 LUCA
    HOGENOMiHOG000025218
    KOiK02626
    OMAiKKKFGFC
    OrthoDBiPOG091H1TON

    Family and domain databases

    Gene3Di3.50.20.10, 1 hit
    InterProiView protein in InterPro
    IPR016104 Pyr-dep_his/arg-deCO2ase
    IPR016105 Pyr-dep_his/arg-deCO2ase_sand
    IPR002724 Pyruvoyl-dep_arg_deCO2ase
    PANTHERiPTHR40438 PTHR40438, 1 hit
    PfamiView protein in Pfam
    PF01862 PvlArgDC, 1 hit
    ProDomiView protein in ProDom or Entries sharing at least one domain
    PD010449 Pyruvoyl-dep_arg_deCO2ase, 1 hit
    SFLDiSFLDG01170 Pyruvoyl-dependent_arginine_de, 1 hit
    SUPFAMiSSF56271 SSF56271, 1 hit

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9Z6M7-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAYGTRYPTL AFHTGGIGES DDGMPPQPFE TFCYDSALLQ AKIENFNIVP
    60 70 80 90 100
    YTSVLPKELF GNIVPVDTCV KSFKHGAVLE VIMAGRGAAL SDGTHAIATG
    110 120 130 140 150
    IGICWGKDKN GELIGGWAAE YVEFFPTWIN DEIAETHAKM WLKKSLQHEL
    160 170 180 190
    DLRSIAKHSE FQFFHNYINI KQKFGFCLTA LGFLNFENAE PAKVN
    Length:195
    Mass (Da):21,655
    Last modified:May 1, 1999 - v1
    Checksum:i1506883FB4854DA2
    GO

    Mass spectrometryi

    Molecular mass is 24283 Da from positions 1 - 195. Determined by MALDI. 1 Publication
    Molecular mass is 15875 Da from positions 53 - 195. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE001363 Genomic DNA Translation: AAD19169.1
    AE002161 Genomic DNA Translation: AAF38615.1
    BA000008 Genomic DNA Translation: BAA99239.1
    AE009440 Genomic DNA Translation: AAP99001.1
    PIRiB72006
    E86619
    RefSeqiNP_225226.1, NC_000922.1
    WP_010883665.1, NZ_LN847257.1

    Genome annotation databases

    EnsemblBacteriaiAAD19169; AAD19169; CPn_1032
    AAF38615; AAF38615; CP_0820
    AAP99001; AAP99001; CpB1072
    BAA99239; BAA99239; BAA99239
    GeneIDi895497
    KEGGicpa:CP_0820
    cpj:CPj1032
    cpn:CPn1032
    cpt:CpB1072
    PATRICifig|115713.3.peg.1130

    Similar proteinsi

    Entry informationi

    Entry nameiAAXB_CHLPN
    AccessioniPrimary (citable) accession number: Q9Z6M7
    Secondary accession number(s): Q7AHX1, Q7BWL3, Q7DE85
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 10, 2009
    Last sequence update: May 1, 1999
    Last modified: May 23, 2018
    This is version 104 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

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