Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9Z6M7

- AAXB_CHLPN

UniProt

Q9Z6M7 - AAXB_CHLPN

Protein

Pyruvoyl-dependent arginine decarboxylase AaxB

Gene

aaxB

Organism
Chlamydia pneumoniae (Chlamydophila pneumoniae)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Pyruvoyl group.

    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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei52 – 532Cleavage (non-hydrolytic)

    GO - Molecular functioni

    1. arginine decarboxylase activity Source: UniProtKB-EC

    GO - Biological processi

    1. arginine catabolic process Source: InterPro
    2. pathogenesis Source: UniProtKB-KW

    Keywords - Molecular functioni

    Decarboxylase, Lyase

    Keywords - Biological processi

    Virulence

    Keywords - Ligandi

    Pyruvate

    Enzyme and pathway databases

    BioCyciCPNE115711:GI7B-846-MONOMER.
    CPNE115713:GHEY-1077-MONOMER.
    CPNE138677:GH8N-1067-MONOMER.
    CPNE182082:GH4N-1108-MONOMER.
    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
    ProteomesiUP000000424: Chromosome, UP000000583: Chromosome, UP000000801: Chromosome, UP000000802: Chromosome

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi52 – 521T → S: 70% loss of activity. Significantly impaired in ability to self-cleave. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 5252Pyruvoyl-dependent arginine decarboxylase subunit betaPRO_0000364033Add
    BLAST
    Chaini53 – 195143Pyruvoyl-dependent arginine decarboxylase subunit alphaPRO_0000364034Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei53 – 531Pyruvic acid (Ser)

    Interactioni

    Subunit structurei

    Trimer of an alpha-beta dimer.

    Protein-protein interaction databases

    STRINGi115713.CPn1032.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z6M7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1945.
    HOGENOMiHOG000025218.
    OMAiWAVEYVE.
    OrthoDBiEOG6Q5NT3.

    Family and domain databases

    Gene3Di3.50.20.10. 1 hit.
    InterProiIPR016104. Pyr-dep_his/arg-deCO2ase.
    IPR016105. Pyr-dep_his/arg-deCO2ase_sand.
    IPR002724. Pyruvoyl-dep_arg_deCO2ase.
    [Graphical view]
    PfamiPF01862. PvlArgDC. 1 hit.
    [Graphical view]
    ProDomiPD010449. Pyruvoyl-dep_arg_deCO2ase. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    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

    MAYGTRYPTL AFHTGGIGES DDGMPPQPFE TFCYDSALLQ AKIENFNIVP    50
    YTSVLPKELF GNIVPVDTCV KSFKHGAVLE VIMAGRGAAL SDGTHAIATG 100
    IGICWGKDKN GELIGGWAAE YVEFFPTWIN DEIAETHAKM WLKKSLQHEL 150
    DLRSIAKHSE FQFFHNYINI KQKFGFCLTA LGFLNFENAE PAKVN 195
    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:
    EMBL
    GenBank
    DDBJ
    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.
    NP_301087.1. NC_002491.1.
    NP_445359.1. NC_002179.2.
    NP_877344.1. NC_005043.1.

    Genome annotation databases

    EnsemblBacteriaiAAD19169; AAD19169; CPn_1032.
    AAF38615; AAF38615; CP_0820.
    AAP99001; AAP99001; CpB1072.
    BAA99239; BAA99239; BAA99239.
    GeneIDi1467751.
    895497.
    919806.
    962776.
    KEGGicpa:CP0820.
    cpj:CPj1032.
    cpn:CPn1032.
    cpt:CpB1072.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi B72006.
    E86619.
    RefSeqi NP_225226.1. NC_000922.1.
    NP_301087.1. NC_002491.1.
    NP_445359.1. NC_002179.2.
    NP_877344.1. NC_005043.1.

    3D structure databases

    ProteinModelPortali Q9Z6M7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 115713.CPn1032.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAD19169 ; AAD19169 ; CPn_1032 .
    AAF38615 ; AAF38615 ; CP_0820 .
    AAP99001 ; AAP99001 ; CpB1072 .
    BAA99239 ; BAA99239 ; BAA99239 .
    GeneIDi 1467751.
    895497.
    919806.
    962776.
    KEGGi cpa:CP0820.
    cpj:CPj1032.
    cpn:CPn1032.
    cpt:CpB1072.

    Phylogenomic databases

    eggNOGi COG1945.
    HOGENOMi HOG000025218.
    OMAi WAVEYVE.
    OrthoDBi EOG6Q5NT3.

    Enzyme and pathway databases

    BioCyci CPNE115711:GI7B-846-MONOMER.
    CPNE115713:GHEY-1077-MONOMER.
    CPNE138677:GH8N-1067-MONOMER.
    CPNE182082:GH4N-1108-MONOMER.
    SABIO-RK Q9Z6M7.

    Family and domain databases

    Gene3Di 3.50.20.10. 1 hit.
    InterProi IPR016104. Pyr-dep_his/arg-deCO2ase.
    IPR016105. Pyr-dep_his/arg-deCO2ase_sand.
    IPR002724. Pyruvoyl-dep_arg_deCO2ase.
    [Graphical view ]
    Pfami PF01862. PvlArgDC. 1 hit.
    [Graphical view ]
    ProDomi PD010449. Pyruvoyl-dep_arg_deCO2ase. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF56271. SSF56271. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CWL029.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: AR39.
    3. "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from Japan and CWL029 from USA."
      Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K., Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.
      Nucleic Acids Res. 28:2311-2314(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: J138.
    4. "The genome sequence of Chlamydia pneumoniae TW183 and comparison with other Chlamydia strains based on whole genome sequence analysis."
      Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P., Schneider S., Pohl T., Essig A., Marre R., Melchers K.
      Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: TW-183.
    5. "Characterization of an acid-dependent arginine decarboxylase enzyme from Chlamydophila pneumoniae."
      Giles T.N., Graham D.E.
      J. Bacteriol. 189:7376-7383(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY, MUTAGENESIS OF THR-52.
      Strain: Kajaani 6.
    6. "Outer and inner membrane proteins compose an arginine-agmatine exchange system in Chlamydophila pneumoniae."
      Smith C.B., Graham D.E.
      J. Bacteriol. 190:7431-7440(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS PYRUVOYL-DEPENDENT ARGININE DECARBOXYLASE.
      Strain: Kajaani 6.

    Entry informationi

    Entry nameiAAXB_CHLPN
    AccessioniPrimary (citable) accession number: Q9Z6M7
    Secondary accession number(s): Q7AHX1, Q7BWL3, Q7DE85
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 10, 2009
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 83 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3