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HAMAP rule MF_01298

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General rule information [?]

Accession MF_01298
Dates 16-JAN-2009 (Created)
1-JUN-2023 (Last updated, Version 14)
Name ArgDC
Scope(s) Archaea
Template(s) Q9UWU1 (ARGDC_SACS2); [ Recover all ]
Triggered by HAMAP; MF_01298 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier ARGDC
Protein name RecName: Full=Arginine decarboxylase proenzyme;
AltName: Full=Pyruvoyl-dependent arginine decarboxylase;
RecName: Full=Arginine decarboxylase beta chain;
RecName: Full=Arginine decarboxylase alpha chain;
                 Flags: Precursor;

Comments [?]

FUNCTIONSpecifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity.
CATALYTIC ACTIVITY Reaction=H(+) + L-arginine = agmatine + CO2; Xref=Rhea:RHEA:17641, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32682, ChEBI:CHEBI:58145; EC=;
COFACTOR Name=pyruvate; Xref=ChEBI:CHEBI:15361; Note=Binds 1 pyruvoyl group covalently per subunit.;
PATHWAYAmine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1.
SUBUNITHeterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers.
PTMIs synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.
SIMILARITYBelongs to the prokaryotic AdoMetDC family. Type 1 subfamily.

Keywords [?]

Gene Ontology [?]

GO:0008792; Molecular function:arginine decarboxylase activity
GO:0006527; Biological process:arginine catabolic process
GO:0006596; Biological process:polyamine biosynthetic process

Cross-references [?]

Pfam PF02675; AdoMet_dc; 1;
NCBIfam TIGR03330; SAM_DCase_Bsu; 1;

Features [?]

Key From To Description Tag Condition FTGroup
CHAIN Nter 81 /note="Arginine decarboxylase beta chain"
CHAIN 82 Cter /note="Arginine decarboxylase alpha chain"
ACT_SITE 82 82 /note="Schiff-base intermediate with substrate; via pyruvic acid" S
ACT_SITE 87 87 /note="Proton acceptor; for processing activity" H
ACT_SITE 102 102 /note="Proton donor; for catalytic activity" C
SITE 81 82 /note="Cleavage (non-hydrolytic); by autolysis" E-S
MOD_RES 82 82 /note="Pyruvic acid (Ser); by autocatalysis" S

Additional information [?]

Size range 126-144 amino acids
Related rules MF_00464
Fusion Nter: None Cter: 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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