ID   AAXB_CHLTA              Reviewed;         195 AA.
AC   Q3KLY3;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 82.
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=CTA_0405;
OS   Chlamydia trachomatis serovar A (strain ATCC VR-571B / DSM 19440 / HAR-13).
OC   Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=315277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-571B / DSM 19440 / HAR-13;
RX   PubMed=16177312; DOI=10.1128/iai.73.10.6407-6418.2005;
RA   Carlson J.H., Porcella S.F., McClarty G., Caldwell H.D.;
RT   "Comparative genomic analysis of Chlamydia trachomatis oculotropic and
RT   genitotropic strains.";
RL   Infect. Immun. 73:6407-6418(2005).
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; CP000051; AAX50639.1; -; Genomic_DNA.
DR   RefSeq; WP_011324706.1; NC_007429.1.
DR   AlphaFoldDB; Q3KLY3; -.
DR   SMR; Q3KLY3; -.
DR   KEGG; cta:CTA_0405; -.
DR   HOGENOM; CLU_1313366_0_0_0; -.
DR   Proteomes; UP000002532; 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; Pyruvoyl-Dependent Histidine Decarboxylase, subunit B; 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; PYRUVOYL-DEPENDENT ARGININE DECARBOXYLASE; 1.
DR   PANTHER; PTHR40438:SF1; PYRUVOYL-DEPENDENT ARGININE DECARBOXYLASE; 1.
DR   Pfam; PF01862; PvlArgDC; 1.
DR   SFLD; SFLDG01170; Pyruvoyl-dependent_arginine_de; 1.
DR   SUPFAM; SSF56271; Pyruvoyl-dependent histidine and arginine decarboxylases; 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_0000364049"
FT   CHAIN           53..195
FT                   /note="Pyruvoyl-dependent arginine decarboxylase subunit
FT                   alpha"
FT                   /id="PRO_0000364050"
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;  21849 MW;  FEA027A238B6FB48 CRC64;
     MPYGTRYPTL AFHTGGVGES DDGMPPQPFE TFCYDSALLQ AKIENFNIVP YTSVLPKELF
     GNILPVDQCT KFFKHGAVLE VIMAGRGATV TDGTQAIATG VGICWGKDKN GELIRGWAVE
     YVEFFPTWID DEIAESHAKM WLKKSLQHEL DLRSISKHSE FQYFHNYINI IKKFGFCLTA
     LGFLNFENAA PAVIQ
//