PDAD_THEAC
ID PDAD_THEAC Reviewed; 182 AA.
AC Q9HK30;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 25-MAY-2022, entry version 94.
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=Ta0778;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC11909.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL445065; CAC11909.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_048161787.1; NC_002578.1.
DR AlphaFoldDB; Q9HK30; -.
DR SMR; Q9HK30; -.
DR STRING; 273075.Ta0778; -.
DR EnsemblBacteria; CAC11909; CAC11909; CAC11909.
DR GeneID; 1456332; -.
DR KEGG; tac:Ta0778; -.
DR eggNOG; arCOG04490; Archaea.
DR HOGENOM; CLU_114389_0_0_2; -.
DR OMA; SEHHSFG; -.
DR OrthoDB; 98606at2157; -.
DR Proteomes; UP000001024; 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_0000023336"
FT CHAIN 44..182
FT /note="Pyruvoyl-dependent arginine decarboxylase subunit
FT alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01404"
FT /id="PRO_0000023337"
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 182 AA; 19672 MW; 2053EE343EE41B89 CRC64;
MSGFVPTHIF FTRGVGRGET QLVSFEAALR DAGIAPYNLS SISSIFPPHA EMITREEGLK
KLSPGQILFT VLARNTSNEL NRMVSAAIGY AIPRDRSKWG YLSEHHSFGE TEKVAGSFAE
KLAAEMLAST IGSSAQLAYD KQKEEYVLED KILTTGSISS TAVVLESGEW TTVVAAAVLI
VE