HAMAP

Accession	MF_01298
Dates	16-JAN-2009 (Created) 18-AUG-2010 (Last updated, Version 5)

Data class

Protein

Predictors

HAMAP; MF_01298; [distribution of match scores in UniProtKB];[seed alignment for MF_01298]

Names

ArgDC

Identifier

ARGDC

Protein name

RecName: Full=Arginine decarboxylase proenzyme; Short=ADC; Short=ArgDC; EC=4.1.1.19; AltName: Full=Pyruvoyl-dependent arginine decarboxylase; RecName: Full=Arginine decarboxylase beta chain; RecName: Full=Arginine decarboxylase alpha chain; Flags: Precursor;

FUNCTION: Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity (By similarity).

CATALYTIC ACTIVITY: L-arginine = agmatine + CO(2).

COFACTOR: Pyruvoyl group (By similarity).

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 (By similarity).

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 (By similarity).

SIMILARITY: Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.

Pfam	PF02675; AdoMet_dc; 1;
TIGRFAMs	TIGR03330; SAM_DCase_Bsu; 1;

Autocatalytic cleavage, Decarboxylase, Lyase, Polyamine biosynthesis, Pyruvate, Schiff base, Zymogen.

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

From: ARGDC_SULSO (Q9UWU1)
Key		From		To		Description		Condition		FTGroup
CHAIN		Nter		81		Arginine decarboxylase beta chain (By similarity)
CHAIN		82		Cter		Arginine decarboxylase alpha chain (By similarity)
ACT_SITE		82		82		Schiff-base intermediate with substrate; via pyruvic acid (By similarity)		S
ACT_SITE		87		87		Proton acceptor; for processing activity (By similarity)		H
ACT_SITE		102		102		Proton donor; for catalytic activity (By similarity)		C
SITE		81		82		Cleavage (non-hydrolytic); by autolysis (By similarity)		E-S
MOD_RES		82		82		Pyruvic acid (Ser); by autocatalysis (By similarity)		S

Size range:	126-144 amino acids
Related UniRules:	MF_00464 (SPEH)
Template:	Q9UWU1 (ARGDC_SULSO)
Scope:	Archaea; Crenarchaeota
Fusion:	Nter: None; Cter: None
Duplicate:	None
Plasmid encoded:	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.