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Protein

Pyruvoyl-dependent arginine decarboxylase AaxB

Gene

aaxB

Organism
Chlamydia trachomatis serovar A (strain HAR-13 / ATCC VR-571B)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

L-arginine = agmatine + CO2.

Cofactori

pyruvateBy similarityNote: Binds 1 pyruvoyl group covalently per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei52 – 532Cleavage (non-hydrolytic)By similarity

GO - Molecular functioni

  1. arginine decarboxylase activity Source: UniProtKB-EC

GO - Biological processi

  1. arginine catabolic process Source: InterPro
  2. pathogenesis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Virulence

Keywords - Ligandi

Pyruvate

Enzyme and pathway databases

BioCyciCTRA315277:GI4C-405-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvoyl-dependent arginine decarboxylase AaxB (EC:4.1.1.19)
Short name:
PvlArgDC
Alternative name(s):
Biodegradative arginine decarboxylase
Cleaved into the following 2 chains:
Gene namesi
Name:aaxB
Ordered Locus Names:CTA_0405
OrganismiChlamydia trachomatis serovar A (strain HAR-13 / ATCC VR-571B)
Taxonomic identifieri315277 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
ProteomesiUP000002532 Componenti: Chromosome

Subcellular locationi

  1. Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 5252Pyruvoyl-dependent arginine decarboxylase subunit betaPRO_0000364049Add
BLAST
Chaini53 – 195143Pyruvoyl-dependent arginine decarboxylase subunit alphaPRO_0000364050Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei53 – 531Pyruvic acid (Ser)By similarity

Interactioni

Subunit structurei

Trimer of an alpha-beta dimer.By similarity

Protein-protein interaction databases

STRINGi315277.CTA_0405.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1945.
HOGENOMiHOG000025218.
OMAiWAVEYVE.
OrthoDBiEOG6Q5NT3.

Family and domain databases

Gene3Di3.50.20.10. 1 hit.
InterProiIPR016104. Pyr-dep_his/arg-deCO2ase.
IPR016105. Pyr-dep_his/arg-deCO2ase_sand.
IPR002724. Pyruvoyl-dep_arg_deCO2ase.
[Graphical view]
PfamiPF01862. PvlArgDC. 1 hit.
[Graphical view]
ProDomiPD010449. Pyruvoyl-dep_arg_deCO2ase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF56271. SSF56271. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q3KLY3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPYGTRYPTL AFHTGGVGES DDGMPPQPFE TFCYDSALLQ AKIENFNIVP
60 70 80 90 100
YTSVLPKELF GNILPVDQCT KFFKHGAVLE VIMAGRGATV TDGTQAIATG
110 120 130 140 150
VGICWGKDKN GELIRGWAVE YVEFFPTWID DEIAESHAKM WLKKSLQHEL
160 170 180 190
DLRSISKHSE FQYFHNYINI IKKFGFCLTA LGFLNFENAA PAVIQ
Length:195
Mass (Da):21,849
Last modified:November 8, 2005 - v1
Checksum:iFEA027A238B6FB48
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000051 Genomic DNA. Translation: AAX50639.1.
RefSeqiWP_011324706.1. NC_007429.1.
YP_328187.1. NC_007429.1.

Genome annotation databases

EnsemblBacteriaiAAX50639; AAX50639; CTA_0405.
KEGGicta:CTA_0405.
PATRICi32022690. VBIChlTra31516_0411.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000051 Genomic DNA. Translation: AAX50639.1.
RefSeqiWP_011324706.1. NC_007429.1.
YP_328187.1. NC_007429.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi315277.CTA_0405.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAX50639; AAX50639; CTA_0405.
KEGGicta:CTA_0405.
PATRICi32022690. VBIChlTra31516_0411.

Phylogenomic databases

eggNOGiCOG1945.
HOGENOMiHOG000025218.
OMAiWAVEYVE.
OrthoDBiEOG6Q5NT3.

Enzyme and pathway databases

BioCyciCTRA315277:GI4C-405-MONOMER.

Family and domain databases

Gene3Di3.50.20.10. 1 hit.
InterProiIPR016104. Pyr-dep_his/arg-deCO2ase.
IPR016105. Pyr-dep_his/arg-deCO2ase_sand.
IPR002724. Pyruvoyl-dep_arg_deCO2ase.
[Graphical view]
PfamiPF01862. PvlArgDC. 1 hit.
[Graphical view]
ProDomiPD010449. Pyruvoyl-dep_arg_deCO2ase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF56271. SSF56271. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiAAXB_CHLTA
AccessioniPrimary (citable) accession number: Q3KLY3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: November 8, 2005
Last modified: April 29, 2015
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.