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PDAD_THESM
ID   PDAD_THESM              Reviewed;         158 AA.
AC   C6A2R5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=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=TSIB_0849;
OS   Thermococcus sibiricus (strain DSM 12597 / MM 739).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=604354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12597 / MM 739;
RX   PubMed=19447963; DOI=10.1128/aem.00718-09;
RA   Mardanov A.V., Ravin N.V., Svetlitchnyi V.A., Beletsky A.V.,
RA   Miroshnichenko M.L., Bonch-Osmolovskaya E.A., Skryabin K.G.;
RT   "Metabolic versatility and indigenous origin of the archaeon Thermococcus
RT   sibiricus, isolated from a siberian oil reservoir, as revealed by genome
RT   analysis.";
RL   Appl. Environ. Microbiol. 75:4580-4588(2009).
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; CP001463; ACS89910.1; -; Genomic_DNA.
DR   RefSeq; WP_015849130.1; NC_012883.1.
DR   AlphaFoldDB; C6A2R5; -.
DR   SMR; C6A2R5; -.
DR   STRING; 604354.TSIB_0849; -.
DR   EnsemblBacteria; ACS89910; ACS89910; TSIB_0849.
DR   GeneID; 8095840; -.
DR   KEGG; tsi:TSIB_0849; -.
DR   eggNOG; arCOG04490; Archaea.
DR   HOGENOM; CLU_114389_2_0_2; -.
DR   OMA; AAALWYK; -.
DR   OrthoDB; 98606at2157; -.
DR   Proteomes; UP000009079; 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..43
FT                   /note="Pyruvoyl-dependent arginine decarboxylase subunit
FT                   beta"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01404"
FT                   /id="PRO_1000215198"
FT   CHAIN           44..158
FT                   /note="Pyruvoyl-dependent arginine decarboxylase subunit
FT                   alpha"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01404"
FT                   /id="PRO_1000215199"
FT   SITE            43..44
FT                   /note="Cleavage (non-hydrolytic)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01404"
FT   MOD_RES         44
FT                   /note="Pyruvic acid (Ser)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01404"
SQ   SEQUENCE   158 AA;  17071 MW;  97831E53ABC8F769 CRC64;
     MSWTTPKKAI LLAASAEGST KLNAFDNALL KMGIGNVNLV KLSSVIPAYI EWIDELPKNI
     PVGMLLPTVY AHIESDEPGS TITAALGVGI SEGNEGGLIY EYSGYCTKEE AEKMVHKMVE
     EGFKVRGWKL KEFKAAVAEI TVKDRPVAAI AAVVMLPY
 
 
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