AAXB_CHLTA
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 25-MAY-2022, entry version 77.
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; Chlamydiae; 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 EnsemblBacteria; AAX50639; AAX50639; CTA_0405.
DR KEGG; cta:CTA_0405; -.
DR HOGENOM; CLU_1313366_0_0_0; -.
DR OMA; KKKFGFC; -.
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; -; 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_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