AAXB_CHLT2
ID AAXB_CHLT2 Reviewed; 195 AA.
AC P0C8R4;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 40.
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=CTL0627;
OS Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=471472;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=434/Bu / ATCC VR-902B;
RX PubMed=18032721; DOI=10.1101/gr.7020108;
RA Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P.,
RA Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D.,
RA Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.;
RT "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT venereum isolates.";
RL Genome Res. 18:161-171(2008).
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 -!- SEQUENCE CAUTION:
CC Sequence=AM884176; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AM884176; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0C8R4; -.
DR SMR; P0C8R4; -.
DR Proteomes; UP000000795; 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_0000364035"
FT CHAIN 53..195
FT /note="Pyruvoyl-dependent arginine decarboxylase subunit
FT alpha"
FT /id="PRO_0000364036"
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; 21751 MW; 29C4CF9A309EC05A CRC64;
MPYGTRYPTL AFHTGGVGES DDGMPPQPFE TFCYDSALLQ AKIENFNIVP YTSVLPKELF
GNILPVDQCT KFFKHGAVLE VIMAGRGATV TDGTQAIATG VGICWGKDKN GELIGGWAAE
YVEFFPTWID DEIAESHAKM WLKKSLQHEL DLRSVSKHSE FQYFHNYINI RKKFGFCLTA
LGFLNFENAA PAVIQ