AC   MF_01298;
DC   Protein; auto
TR   HAMAP; MF_01298; -; 1; level=0
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Names: ArgDC
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ID   ARGDC
DE   RecName: Full=Arginine decarboxylase proenzyme;
DE            Short=ADC;
DE            Short=ArgDC;
DE            EC=4.1.1.19;
DE   AltName: Full=Pyruvoyl-dependent arginine decarboxylase;
DE   Contains:
DE     RecName: Full=Arginine decarboxylase beta chain;
DE   Contains:
DE     RecName: Full=Arginine decarboxylase alpha chain;
DE   Flags: Precursor;
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CC   -!- FUNCTION: Specifically catalyzes the decarboxylation of L-arginine to
CC       agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC)
CC       activity.
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;
CC       Note=Binds 1 pyruvoyl group covalently per subunit.;
CC   -!- PATHWAY: Amine and polyamine biosynthesis; agmatine biosynthesis;
CC       agmatine from L-arginine: step 1/1.
CC   -!- SUBUNIT: Heterooctamer of four alpha and four beta chains arranged as a
CC       tetramer of alpha/beta heterodimers.
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.
CC   -!- SIMILARITY: Belongs to the prokaryotic AdoMetDC family. Type 1
CC       subfamily.
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DR   Pfam; PF02675; AdoMet_dc; 1; trigger=no
DR   NCBIfam; TIGR03330; SAM_DCase_Bsu; 1; trigger=no
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KW   Autocatalytic cleavage
KW   Decarboxylase
KW   Lyase
KW   Polyamine biosynthesis
KW   Pyruvate
KW   Schiff base
KW   Zymogen
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GO   GO:0008792; F:arginine decarboxylase activity
GO   GO:0006527; P:arginine catabolic process
GO   GO:0006596; P:polyamine biosynthetic process
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FT   From: ARGDC_SACS2 (Q9UWU1)
FT   CHAIN           Nter..81
FT                   /note="Arginine decarboxylase beta chain"
FT   CHAIN           82..Cter
FT                   /note="Arginine decarboxylase alpha chain"
FT   ACT_SITE        82
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid"
FT   Condition: S
FT   ACT_SITE        87
FT                   /note="Proton acceptor; for processing activity"
FT   Condition: H
FT   ACT_SITE        102
FT                   /note="Proton donor; for catalytic activity"
FT   Condition: C
FT   SITE            81..82
FT                   /note="Cleavage (non-hydrolytic); by autolysis"
FT   Condition: E-S
FT   MOD_RES         82
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT   Condition: S
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Size: 126-144;
Related: MF_00464;
Template: Q9UWU1;
Scope:
 Archaea; Thermoproteota
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: Prokaryotic AdoMetDC type 1 subfamily comprises 2 branches, one with S-adenosylmethionine
 decarboxylase (AdoMetDC) activity (see MF_00464) and the other with arginine decarboxylase (ArgDC)
 activity (this rule, MF_01298). Thermoproteota possess 2 paralogs, one protein from each branch associated
 with each function.
 Two nonhomologous classes of pyruvoyl-dependent ArgDC enzymes exist: one found in euryarchaea and some
 bacteria (pdaD, MF_01404) and the second one described here, found only in Thermoproteota. The Thermoproteota
 (CENSY, NITMS, THEPD) that do not possess a member of the family described here have homologs of the
 euryarchaeal ArgDC.
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# Revision 1.14 2023/06/01
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