ID   PDAD2_ARCFU             Reviewed;         157 AA.
AC   O30240;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 116.
DE   RecName: Full=Pyruvoyl-dependent arginine decarboxylase 2;
DE            Short=PvlArgDC 2;
DE            EC=4.1.1.19;
DE   Contains:
DE     RecName: Full=Pyruvoyl-dependent arginine decarboxylase 2 subunit beta;
DE   Contains:
DE     RecName: Full=Pyruvoyl-dependent arginine decarboxylase 2 subunit alpha;
GN   Name=pdaD2; OrderedLocusNames=AF_2431;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
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; AE000782; AAB91232.1; -; Genomic_DNA.
DR   PIR; H69553; H69553.
DR   RefSeq; WP_010879918.1; NC_000917.1.
DR   AlphaFoldDB; O30240; -.
DR   SMR; O30240; -.
DR   STRING; 224325.AF_2431; -.
DR   PaxDb; 224325-AF_2431; -.
DR   EnsemblBacteria; AAB91232; AAB91232; AF_2431.
DR   GeneID; 24796155; -.
DR   KEGG; afu:AF_2431; -.
DR   eggNOG; arCOG04490; Archaea.
DR   HOGENOM; CLU_114389_0_0_2; -.
DR   OrthoDB; 30748at2157; -.
DR   PhylomeDB; O30240; -.
DR   Proteomes; UP000002199; 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; Pyruvoyl-Dependent Histidine Decarboxylase, subunit B; 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   NCBIfam; TIGR00286; arginine decarboxylase, pyruvoyl-dependent; 1.
DR   PANTHER; PTHR40438; PYRUVOYL-DEPENDENT ARGININE DECARBOXYLASE; 1.
DR   PANTHER; PTHR40438:SF1; PYRUVOYL-DEPENDENT ARGININE DECARBOXYLASE; 1.
DR   Pfam; PF01862; PvlArgDC; 1.
DR   PIRSF; PIRSF005216; Pyruvoyl-dep_arg_deCO2ase; 1.
DR   SFLD; SFLDG01170; Pyruvoyl-dependent_arginine_de; 1.
DR   SFLD; SFLDS00055; Pyruvoyl-Dependent_Histidine/A; 1.
DR   SUPFAM; SSF56271; Pyruvoyl-dependent histidine and arginine decarboxylases; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Pyruvate; Reference proteome.
FT   CHAIN           1..42
FT                   /note="Pyruvoyl-dependent arginine decarboxylase 2 subunit
FT                   beta"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000023306"
FT   CHAIN           43..157
FT                   /note="Pyruvoyl-dependent arginine decarboxylase 2 subunit
FT                   alpha"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000023307"
FT   SITE            42..43
FT                   /note="Cleavage (non-hydrolytic)"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         43
FT                   /note="Pyruvic acid (Ser)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   157 AA;  17165 MW;  F39D137F73862679 CRC64;
     MALIPKEVFF VSGVGRHEDE LVSFELALRD AGIERFNLVP VSSIVPPGCR VVSKEEGLRK
     LSPGQIVFCV MARYASNVEG REIFASVGAA FPEDKDMNGY IAEHSGEWYE GAEQHAKRLA
     EEMLKTQGSK VARTFAITAR GKVKEFTTAV AAAVFVI
//