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Annotation rule MF_01298
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General rule information [?]

Accession MF_01298
Dates 16-JAN-2009 (Created)
19-NOV-2019 (Last updated, Version 12)
Name ArgDC
Scope
Archaea; Crenarchaeota
Template Q9UWU1 (ARGDC_SACS2)

Propagated annotation [?]


Identifier, protein and gene names [?]

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 [?]

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 [?]


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;
TIGRFAMs TIGR03330; SAM_DCase_Bsu; 1;

Features [?]

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 [?]

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.