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Q9PK21

- AAXB_CHLMU

UniProt

Q9PK21 - AAXB_CHLMU

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Protein
Pyruvoyl-dependent arginine decarboxylase AaxB
Gene
aaxB, TC_0652
Organism
Chlamydia muridarum (strain MoPn / Nigg)
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.

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

BioCyciCMUR243161:GHYU-675-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:TC_0652
OrganismiChlamydia muridarum (strain MoPn / Nigg)
Taxonomic identifieri243161 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
ProteomesiUP000000800: Chromosome

Subcellular locationi

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 beta
PRO_0000364045Add
BLAST
Chaini53 – 195143Pyruvoyl-dependent arginine decarboxylase subunit alpha
PRO_0000364046Add
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

STRINGi243161.TC0652.

Structurei

3D structure databases

ProteinModelPortaliQ9PK21.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1945.
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.

Q9PK21-1 [UniParc]FASTAAdd to Basket

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MPYGTRYPTL AFHTGGVGES DDGMPPQPFE TFCYDSALLQ AKIENFNIVP    50
YTSVLPKELF GNILPVDQCT KFFKHGAVLE VIMAGKGAAV AEGTQAIATG 100
VGICWGKDKN GDLIGGWAAE YVEFFPTWID DEIAESHAKM WLKKSLQHEL 150
DLRSVSKHSE FQYFHNYINI KKKFGFCLTA LGFLNFENAD PVVIQ 195
Length:195
Mass (Da):21,707
Last modified:October 1, 2000 - v1
Checksum:i865D6DAED68C1463
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE002160 Genomic DNA. Translation: AAF39478.1.
PIRiB81680.
RefSeqiNP_297026.1. NC_002620.2.

Genome annotation databases

EnsemblBacteriaiAAF39478; AAF39478; TC_0652.
GeneIDi1246013.
KEGGicmu:TC_0652.
PATRICi20372758. VBIChlMur19118_0691.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE002160 Genomic DNA. Translation: AAF39478.1 .
PIRi B81680.
RefSeqi NP_297026.1. NC_002620.2.

3D structure databases

ProteinModelPortali Q9PK21.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243161.TC0652.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAF39478 ; AAF39478 ; TC_0652 .
GeneIDi 1246013.
KEGGi cmu:TC_0652.
PATRICi 20372758. VBIChlMur19118_0691.

Phylogenomic databases

eggNOGi COG1945.
OMAi WAVEYVE.
OrthoDBi EOG6Q5NT3.

Enzyme and pathway databases

BioCyci CMUR243161:GHYU-675-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: MoPn / Nigg.

Entry informationi

Entry nameiAAXB_CHLMU
AccessioniPrimary (citable) accession number: Q9PK21
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 65 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

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