ARGDC_HYPBU
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 25-MAY-2022, entry version 81.
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; Crenarchaeota; 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;
CC Evidence={ECO:0000255|HAMAP-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 OMA; VYTCGEH; -.
DR OrthoDB; 106151at2157; -.
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 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 PANTHER; PTHR33866; PTHR33866; 1.
DR Pfam; PF02675; AdoMet_dc; 1.
DR SUPFAM; SSF56276; SSF56276; 1.
DR TIGRFAMs; TIGR03330; SAM_DCase_Bsu; 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
