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Q822F3 (AAXB_CHLCV) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 56. 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:CCA_00730
OrganismChlamydophila caviae (strain GPIC) [Complete proteome] [HAMAP]
Taxonomic identifier227941 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydophila

Protein attributes

Sequence length195 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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 By similarity.

Catalytic activity

L-arginine = agmatine + CO2.

Cofactor

Pyruvoyl group By similarity.

Subunit structure

Trimer of an alpha-beta dimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the pyruvoyl-dependent arginine decarboxylase family.

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_0000364039
Chain53 – 195143Pyruvoyl-dependent arginine decarboxylase subunit alpha
PRO_0000364040

Sites

Site52 – 532Cleavage (non-hydrolytic) By similarity

Amino acid modifications

Modified residue531Pyruvic acid (Ser) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q822F3 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: BD1D5CDC01D351C5

FASTA19521,775
        10         20         30         40         50         60 
MPYGTRYPTL AFHTGGIGES DDGMPPQPFE TFCYDSALLQ AKIENFNIVP YTSVLPKELF 

        70         80         90        100        110        120 
GNIVPVDQCI KFFKHGAVLE VIMAGRGAST SDGTHAIATG VGICWGQDKN GELIGGWAAE 

       130        140        150        160        170        180 
YVEFFPTWIN DEIAESHAKM WLKKSLQHEL DLRSVVKHSE FQYFHNYINI KQKYGFSLTA 

       190 
LGFLNFENAD PATIK 

« Hide

References

[1]"Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC): examining the role of niche-specific genes in the evolution of the Chlamydiaceae."
Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T., Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A., Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O., Salzberg S.L., Hsia R.-C., McClarty G. expand/collapse author list , Rank R.G., Bavoil P.M., Fraser C.M.
Nucleic Acids Res. 31:2134-2147(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GPIC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015925 Genomic DNA. Translation: AAP05471.1.
RefSeqNP_829593.1. NC_003361.3.

3D structure databases

ProteinModelPortalQ822F3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING227941.CCA00730.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP05471; AAP05471; CCA_00730.
GeneID1218415.
KEGGcca:CCA00730.
PATRIC20270583. VBIChlCav107360_0775.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1945.
OMAWAVEYVE.
OrthoDBEOG6Q5NT3.
ProtClustDBCLSK403032.

Enzyme and pathway databases

BioCycCCAV227941:GH8L-759-MONOMER.

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_CHLCV
AccessionPrimary (citable) accession number: Q822F3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: June 1, 2003
Last modified: November 13, 2013
This is version 56 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