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P0C8R4 (AAXB_CHLT2) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 22. 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:CTL0627
OrganismChlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B) [Complete proteome] [HAMAP]
Taxonomic identifier471472 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia

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.

Sequence caution

The sequence AM884176 differs from that shown. Reason: Erroneous termination at position 128. Translated as Trp.

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_0000364035
Chain53 – 195143Pyruvoyl-dependent arginine decarboxylase subunit alpha
PRO_0000364036

Sites

Site52 – 532Cleavage (non-hydrolytic) By similarity

Amino acid modifications

Modified residue531Pyruvic acid (Ser) By similarity

Sequences

Sequence LengthMass (Da)Tools
P0C8R4 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 29C4CF9A309EC05A

FASTA19521,751
        10         20         30         40         50         60 
MPYGTRYPTL AFHTGGVGES DDGMPPQPFE TFCYDSALLQ AKIENFNIVP YTSVLPKELF 

        70         80         90        100        110        120 
GNILPVDQCT KFFKHGAVLE VIMAGRGATV TDGTQAIATG VGICWGKDKN GELIGGWAAE 

       130        140        150        160        170        180 
YVEFFPTWID DEIAESHAKM WLKKSLQHEL DLRSVSKHSE FQYFHNYINI RKKFGFCLTA 

       190 
LGFLNFENAA PAVIQ 

« Hide

References

[1]"Chlamydia trachomatis: genome sequence analysis of lymphogranuloma venereum isolates."
Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P., Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D., Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.
Genome Res. 18:161-171(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 434/Bu / ATCC VR-902B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM884176 Genomic DNA. No translation available.

3D structure databases

ProteinModelPortalP0C8R4.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

CMRSearch...

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_CHLT2
AccessionPrimary (citable) accession number: P0C8R4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: February 10, 2009
Last modified: October 16, 2013
This is version 22 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