ID   AAXB_CHLTR              Reviewed;         195 AA.
AC   O84378;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-2024, entry version 94.
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=CT_373;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
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}.
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; AE001273; AAC67969.1; -; Genomic_DNA.
DR   PIR; F71523; F71523.
DR   RefSeq; NP_219882.1; NC_000117.1.
DR   RefSeq; WP_010725175.1; NC_000117.1.
DR   AlphaFoldDB; O84378; -.
DR   SMR; O84378; -.
DR   STRING; 272561.CT_373; -.
DR   EnsemblBacteria; AAC67969; AAC67969; CT_373.
DR   GeneID; 884742; -.
DR   KEGG; ctr:CT_373; -.
DR   PATRIC; fig|272561.5.peg.402; -.
DR   HOGENOM; CLU_1313366_0_0_0; -.
DR   InParanoid; O84378; -.
DR   OrthoDB; 9783061at2; -.
DR   Proteomes; UP000000431; 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; Reference proteome; Virulence.
FT   CHAIN           1..52
FT                   /note="Pyruvoyl-dependent arginine decarboxylase subunit
FT                   beta"
FT                   /id="PRO_0000364047"
FT   CHAIN           53..195
FT                   /note="Pyruvoyl-dependent arginine decarboxylase subunit
FT                   alpha"
FT                   /id="PRO_0000364048"
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;  21864 MW;  2BF6DCA22A2F705A CRC64;
     MPYGTRYPTL AFHTGGVGES DDGMPPQPFE TFCYDSALLQ AKIENFNIVP YTSVLPKELF
     GNILPVDQCT KFFKHGAVLE VIMAGRGATV TDGTQAIATG VGICWGKDKN GELIRGWAAE
     YVEFFPTWID DEIAESHAKM WLKKSLQHEL DLRSISKHSE FQYFHNYINI RKKFGFCLTA
     LGFLNFENAA PAVIQ
//