ID   PDAD_PROA2              Reviewed;         181 AA.
AC   B4S6J7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 64.
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=Paes_0705;
OS   Prosthecochloris aestuarii (strain DSM 271 / SK 413).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Prosthecochloris.
OX   NCBI_TaxID=290512;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 271 / SK 413;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Anderson I., Liu Z., Li T., Zhao F., Overmann J.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of chromosome of Prosthecochloris aestuarii DSM 271.";
RL   Submitted (JUN-2008) 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; CP001108; ACF45752.1; -; Genomic_DNA.
DR   RefSeq; WP_012505289.1; NC_011059.1.
DR   AlphaFoldDB; B4S6J7; -.
DR   SMR; B4S6J7; -.
DR   STRING; 290512.Paes_0705; -.
DR   EnsemblBacteria; ACF45752; ACF45752; Paes_0705.
DR   KEGG; paa:Paes_0705; -.
DR   eggNOG; COG1945; Bacteria.
DR   HOGENOM; CLU_114389_0_0_10; -.
DR   OMA; SEHHSFG; -.
DR   OrthoDB; 1428605at2; -.
DR   Proteomes; UP000002725; 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; Reference proteome.
FT   CHAIN           1..42
FT                   /note="Pyruvoyl-dependent arginine decarboxylase subunit
FT                   beta"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01404"
FT                   /id="PRO_1000145474"
FT   CHAIN           43..181
FT                   /note="Pyruvoyl-dependent arginine decarboxylase subunit
FT                   alpha"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01404"
FT                   /id="PRO_1000145475"
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;  19898 MW;  968B05A7649D11F7 CRC64;
     MSFVPTKVFF TKGVGRHKEY LSSFELALRE AKIEKCNLVT VSSIFPPQCE RISVEEGLKS
     LSPGEITFAV MARNSTNEHG RLIASSIGVA LPADESVYGY LSEHHPYGQT EEQSGEYAED
     LAATMLATTL GIEFDPNKDW DEREGIYKMS GKIINSFNIT QSAEGQNGLW TTVIACAVLL
     P