ID   AAXB_CHLMU              Reviewed;         195 AA.
AC   Q9PK21;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 92.
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=TC_0652;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
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).
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 (By
CC       similarity). {ECO:0000250}.
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; Evidence={ECO:0000250};
CC       Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Trimer of an alpha-beta dimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the pyruvoyl-dependent arginine decarboxylase
CC       family. {ECO:0000305}.
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DR   EMBL; AE002160; AAF39478.1; -; Genomic_DNA.
DR   PIR; B81680; B81680.
DR   RefSeq; WP_010231121.1; NZ_CP027217.1.
DR   AlphaFoldDB; Q9PK21; -.
DR   SMR; Q9PK21; -.
DR   STRING; 243161.TC_0652; -.
DR   EnsemblBacteria; AAF39478; AAF39478; TC_0652.
DR   GeneID; 1246013; -.
DR   KEGG; cmu:TC_0652; -.
DR   eggNOG; COG1945; Bacteria.
DR   HOGENOM; CLU_1313366_0_0_0; -.
DR   OMA; KKKFGFC; -.
DR   OrthoDB; 1265324at2; -.
DR   Proteomes; UP000000800; 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   3: Inferred from homology;
KW   Cytoplasm; Decarboxylase; Lyase; Pyruvate; Virulence.
FT   CHAIN           1..52
FT                   /note="Pyruvoyl-dependent arginine decarboxylase subunit
FT                   beta"
FT                   /id="PRO_0000364045"
FT   CHAIN           53..195
FT                   /note="Pyruvoyl-dependent arginine decarboxylase subunit
FT                   alpha"
FT                   /id="PRO_0000364046"
FT   SITE            52..53
FT                   /note="Cleavage (non-hydrolytic)"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         53
FT                   /note="Pyruvic acid (Ser)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   195 AA;  21707 MW;  865D6DAED68C1463 CRC64;
     MPYGTRYPTL AFHTGGVGES DDGMPPQPFE TFCYDSALLQ AKIENFNIVP YTSVLPKELF
     GNILPVDQCT KFFKHGAVLE VIMAGKGAAV AEGTQAIATG VGICWGKDKN GDLIGGWAAE
     YVEFFPTWID DEIAESHAKM WLKKSLQHEL DLRSVSKHSE FQYFHNYINI KKKFGFCLTA
     LGFLNFENAD PVVIQ