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| Annotation rule MF_01298 |
General rule information
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| Accession | MF_01298 |
| Dates | 16-JAN-2009 (Created) 19-NOV-2019 (Last updated, Version 12) |
| Name | ArgDC |
| Scope | Archaea; Crenarchaeota |
| Template | Q9UWU1 (ARGDC_SACS2) |
| Triggered by |
Propagated annotation
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Identifier, protein and gene names
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| Identifier |
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| Protein name |
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Comments
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| Function | Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity. |
| Catalytic activity | RHEA:17641: H(+) + L-arginine = agmatine + CO2
EC 4.1.1.19 |
| Cofactor | pyruvate 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.
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 | Arginine decarboxylase beta chain | |||||||||
| CHAIN | 82 | Cter | Arginine decarboxylase alpha chain | |||||||||
| ACT_SITE | 82 | 82 | Schiff-base intermediate with substrate; via pyruvic acid | S | ||||||||
| ACT_SITE | 87 | 87 | Proton acceptor; for processing activity | H | ||||||||
| ACT_SITE | 102 | 102 | Proton donor; for catalytic activity | C | ||||||||
| SITE | 81 | 82 | Cleavage (non-hydrolytic); by autolysis | E-S | ||||||||
| MOD_RES | 82 | 82 | Pyruvic acid (Ser); by autocatalysis | S | ||||||||
Additional information
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| Size range | 126-144 amino acids |
| Related rules | MF_00464 (SPEH) |
| Fusion | 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). Crenarchaeota 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 crenarchaea. The crenarchaea (CENSY, NITMS, THEPD) that do not possess a member of the family described here have homologs of the euryarchaeal ArgDC. |