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Q255I0

- AAXB_CHLFF

UniProt

Q255I0 - AAXB_CHLFF

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Protein

Pyruvoyl-dependent arginine decarboxylase AaxB

Gene

aaxB

Organism
Chlamydophila felis (strain Fe/C-56)
Status
Reviewed - 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

Pyruvoyl group.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

BioCyciCFEL264202:GJCG-298-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:CF0286
OrganismiChlamydophila felis (strain Fe/C-56)
Taxonomic identifieri264202 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydophila
ProteomesiUP000001260: Chromosome

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 5252Pyruvoyl-dependent arginine decarboxylase subunit betaPRO_0000364041Add
BLAST
Chaini53 – 195143Pyruvoyl-dependent arginine decarboxylase subunit alphaPRO_0000364042Add
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

STRINGi264202.CF0286.

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.

Q255I0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTYGTRYPTL AFHTGGIGES DDGMPPQPFE TFCYDSALLQ AKIENFNIVP
60 70 80 90 100
YTSVLPKELF GNIVPVDQCV KSFKHGAVLE VIMAGRGAAT VDGTHAIATG
110 120 130 140 150
VGICWGQDKN GELIGGWAAE YVEFFPTWIN DEIAESHAKM WLKKSLQHEL
160 170 180 190
DLRSIVKHSE FQYFHNYINI KKKYGFSLTA LGFLNFENAD PVTIK
Length:195
Mass (Da):21,743
Last modified:April 18, 2006 - v1
Checksum:iEB6BEE3D1C2FD826
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP006861 Genomic DNA. Translation: BAE81058.1.
RefSeqiWP_011457839.1. NC_007899.1.
YP_515203.1. NC_007899.1.

Genome annotation databases

GeneIDi3958395.
KEGGicfe:CF0286.
PATRICi20204148. VBIChlFel51660_0293.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP006861 Genomic DNA. Translation: BAE81058.1 .
RefSeqi WP_011457839.1. NC_007899.1.
YP_515203.1. NC_007899.1.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 264202.CF0286.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 3958395.
KEGGi cfe:CF0286.
PATRICi 20204148. VBIChlFel51660_0293.

Phylogenomic databases

eggNOGi COG1945.
HOGENOMi HOG000025218.
OMAi WAVEYVE.
OrthoDBi EOG6Q5NT3.

Enzyme and pathway databases

BioCyci CFEL264202:GJCG-298-MONOMER.

Family and domain databases

Gene3Di 3.50.20.10. 1 hit.
InterProi IPR016104. Pyr-dep_his/arg-deCO2ase.
IPR016105. Pyr-dep_his/arg-deCO2ase_sand.
IPR002724. Pyruvoyl-dep_arg_deCO2ase.
[Graphical view ]
Pfami PF01862. PvlArgDC. 1 hit.
[Graphical view ]
ProDomi PD010449. Pyruvoyl-dep_arg_deCO2ase. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF56271. SSF56271. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Fe/C-56.

Entry informationi

Entry nameiAAXB_CHLFF
AccessioniPrimary (citable) accession number: Q255I0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: April 18, 2006
Last modified: October 29, 2014
This is version 46 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