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Reviewed, UniProtKB/Swiss-Prot Q5L5E7 (AAXB_CHLAB)

Last modified January 19, 2010. Version 23. 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: CAB697
OrganismChlamydophila abortus [Complete proteome] [HAMAP]
Taxonomic identifier83555 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydophila

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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5252Pyruvoyl-dependent arginine decarboxylase subunit beta
PRO_0000364043
Chain53 – 195143Pyruvoyl-dependent arginine decarboxylase subunit alpha
PRO_0000364044

Sites

Site52 – 532Cleavage (non-hydrolytic) By similarity

Amino acid modifications

Modified residue531Pyruvic acid (Ser) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5L5E7-1 [UniParc].

Last modified June 21, 2005. Version 1.
Checksum: A81BEBE617A50B90

FASTA19521,831
        10         20         30         40         50         60 
MPYGTRYPTL AFHTGGVGES DDGMPPQPFE TFCYDSALLQ AKIENFNIVP YTSVLPKELF 

        70         80         90        100        110        120 
GNIVPVDQCV KFFKHGAVLE VIMAGRGAST VEGTHAITTG VGICWGQDKN GELIGGWAAE 

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

       190 
LGFLNFENAD PVTIK 

« Hide

References

[1]"The Chlamydophila abortus genome sequence reveals an array of variable proteins that contribute to interspecies variation."
Thomson N.R., Yeats C., Bell K., Holden M.T.G., Bentley S.D., Livingstone M., Cerdeno-Tarraga A.-M., Harris B., Doggett J., Ormond D., Mungall K., Clarke K., Feltwell T., Hance Z., Sanders M., Quail M.A., Price C., Barrell B.G., Parkhill J., Longbottom D.
Genome Res. 15:629-640(2005) [PubMed: 15837807] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: S26/3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR848038 Genomic DNA. Translation: CAH64144.1.
RefSeqYP_220095.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3337603.
GenomeReviewsGene locus CAB697 in contig CR848038_GR.
KEGGcab:CAB697.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG414056.
OMAVEFFPTW.

Enzyme and pathway databases

BioCycCABO218497:CAB697-MONOMER.

Family and domain databases

InterProIPR016104. Pyr-dep_his/arg-deCO2ase.
IPR016105. 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]
ProDomPD010449. Pyruvoyl-dep_arg_deCO2ase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Entry information

Entry nameAAXB_CHLAB
AccessionPrimary (citable) accession number: Q5L5E7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: June 21, 2005
Last modified: January 19, 2010
This is version 23 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