AAXB_CHLPN
ID AAXB_CHLPN Reviewed; 195 AA.
AC Q9Z6M7; Q7AHX1; Q7BWL3; Q7DE85;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Pyruvoyl-dependent arginine decarboxylase AaxB;
DE Short=PvlArgDC;
DE EC=4.1.1.19;
DE AltName: Full=Biodegradative arginine decarboxylase;
DE Contains:
DE RecName: Full=Pyruvoyl-dependent arginine decarboxylase subunit beta;
DE Contains:
DE RecName: Full=Pyruvoyl-dependent arginine decarboxylase subunit alpha;
GN Name=aaxB; OrderedLocusNames=CPn_1032, CP_0820, CPj1032, CpB1072;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY,
RP MUTAGENESIS OF THR-52, AND PYRUVATE FORMATION AT SER-53.
RC STRAIN=Kajaani 6;
RX PubMed=17693492; DOI=10.1128/jb.00772-07;
RA Giles T.N., Graham D.E.;
RT "Characterization of an acid-dependent arginine decarboxylase enzyme from
RT Chlamydophila pneumoniae.";
RL J. Bacteriol. 189:7376-7383(2007).
RN [6]
RP FUNCTION AS PYRUVOYL-DEPENDENT ARGININE DECARBOXYLASE.
RC STRAIN=Kajaani 6;
RX PubMed=18790867; DOI=10.1128/jb.00652-08;
RA Smith C.B., Graham D.E.;
RT "Outer and inner membrane proteins compose an arginine-agmatine exchange
RT system in Chlamydophila pneumoniae.";
RL J. Bacteriol. 190:7431-7440(2008).
CC -!- FUNCTION: Part of the AaxABC system, catalyzes the decarboxylation of
CC L-arginine. The arginine uptake by the bacterium in the macrophage may
CC be a virulence factor against the host innate immune response.
CC {ECO:0000269|PubMed:18790867}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-arginine = agmatine + CO2; Xref=Rhea:RHEA:17641,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:58145; EC=4.1.1.19;
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Note=Binds 1 pyruvoyl group covalently per subunit.;
CC -!- ACTIVITY REGULATION: Inhibited by argininamide.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.0 mM for L-arginine {ECO:0000269|PubMed:17693492};
CC pH dependence:
CC Optimum pH is 3.4. {ECO:0000269|PubMed:17693492};
CC Temperature dependence:
CC Thermostable. Retains 48% activity at 50 degrees Celsius, and 13%
CC activity at 100 degrees Celsius. {ECO:0000269|PubMed:17693492};
CC -!- SUBUNIT: Trimer of an alpha-beta dimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- MASS SPECTROMETRY: [Pyruvoyl-dependent arginine decarboxylase subunit
CC alpha]: Mass=15875; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:17693492};
CC -!- SIMILARITY: Belongs to the pyruvoyl-dependent arginine decarboxylase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE001363; AAD19169.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF38615.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA99239.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP99001.1; -; Genomic_DNA.
DR PIR; B72006; B72006.
DR PIR; E86619; E86619.
DR RefSeq; NP_225226.1; NC_000922.1.
DR RefSeq; WP_010883665.1; NZ_LN847257.1.
DR AlphaFoldDB; Q9Z6M7; -.
DR SMR; Q9Z6M7; -.
DR STRING; 115711.CP_0820; -.
DR EnsemblBacteria; AAD19169; AAD19169; CPn_1032.
DR EnsemblBacteria; AAF38615; AAF38615; CP_0820.
DR GeneID; 45051090; -.
DR KEGG; cpa:CP_0820; -.
DR KEGG; cpj:CPj1032; -.
DR KEGG; cpn:CPn_1032; -.
DR KEGG; cpt:CpB1072; -.
DR PATRIC; fig|115713.3.peg.1130; -.
DR eggNOG; COG1945; Bacteria.
DR HOGENOM; CLU_1313366_0_0_0; -.
DR OMA; KKKFGFC; -.
DR OrthoDB; 1265324at2; -.
DR SABIO-RK; Q9Z6M7; -.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR Gene3D; 3.50.20.10; -; 1.
DR InterPro; IPR016104; Pyr-dep_his/arg-deCO2ase.
DR InterPro; IPR016105; Pyr-dep_his/arg-deCO2ase_sand.
DR InterPro; IPR002724; Pyruvoyl-dep_arg_deCO2ase.
DR PANTHER; PTHR40438; PTHR40438; 1.
DR Pfam; PF01862; PvlArgDC; 1.
DR SFLD; SFLDG01170; Pyruvoyl-dependent_arginine_de; 1.
DR SUPFAM; SSF56271; SSF56271; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Decarboxylase; Lyase; Pyruvate; Virulence.
FT CHAIN 1..52
FT /note="Pyruvoyl-dependent arginine decarboxylase subunit
FT beta"
FT /id="PRO_0000364033"
FT CHAIN 53..195
FT /note="Pyruvoyl-dependent arginine decarboxylase subunit
FT alpha"
FT /id="PRO_0000364034"
FT SITE 52..53
FT /note="Cleavage (non-hydrolytic)"
FT MOD_RES 53
FT /note="Pyruvic acid (Ser)"
FT /evidence="ECO:0000269|PubMed:17693492"
FT MUTAGEN 52
FT /note="T->S: 70% loss of activity. Significantly impaired
FT in ability to self-cleave."
FT /evidence="ECO:0000269|PubMed:17693492"
SQ SEQUENCE 195 AA; 21655 MW; 1506883FB4854DA2 CRC64;
MAYGTRYPTL AFHTGGIGES DDGMPPQPFE TFCYDSALLQ AKIENFNIVP YTSVLPKELF
GNIVPVDTCV KSFKHGAVLE VIMAGRGAAL SDGTHAIATG IGICWGKDKN GELIGGWAAE
YVEFFPTWIN DEIAETHAKM WLKKSLQHEL DLRSIAKHSE FQFFHNYINI KQKFGFCLTA
LGFLNFENAE PAKVN
