ID   ARGDC_HYPBU             Reviewed;         142 AA.
AC   A2BM05;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=Arginine decarboxylase proenzyme {ECO:0000255|HAMAP-Rule:MF_01298};
DE            Short=ADC {ECO:0000255|HAMAP-Rule:MF_01298};
DE            Short=ArgDC {ECO:0000255|HAMAP-Rule:MF_01298};
DE            EC=4.1.1.19 {ECO:0000255|HAMAP-Rule:MF_01298};
DE   AltName: Full=Pyruvoyl-dependent arginine decarboxylase {ECO:0000255|HAMAP-Rule:MF_01298};
DE   Contains:
DE     RecName: Full=Arginine decarboxylase beta chain {ECO:0000255|HAMAP-Rule:MF_01298};
DE   Contains:
DE     RecName: Full=Arginine decarboxylase alpha chain {ECO:0000255|HAMAP-Rule:MF_01298};
DE   Flags: Precursor;
GN   OrderedLocusNames=Hbut_1182;
OS   Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5).
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC   Hyperthermus.
OX   NCBI_TaxID=415426;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5456 / JCM 9403 / PLM1-5;
RX   PubMed=17350933; DOI=10.1155/2007/745987;
RA   Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M.,
RA   She Q., Garrett R.A., Klenk H.-P.;
RT   "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide
RT   fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.";
RL   Archaea 2:127-135(2007).
CC   -!- FUNCTION: Specifically catalyzes the decarboxylation of L-arginine to
CC       agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC)
CC       activity. {ECO:0000255|HAMAP-Rule:MF_01298}.
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_01298};
CC   -!- COFACTOR:
CC       Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01298};
CC       Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01298};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; agmatine biosynthesis;
CC       agmatine from L-arginine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01298}.
CC   -!- SUBUNIT: Heterooctamer of four alpha and four beta chains arranged as a
CC       tetramer of alpha/beta heterodimers. {ECO:0000255|HAMAP-Rule:MF_01298}.
CC   -!- PTM: Is synthesized initially as an inactive proenzyme. Formation of
CC       the active enzyme involves a self-maturation process in which the
CC       active site pyruvoyl group is generated from an internal serine residue
CC       via an autocatalytic post-translational modification. Two non-identical
CC       subunits are generated from the proenzyme in this reaction, and the
CC       pyruvate is formed at the N-terminus of the alpha chain, which is
CC       derived from the carboxyl end of the proenzyme. The post-translation
CC       cleavage follows an unusual pathway, termed non-hydrolytic serinolysis,
CC       in which the side chain hydroxyl group of the serine supplies its
CC       oxygen atom to form the C-terminus of the beta chain, while the
CC       remainder of the serine residue undergoes an oxidative deamination to
CC       produce ammonia and the pyruvoyl group blocking the N-terminus of the
CC       alpha chain. {ECO:0000255|HAMAP-Rule:MF_01298}.
CC   -!- SIMILARITY: Belongs to the prokaryotic AdoMetDC family. Type 1
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01298}.
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DR   EMBL; CP000493; ABM81016.1; -; Genomic_DNA.
DR   RefSeq; WP_011822334.1; NC_008818.1.
DR   AlphaFoldDB; A2BM05; -.
DR   SMR; A2BM05; -.
DR   STRING; 415426.Hbut_1182; -.
DR   EnsemblBacteria; ABM81016; ABM81016; Hbut_1182.
DR   GeneID; 4782734; -.
DR   KEGG; hbu:Hbut_1182; -.
DR   eggNOG; arCOG00279; Archaea.
DR   HOGENOM; CLU_125470_2_1_2; -.
DR   OrthoDB; 114016at2157; -.
DR   UniPathway; UPA00186; UER00284.
DR   Proteomes; UP000002593; Chromosome.
DR   GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006527; P:arginine catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006596; P:polyamine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.60.90.10; S-adenosylmethionine decarboxylase; 1.
DR   HAMAP; MF_00464; AdoMetDC_1; 1.
DR   HAMAP; MF_01298; ArgDC; 1.
DR   InterPro; IPR003826; AdoMetDC_fam_prok.
DR   InterPro; IPR027549; ArgDC.
DR   InterPro; IPR016067; S-AdoMet_deCO2ase_core.
DR   InterPro; IPR017716; S-AdoMet_deCOase_pro-enz.
DR   NCBIfam; TIGR03330; SAM_DCase_Bsu; 1.
DR   PANTHER; PTHR33866; S-ADENOSYLMETHIONINE DECARBOXYLASE PROENZYME; 1.
DR   PANTHER; PTHR33866:SF2; S-ADENOSYLMETHIONINE DECARBOXYLASE PROENZYME; 1.
DR   Pfam; PF02675; AdoMet_dc; 1.
DR   SUPFAM; SSF56276; S-adenosylmethionine decarboxylase; 1.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage; Decarboxylase; Lyase; Polyamine biosynthesis;
KW   Pyruvate; Reference proteome; Schiff base; Zymogen.
FT   CHAIN           1..80
FT                   /note="Arginine decarboxylase beta chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01298"
FT                   /id="PRO_0000364113"
FT   CHAIN           81..142
FT                   /note="Arginine decarboxylase alpha chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01298"
FT                   /id="PRO_0000364114"
FT   ACT_SITE        81
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01298"
FT   ACT_SITE        86
FT                   /note="Proton acceptor; for processing activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01298"
FT   ACT_SITE        101
FT                   /note="Proton donor; for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01298"
FT   SITE            80..81
FT                   /note="Cleavage (non-hydrolytic); by autolysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01298"
FT   MOD_RES         81
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01298"
SQ   SEQUENCE   142 AA;  16010 MW;  A85E0FA247A6D17E CRC64;
     MAVQQNVKKG GREAGGDLIV GKHVYGNLYG VDEEKLWDEE LLKDIVVEAA RVANMNLVDI
     KTWKFTGFHG GVSVIALVLE SHISIHTWPD YGYATVDVYT CGANSDPWKA FNYIVLKLKP
     RYYIVHYADR SSIPGYTESE KR
//