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Q9Z6M7 (AAXB_CHLPN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pyruvoyl-dependent arginine decarboxylase AaxB

Short name=PvlArgDC
EC=4.1.1.19
Alternative name(s):
Biodegradative arginine decarboxylase
Gene names
Name:aaxB
Ordered Locus Names:CPn_1032, CP_0820, CPj1032, CpB1072
OrganismChlamydia pneumoniae (Chlamydophila pneumoniae) [Complete proteome] [HAMAP]
Taxonomic identifier83558 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia

Protein attributes

Sequence length195 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6

Catalytic activity

L-arginine = agmatine + CO2.

Cofactor

Pyruvoyl group.

Enzyme regulation

Inhibited by argininamide.

Subunit structure

Trimer of an alpha-beta dimer.

Subcellular location

Cytoplasm Probable.

Sequence similarities

Belongs to the pyruvoyl-dependent arginine decarboxylase family.

Biophysicochemical properties

Kinetic parameters:

KM=5.0 mM for L-arginine Ref.5

pH dependence:

Optimum pH is 3.4.

Temperature dependence:

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

Mass spectrometry

Molecular mass is 24283 Da from positions 1 - 195. Determined by MALDI. Ref.5

Molecular mass is 15875 Da from positions 53 - 195. Determined by MALDI. Ref.5

Ontologies

Keywords
   Biological processVirulence
   Cellular componentCytoplasm
   LigandPyruvate
   Molecular functionDecarboxylase
Lyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processarginine catabolic process

Inferred from electronic annotation. Source: InterPro

pathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionarginine decarboxylase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5252Pyruvoyl-dependent arginine decarboxylase subunit beta
PRO_0000364033
Chain53 – 195143Pyruvoyl-dependent arginine decarboxylase subunit alpha
PRO_0000364034

Sites

Site52 – 532Cleavage (non-hydrolytic)

Amino acid modifications

Modified residue531Pyruvic acid (Ser)

Experimental info

Mutagenesis521T → S: 70% loss of activity. Significantly impaired in ability to self-cleave. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9Z6M7 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 1506883FB4854DA2

FASTA19521,655
        10         20         30         40         50         60 
MAYGTRYPTL AFHTGGIGES DDGMPPQPFE TFCYDSALLQ AKIENFNIVP YTSVLPKELF 

        70         80         90        100        110        120 
GNIVPVDTCV KSFKHGAVLE VIMAGRGAAL SDGTHAIATG IGICWGKDKN GELIGGWAAE 

       130        140        150        160        170        180 
YVEFFPTWIN DEIAETHAKM WLKKSLQHEL DLRSIAKHSE FQFFHNYINI KQKFGFCLTA 

       190 
LGFLNFENAE PAKVN 

« Hide

References

« Hide 'large scale' references
[1]"Comparative genomes of Chlamydia pneumoniae and C. trachomatis."
Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W., Olinger L., Grimwood J., Davis R.W., Stephens R.S.
Nat. Genet. 21:385-389(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CWL029.
[2]"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39."
Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L. expand/collapse author list , Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.
Nucleic Acids Res. 28:1397-1406(2000) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE001363 Genomic DNA. Translation: AAD19169.1.
AE002161 Genomic DNA. Translation: AAF38615.1.
BA000008 Genomic DNA. Translation: BAA99239.1.
AE009440 Genomic DNA. Translation: AAP99001.1.
PIRB72006.
E86619.
RefSeqNP_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

ProteinModelPortalQ9Z6M7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING115713.CPn1032.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD19169; AAD19169; CPn_1032.
AAF38615; AAF38615; CP_0820.
AAP99001; AAP99001; CpB1072.
BAA99239; BAA99239; BAA99239.
GeneID1467751.
895497.
919806.
962776.
KEGGcpa:CP0820.
cpj:CPj1032.
cpn:CPn1032.
cpt:CpB1072.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1945.
HOGENOMHOG000025218.
OMAWAVEYVE.
OrthoDBEOG6Q5NT3.

Enzyme and pathway databases

BioCycCPNE115711:GI7B-846-MONOMER.
CPNE115713:GHEY-1077-MONOMER.
CPNE138677:GH8N-1067-MONOMER.
CPNE182082:GH4N-1108-MONOMER.
SABIO-RKQ9Z6M7.

Family and domain databases

Gene3D3.50.20.10. 1 hit.
InterProIPR016104. Pyr-dep_his/arg-deCO2ase.
IPR016105. Pyr-dep_his/arg-deCO2ase_sand.
IPR002724. Pyruvoyl-dep_arg_deCO2ase.
[Graphical view]
PfamPF01862. PvlArgDC. 1 hit.
[Graphical view]
ProDomPD010449. Pyruvoyl-dep_arg_deCO2ase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF56271. SSF56271. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAAXB_CHLPN
AccessionPrimary (citable) accession number: Q9Z6M7
Secondary accession number(s): Q7AHX1, Q7BWL3, Q7DE85
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: May 1, 1999
Last modified: May 14, 2014
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families