ID   PDAD1_METMA             Reviewed;         165 AA.
AC   P58889;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2002, sequence version 1.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Pyruvoyl-dependent arginine decarboxylase 1;
DE            Short=PvlArgDC 1;
DE            EC=4.1.1.19;
DE   Contains:
DE     RecName: Full=Pyruvoyl-dependent arginine decarboxylase 1 subunit beta;
DE   Contains:
DE     RecName: Full=Pyruvoyl-dependent arginine decarboxylase 1 subunit alpha;
GN   Name=pdaD1; OrderedLocusNames=MM_0286;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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; AE008384; AAM29982.1; -; Genomic_DNA.
DR   RefSeq; WP_011032240.1; NC_003901.1.
DR   AlphaFoldDB; P58889; -.
DR   SMR; P58889; -.
DR   STRING; 192952.MM_0286; -.
DR   EnsemblBacteria; AAM29982; AAM29982; MM_0286.
DR   GeneID; 24877195; -.
DR   KEGG; mma:MM_0286; -.
DR   PATRIC; fig|192952.21.peg.353; -.
DR   eggNOG; arCOG04490; Archaea.
DR   HOGENOM; CLU_114389_0_0_2; -.
DR   OMA; VFCVMSR; -.
DR   Proteomes; UP000000595; 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..44
FT                   /note="Pyruvoyl-dependent arginine decarboxylase 1 subunit
FT                   beta"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000023318"
FT   CHAIN           45..165
FT                   /note="Pyruvoyl-dependent arginine decarboxylase 1 subunit
FT                   alpha"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000023319"
FT   SITE            44..45
FT                   /note="Cleavage (non-hydrolytic)"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         45
FT                   /note="Pyruvic acid (Ser)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   165 AA;  17992 MW;  5F56185DBD942D92 CRC64;
     MITKLIPKKV FFTSGAGTHP EKLESFEAAL RDACIEKFNL VTVSSILPPR CEIVTKEEGL
     KELSPGEIVF CVMSRISSND PGKTLTSSVG CALPVDISKH GYISEYHAYE ESAQDAGAHA
     VKLAESMYST WTKEEPLKTF SIPRSSTVKD SGDWMTVISA AVFVI