ID   AAXB_CHLFF              Reviewed;         195 AA.
AC   Q255I0;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   25-MAY-2022, entry version 73.
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=CF0286;
OS   Chlamydia felis (strain Fe/C-56) (Chlamydophila felis).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=264202;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fe/C-56;
RX   PubMed=16766509; DOI=10.1093/dnares/dsi027;
RA   Azuma Y., Hirakawa H., Yamashita A., Cai Y., Rahman M.A., Suzuki H.,
RA   Mitaku S., Toh H., Goto S., Murakami T., Sugi K., Hayashi H., Fukushi H.,
RA   Hattori M., Kuhara S., Shirai M.;
RT   "Genome sequence of the cat pathogen, Chlamydophila felis.";
RL   DNA Res. 13:15-23(2006).
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; AP006861; BAE81058.1; -; Genomic_DNA.
DR   RefSeq; WP_011457839.1; NC_007899.1.
DR   AlphaFoldDB; Q255I0; -.
DR   SMR; Q255I0; -.
DR   STRING; 264202.CF0286; -.
DR   KEGG; cfe:CF0286; -.
DR   eggNOG; COG1945; Bacteria.
DR   HOGENOM; CLU_1313366_0_0_0; -.
DR   OMA; KKKFGFC; -.
DR   OrthoDB; 1265324at2; -.
DR   Proteomes; UP000001260; 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_0000364041"
FT   CHAIN           53..195
FT                   /note="Pyruvoyl-dependent arginine decarboxylase subunit
FT                   alpha"
FT                   /id="PRO_0000364042"
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;  21743 MW;  EB6BEE3D1C2FD826 CRC64;
     MTYGTRYPTL AFHTGGIGES DDGMPPQPFE TFCYDSALLQ AKIENFNIVP YTSVLPKELF
     GNIVPVDQCV KSFKHGAVLE VIMAGRGAAT VDGTHAIATG VGICWGQDKN GELIGGWAAE
     YVEFFPTWIN DEIAESHAKM WLKKSLQHEL DLRSIVKHSE FQYFHNYINI KKKYGFSLTA
     LGFLNFENAD PVTIK