Reviewed, UniProtKB/Swiss-Prot A2BM05 (ARGDC_HYPBU)

Names and origin

Protein names

Recommended name:
    Arginine decarboxylase proenzyme
      Short name=ArgDC
      Short name=ADC
    EC=4.1.1.19
Alternative name(s):
    Pyruvoyl-dependent arginine decarboxylase
Cleaved into the following 2 chains:
    1- Recommended name:
            Arginine decarboxylase beta chain
    2- Recommended name:
            Arginine decarboxylase alpha chain

Gene names

Ordered Locus Names:

Hbut_1182

Organism

Hyperthermus butylicus (strain DSM 5456 / JCM 9403) [Complete proteome] [HAMAP]

Taxonomic identifier

415426 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Pyrodictiaceae › Hyperthermus

Protein attributes

Sequence length	142 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity By similarity.
Catalytic activity	L-arginine = agmatine + CO2. HAMAP MF_01298
Cofactor	Pyruvoyl group By similarity.
Pathway	Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1. HAMAP MF_01298
Subunit structure	Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers By similarity.
Post-translational modification	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.
Sequence similarities	Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.

Ontologies

Keywords
Biological process	Polyamine biosynthesis
Ligand	Pyruvate Schiff base
Molecular function	Decarboxylase Lyase
PTM	Autocatalytic cleavage Zymogen
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	arginine catabolic process Inferred from electronic annotation. Source: HAMAP spermidine biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular function	adenosylmethionine decarboxylase activity Inferred from electronic annotation. Source: InterPro arginine decarboxylase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 80	80	Arginine decarboxylase beta chain By similarity		PRO_0000364113
	Chain	81 – 142	62	Arginine decarboxylase alpha chain By similarity		PRO_0000364114
Sites
	Active site	81	1	Schiff-base intermediate with substrate; via pyruvic acid By similarity
	Active site	86	1	Proton acceptor; for processing activity By similarity
	Active site	101	1	Proton donor; for catalytic activity By similarity
	Site	80 – 81	2	Cleavage (non-hydrolytic); by autolysis By similarity
Amino acid modifications
	Modified residue	81	1	Pyruvic acid (Ser); by autocatalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	A2BM05-1 [UniParc]. Last modified February 20, 2007. Version 1. Checksum: A85E0FA247A6D17E	FASTA	142	16,010
	10 20 30 40 50 60 MAVQQNVKKG GREAGGDLIV GKHVYGNLYG VDEEKLWDEE LLKDIVVEAA RVANMNLVDI 70 80 90 100 110 120 KTWKFTGFHG GVSVIALVLE SHISIHTWPD YGYATVDVYT CGANSDPWKA FNYIVLKLKP 130 140 RYYIVHYADR SSIPGYTESE KR

References

[1]

"The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C." Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M., She Q., Garrett R.A., Klenk H.-P. Archaea 2:127-135(2006) [PubMed: 17350933] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000493 Genomic DNA. Translation: ABM81016.1.
RefSeq	YP_001013361.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A2BM05.
Genome annotation databases
GeneID	4782734.
GenomeReviews	Gene locus Hbut_1182 in contig CP000493_GR.
KEGG	hbu:Hbut_1182.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	YTESEKR.
Family and domain databases
HAMAP	MF_01298. [Tree]
InterPro	IPR003826. S-AdoMet_decarboxylase-bac/arc. IPR016067. S-AdoMet_deCO2ase_core. IPR017716. S-AdoMet_deCOase_pro-enz. [Graphical view]
Gene3D	G3DSA:3.60.90.10. SAM_decarbox. 1 hit.
Pfam	PF02675. AdoMet_dc. 1 hit. [Graphical view]
TIGRFAMs	TIGR03330. SAM_DCase_Bsu. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ARGDC_HYPBU

Accession

Primary (citable) accession number: A2BM05

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 10, 2009
Last sequence update:	February 20, 2007
Last modified:	November 3, 2009
This is version 23 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)