Reviewed, UniProtKB/Swiss-Prot Q4J932 (ARGDC_SULAC)

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:

Saci_1363

Organism

Sulfolobus acidocaldarius [Complete proteome] [HAMAP]

Taxonomic identifier

2285 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Sulfolobus

Protein attributes

Sequence length	130 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. HAMAP MF_01298
Catalytic activity	L-arginine = agmatine + CO2. HAMAP MF_01298
Cofactor	Pyruvoyl group By similarity. HAMAP MF_01298
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. HAMAP MF_01298
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. HAMAP MF_01298
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 – 77	77	Arginine decarboxylase beta chain By similarity		PRO_0000041966
	Chain	78 – 130	53	Arginine decarboxylase alpha chain By similarity		PRO_0000041967
Sites
	Active site	78	1	Schiff-base intermediate with substrate; via pyruvic acid By similarity
	Active site	83	1	Proton acceptor; for processing activity By similarity
	Active site	98	1	Proton donor; for catalytic activity By similarity
	Site	77 – 78	2	Cleavage (non-hydrolytic); by autolysis By similarity
Amino acid modifications
	Modified residue	78	1	Pyruvic acid (Ser); by autocatalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4J932-1 [UniParc]. Last modified August 2, 2005. Version 1. Checksum: 22A84EFDAD722E9F	FASTA	130	14,623
	10 20 30 40 50 60 MSQQLSSQTP SNQDRIVGKH VFGNLYDIDD KLLMDKDLLE GLVLEAVKIA KMNLVEIKSW 70 80 90 100 110 120 SFGGKKGGVS VIALVEESHI ALHTWNEYKY ATLDVYTCGV DSNPQAAFEF IVSNLKPKRH 130 QMFFADRSSE

References

[1]

"The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota." Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E., Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A. J. Bacteriol. 187:4992-4999(2005) [PubMed: 15995215] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33909 / DSM 639 / IFO 15157 / JCM 8929 / NCIB 11770.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000077 Genomic DNA. Translation: AAY80698.1.
RefSeq	YP_255991.1.
3D structure databases
SMR	Q4J932. Positions 16-129.
ModBase	Search...
Genome annotation databases
GeneID	3472928.
GenomeReviews	Gene locus Saci_1363 in contig CP000077_GR.
KEGG	sai:Saci_1363.
NMPDR	fig|330779.3.peg.129.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG485559.
OMA	ARECIAP.
Enzyme and pathway databases
BioCyc	SACI330779:SACI_1363-MONOMER.
BRENDA	4.1.1.50. 434.
Family and domain databases
HAMAP	MF_01298. ArgDC. [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_SULAC

Accession

Primary (citable) accession number: Q4J932

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2005
Last sequence update:	August 2, 2005
Last modified:	February 9, 2010
This is version 36 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)