ID   PDAD_HALS3              Reviewed;         160 AA.
AC   B0R6U7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Pyruvoyl-dependent arginine decarboxylase;
DE            Short=PvlArgDC;
DE            EC=4.1.1.19;
DE   Contains:
DE     RecName: Full=Pyruvoyl-dependent arginine decarboxylase subunit beta;
DE   Contains:
DE     RecName: Full=Pyruvoyl-dependent arginine decarboxylase subunit alpha;
GN   Name=pdaD; OrderedLocusNames=OE_3803R;
OS   Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=478009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29341 / DSM 671 / R1;
RX   PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA   Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA   Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT   "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT   R1 compared to that of strain NRC-1.";
RL   Genomics 91:335-346(2008).
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   -!- SIMILARITY: Belongs to the PdaD family. {ECO:0000305}.
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DR   EMBL; AM774415; CAP14466.1; -; Genomic_DNA.
DR   RefSeq; WP_010903471.1; NC_010364.1.
DR   AlphaFoldDB; B0R6U7; -.
DR   SMR; B0R6U7; -.
DR   EnsemblBacteria; CAP14466; CAP14466; OE_3803R.
DR   GeneID; 5953199; -.
DR   GeneID; 62887328; -.
DR   KEGG; hsl:OE_3803R; -.
DR   HOGENOM; CLU_134253_0_0_2; -.
DR   OMA; TIRVVWG; -.
DR   Proteomes; UP000001321; Chromosome.
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   PIRSF; PIRSF005216; Pyruvoyl-dep_arg_deCO2ase; 1.
DR   SFLD; SFLDG01170; Pyruvoyl-dependent_arginine_de; 1.
DR   SUPFAM; SSF56271; SSF56271; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Pyruvate.
FT   CHAIN           1..38
FT                   /note="Pyruvoyl-dependent arginine decarboxylase subunit
FT                   beta"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_1000145468"
FT   CHAIN           39..160
FT                   /note="Pyruvoyl-dependent arginine decarboxylase subunit
FT                   alpha"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_1000145469"
FT   SITE            38..39
FT                   /note="Cleavage (non-hydrolytic)"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         39
FT                   /note="Pyruvic acid (Ser)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   160 AA;  16364 MW;  B77749F3A1E97BCD CRC64;
     MPRIRIAWGS GVAPTEMAAY DAALADANVH NYNLIRVSSV IPADATVSPV DTAPDLGPAG
     NTLTVVEARG QTAGPGQASA GLAWAPRDGA PGLFYEAADE TTPDDVADRV TTGITAGMDV
     RDWDGVEPSV RTETVTADAG EHAAAVVIAA YGDSDPVFDQ