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Reviewed, UniProtKB/Swiss-Prot P0C8R5 (AAXB_CHLTB)

Last modified June 16, 2009. Version 5. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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
Cleaved into the following 2 chains:
    1- Recommended name:
            Pyruvoyl-dependent arginine decarboxylase subunit beta
    2- Recommended name:
            Pyruvoyl-dependent arginine decarboxylase subunit alpha
Gene names
Name: aaxB
Ordered Locus Names: CTLon_0625
OrganismChlamydia trachomatis (strain L2b/UCH-1/proctitis) [Complete proteome] [HAMAP]
Taxonomic identifier471473 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia

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 AM884177 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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5252Pyruvoyl-dependent arginine decarboxylase subunit beta
PRO_0000364037
Chain53 – 195143Pyruvoyl-dependent arginine decarboxylase subunit alpha
PRO_0000364038

Sites

Site52 – 532Cleavage (non-hydrolytic) By similarity

Amino acid modifications

Modified residue531Pyruvic acid (Ser) By similarity

Sequences

Sequence LengthMass (Da)Tools
P0C8R5-1 [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: 18032721] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AM884177 Genomic DNA. No translation available.

3D structure databases

ModBaseSearch...

Genome annotation databases

GenomeReviewsGene locus CTLon_0625 in contig AM884177_GR.
KEGGctl:CTLon_0625.

Organism-specific databases

CMRSearch...

Family and domain databases

InterProIPR016105. Pyr-dep_his/arg-deCO2ase_sand.
IPR002724. Pyruvoyl-dep_arg_deCO2ase.
[Graphical view]
Gene3DG3DSA:3.50.20.10. Pyr-dep_his/arg-deCO2ase_sand. 1 hit.
PfamPF01862. PvlArgDC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAAXB_CHLTB
AccessionPrimary (citable) accession number: P0C8R5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: February 10, 2009
Last modified: June 16, 2009
This is version 5 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents