Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q3KLY3 (AAXB_CHLTA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 47. 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:CTA_0405
OrganismChlamydia trachomatis serovar A (strain HAR-13 / ATCC VR-571B) [Complete proteome] [HAMAP]
Taxonomic identifier315277 [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.

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_0000364049
Chain53 – 195143Pyruvoyl-dependent arginine decarboxylase subunit alpha
PRO_0000364050

Sites

Site52 – 532Cleavage (non-hydrolytic) By similarity

Amino acid modifications

Modified residue531Pyruvic acid (Ser) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3KLY3 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: FEA027A238B6FB48

FASTA19521,849
        10         20         30         40         50         60 
MPYGTRYPTL AFHTGGVGES DDGMPPQPFE TFCYDSALLQ AKIENFNIVP YTSVLPKELF 

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

       130        140        150        160        170        180 
YVEFFPTWID DEIAESHAKM WLKKSLQHEL DLRSISKHSE FQYFHNYINI IKKFGFCLTA 

       190 
LGFLNFENAA PAVIQ 

« Hide

References

[1]"Comparative genomic analysis of Chlamydia trachomatis oculotropic and genitotropic strains."
Carlson J.H., Porcella S.F., McClarty G., Caldwell H.D.
Infect. Immun. 73:6407-6418(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HAR-13 / ATCC VR-571B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000051 Genomic DNA. Translation: AAX50639.1.
RefSeqYP_328187.1. NC_007429.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING315277.CTA_0405.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAX50639; AAX50639; CTA_0405.
GeneID3688033.
KEGGcta:CTA_0405.
PATRIC32022690. VBIChlTra31516_0411.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1945.
HOGENOMHOG000025218.
OMAWAVEYVE.
OrthoDBEOG6Q5NT3.
ProtClustDBCLSK403032.

Enzyme and pathway databases

BioCycCTRA315277:GI4C-405-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_CHLTA
AccessionPrimary (citable) accession number: Q3KLY3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: November 8, 2005
Last modified: November 13, 2013
This is version 47 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