HAMAP rule MF_01298
General rule information
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| Accession | MF_01298 |
| Dates | 16-JAN-2009 (Created)
3-SEP-2024 (Last updated, Version 15) |
| Name | ArgDC |
| Scope(s) |
Archaea Thermoproteota |
| Template(s) | Q9UWU1 (ARGDC_SACS2); [ Recover all ] |
| Triggered by |
HAMAP; MF_01298 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | ARGDC |
| Protein name | RecName: Full=Arginine decarboxylase proenzyme; Short=ADC; Short=ArgDC; EC=4.1.1.19; AltName: Full=Pyruvoyl-dependent arginine decarboxylase; Contains: RecName: Full=Arginine decarboxylase beta chain; Contains: RecName: Full=Arginine decarboxylase alpha chain; Flags: Precursor; |
Comments
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| FUNCTION | Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity. |
| CATALYTIC ACTIVITY | Reaction=L-arginine + H(+) = agmatine + CO2; Xref=Rhea:RHEA:17641, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32682, ChEBI:CHEBI:58145; EC=4.1.1.19; |
| COFACTOR | Name=pyruvate; Xref=ChEBI:CHEBI:15361; Note=Binds 1 pyruvoyl group covalently per subunit.; |
| PATHWAY | Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1. |
| SUBUNIT | Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers. |
| PTM | Is 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. |
| SIMILARITY | Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily. |
Keywords
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Gene Ontology
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| GO:0008792; Molecular function:arginine decarboxylase activity |
| GO:0006527; Biological process:arginine catabolic process |
| GO:0006596; Biological process:polyamine biosynthetic process |
Cross-references
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Features
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| From: ARGDC_SACS2 (Q9UWU1) | ||||||||||||
| 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
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| 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. |