Reviewed, UniProtKB/Swiss-Prot Q9Z6M7 (AAXB_CHLPN)

Names and origin

Protein names

Recommended 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:	CPn_1032, CP_0820, CPj1032, CpB1072

Organism

Chlamydia pneumoniae (Chlamydophila pneumoniae) [Complete proteome] [HAMAP]

Taxonomic identifier

83558 [NCBI]

Taxonomic lineage

Bacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydophila

Protein attributes

Sequence length	195 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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. Ref.6
Catalytic activity	L-arginine = agmatine + CO2.
Cofactor	Pyruvoyl group.
Enzyme regulation	Inhibited by argininamide.
Subunit structure	Trimer of an alpha-beta dimer.
Subcellular location	Cytoplasm Probable.
Sequence similarities	Belongs to the pyruvoyl-dependent arginine decarboxylase family.
Biophysicochemical properties	Kinetic parameters: KM=5.0 mM for L-arginine pH dependence: Optimum pH is 3.4. Temperature dependence: Thermostable. Retains 48% activity at 50 degrees Celsius, and 13% activity at 100 degrees Celsius.
Mass spectrometry	Molecular mass is 24283 Da from positions 1 - 195. Determined by MALDI. Ref.5 Molecular mass is 15875 Da from positions 53 - 195. Determined by MALDI. Ref.5

Ontologies

Keywords
Biological process	Virulence
Cellular component	Cytoplasm
Ligand	Pyruvate
Molecular function	Decarboxylase Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	arginine catabolic process Inferred from electronic annotation. Source: InterPro pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	arginine decarboxylase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 52	52	Pyruvoyl-dependent arginine decarboxylase subunit beta		PRO_0000364033
	Chain	53 – 195	143	Pyruvoyl-dependent arginine decarboxylase subunit alpha		PRO_0000364034
Sites
	Site	52 – 53	2	Cleavage (non-hydrolytic)
Amino acid modifications
	Modified residue	53	1	Pyruvic acid (Ser)
Experimental info
	Mutagenesis	52	1	T → S: 70% loss of activity. Significantly impaired in ability to self-cleave. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q9Z6M7-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 1506883FB4854DA2	FASTA	195	21,655
	10 20 30 40 50 60 MAYGTRYPTL AFHTGGIGES DDGMPPQPFE TFCYDSALLQ AKIENFNIVP YTSVLPKELF 70 80 90 100 110 120 GNIVPVDTCV KSFKHGAVLE VIMAGRGAAL SDGTHAIATG IGICWGKDKN GELIGGWAAE 130 140 150 160 170 180 YVEFFPTWIN DEIAETHAKM WLKKSLQHEL DLRSIAKHSE FQFFHNYINI KQKFGFCLTA 190 LGFLNFENAE PAKVN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Comparative genomes of Chlamydia pneumoniae and C. trachomatis." Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W., Olinger L., Grimwood J., Davis R.W., Stephens R.S. Nat. Genet. 21:385-389(1999) [PubMed: 10192388] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CWL029.
[2]	"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39." Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L. , Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M. Nucleic Acids Res. 28:1397-1406(2000) [PubMed: 10684935] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AR39.
[3]	"Comparison of whole genome sequences of Chlamydia pneumoniae J138 from Japan and CWL029 from USA." Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K., Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T. Nucleic Acids Res. 28:2311-2314(2000) [PubMed: 10871362] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: J138.
[4]	"The genome sequence of Chlamydia pneumoniae TW183 and comparison with other Chlamydia strains based on whole genome sequence analysis." Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P., Schneider S., Pohl T., Essig A., Marre R., Melchers K. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TW-183.
[5]	"Characterization of an acid-dependent arginine decarboxylase enzyme from Chlamydophila pneumoniae." Giles T.N., Graham D.E. J. Bacteriol. 189:7376-7383(2007) [PubMed: 17693492] [Abstract] Cited for: CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY, MUTAGENESIS OF THR-52. Strain: Kajaani 6.
[6]	"Outer and inner membrane proteins compose an arginine-agmatine exchange system in Chlamydophila pneumoniae." Smith C.B., Graham D.E. J. Bacteriol. 190:7431-7440(2008) [PubMed: 18790867] [Abstract] Cited for: FUNCTION AS PYRUVOYL-DEPENDENT ARGININE DECARBOXYLASE. Strain: Kajaani 6.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE001363 Genomic DNA. Translation: AAD19169.1. AE002161 Genomic DNA. Translation: AAF38615.1. BA000008 Genomic DNA. Translation: BAA99239.1. AE009440 Genomic DNA. Translation: AAP99001.1.
PIR	B72006. E86619.
RefSeq	NP_225226.1. NP_301087.1. NP_445359.1. NP_877344.1.
3D structure databases
ModBase	Search...
2-D gel databases
PHCI-2DPAGE	Q9Z6M7.
Genome annotation databases
GeneID	1467751. 895497. 919806. 962776.
GenomeReviews	Gene locus CPn_1032 in contig AE001363_GR. Gene locus CP_0820 in contig AE002161_GR. Gene locus CpB1072 in contig AE009440_GR. Gene locus CPj1032 in contig BA000008_GR.
KEGG	cpa:CP0820. cpj:CPj1032. cpn:CPn1032. cpt:CpB1072.
TIGR	CP_0820.
Phylogenomic databases
HOGENOM	Q9Z6M7.
OMA	VEFFPTW.
Enzyme and pathway databases
BioCyc	CPNE115711:CP_0820-MON. CPNE115713:CPN1032-MON. CPNE138677:CPJ1032-MON. CPNE182082:CPB1072-MON.
Family and domain databases
InterPro	IPR016105. Pyr-dep_his/arg-deCO2ase_sand. IPR002724. Pyruvoyl-dep_arg_deCO2ase. [Graphical view]
Gene3D	G3DSA:3.50.20.10. Pyr-dep_his/arg-deCO2ase_sand. 1 hit.
Pfam	PF01862. PvlArgDC. 1 hit. [Graphical view]
ProDom	PD010449. DUF44. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...

Entry information

Entry name

AAXB_CHLPN

Accession

Primary (citable) accession number: Q9Z6M7
Secondary accession number(s): Q7AHX1, Q7BWL3, Q7DE85

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 10, 2009
Last sequence update:	May 1, 1999
Last modified:	November 3, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)