ID   PDAD_CHLL3              Reviewed;         181 AA.
AC   Q3B5D1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Probable pyruvoyl-dependent arginine decarboxylase {ECO:0000255|HAMAP-Rule:MF_01404};
DE            Short=PvlArgDC {ECO:0000255|HAMAP-Rule:MF_01404};
DE            EC=4.1.1.19 {ECO:0000255|HAMAP-Rule:MF_01404};
DE   Contains:
DE     RecName: Full=Pyruvoyl-dependent arginine decarboxylase subunit beta {ECO:0000255|HAMAP-Rule:MF_01404};
DE   Contains:
DE     RecName: Full=Pyruvoyl-dependent arginine decarboxylase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01404};
GN   Name=pdaD {ECO:0000255|HAMAP-Rule:MF_01404}; OrderedLocusNames=Plut_0567;
OS   Chlorobium luteolum (strain DSM 273 / BCRC 81028 / 2530) (Pelodictyon
OS   luteolum).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Pelodictyon.
OX   NCBI_TaxID=319225;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 273 / BCRC 81028 / 2530;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Pelodictyon luteolum DSM 273.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01404};
CC   -!- COFACTOR:
CC       Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01404};
CC       Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01404};
CC   -!- SIMILARITY: Belongs to the PdaD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01404}.
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DR   EMBL; CP000096; ABB23450.1; -; Genomic_DNA.
DR   RefSeq; WP_011357325.1; NC_007512.1.
DR   AlphaFoldDB; Q3B5D1; -.
DR   SMR; Q3B5D1; -.
DR   STRING; 319225.Plut_0567; -.
DR   EnsemblBacteria; ABB23450; ABB23450; Plut_0567.
DR   KEGG; plt:Plut_0567; -.
DR   eggNOG; COG1945; Bacteria.
DR   HOGENOM; CLU_114389_0_0_10; -.
DR   OMA; SEHHSFG; -.
DR   OrthoDB; 1428605at2; -.
DR   Proteomes; UP000002709; Chromosome.
DR   GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR   Gene3D; 3.50.20.10; -; 1.
DR   HAMAP; MF_01404; PvlArgDC; 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   PIRSF; PIRSF005216; Pyruvoyl-dep_arg_deCO2ase; 1.
DR   SFLD; SFLDG01170; Pyruvoyl-dependent_arginine_de; 1.
DR   SUPFAM; SSF56271; SSF56271; 1.
DR   TIGRFAMs; TIGR00286; TIGR00286; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Pyruvate.
FT   CHAIN           1..42
FT                   /note="Pyruvoyl-dependent arginine decarboxylase subunit
FT                   beta"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01404"
FT                   /id="PRO_1000068401"
FT   CHAIN           43..181
FT                   /note="Pyruvoyl-dependent arginine decarboxylase subunit
FT                   alpha"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01404"
FT                   /id="PRO_1000068402"
FT   SITE            42..43
FT                   /note="Cleavage (non-hydrolytic)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01404"
FT   MOD_RES         43
FT                   /note="Pyruvic acid (Ser)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01404"
SQ   SEQUENCE   181 AA;  19988 MW;  7C61194128C950C0 CRC64;
     MSFVPSKVFF TKGVGRHKEY LSSFELALRD AKIEKCNLVT VSSIFPPKCE RVSVEEGVKM
     LTPGQITFAV MARNSTNEYN RLIAASIGVA IPADDTQYGY LSEHHPFGED AEQSGEYAED
     LAATMLATTL GIEFDPNKDW DEREGIYKMS GKIINSYNIT QSAEGENGMW TTVISCAVLL
     P