A4YH98 (ARGDC_METS5) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Arginine decarboxylase proenzyme
Short name=ADC
Short name=ArgDC
EC=4.1.1.19

Alternative name(s):
Pyruvoyl-dependent arginine decarboxylase

Cleaved into the following 2 chains:

1. Arginine decarboxylase beta chain
2. Arginine decarboxylase alpha chain

Gene names

Ordered Locus Names:

Msed_1645

Organism

Metallosphaera sedula (strain ATCC 51363 / DSM 5348) [Complete proteome] [HAMAP]

Taxonomic identifier

399549 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Metallosphaera

Protein attributes

Sequence length	128 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.
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	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: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 75	75	Arginine decarboxylase beta chain By similarity		PRO_0000364117
	Chain	76 – 128	53	Arginine decarboxylase alpha chain By similarity		PRO_0000364118
Sites
	Active site	76	1	Schiff-base intermediate with substrate; via pyruvic acid By similarity
	Active site	81	1	Proton acceptor; for processing activity By similarity
	Active site	96	1	Proton donor; for catalytic activity By similarity
	Site	75 – 76	2	Cleavage (non-hydrolytic); by autolysis By similarity
Amino acid modifications
	Modified residue	76	1	Pyruvic acid (Ser); by autocatalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	A4YH98 [UniParc]. Last modified May 29, 2007. Version 1. Checksum: 1CAC28ABABA66EE3	FASTA	128	14,523
	10 20 30 40 50 60 MSEQVTFQSH EDRIVGKHVF GNLYDIDPED LNNEQLLKDL VLKAVEIAHM NLVEAKSWSF 70 80 90 100 110 120 GGKKGGVSVI ALIEESHIAL HTWNEYNYAT LDVYTCGEDS DPQAAFKFIV EALKPRRYQV FFADRSSS

References

[1]

"The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism." Auernik K.S., Maezato Y., Blum P.H., Kelly R.M. Appl. Environ. Microbiol. 74:682-692(2008) [PubMed: 18083856] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51363 / DSM 5348.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000682 Genomic DNA. Translation: ABP95800.1.
RefSeq	YP_001191724.1. NC_009440.1.
3D structure databases
ProteinModelPortal	A4YH98.
ModBase	Search...
Protein-protein interaction databases
STRING	A4YH98.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5104850.
GenomeReviews	Gene locus Msed_1645 in contig CP000682_GR.
KEGG	mse:Msed_1645.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	arNOG11873.
HOGENOM	HBG485559.
OMA	FKAMEYI.
ProtClustDB	PRK00458.
Enzyme and pathway databases
BioCyc	MSED399549:MSED_1645-MONOMER.
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.
KO	K01611.
Pfam	PF02675. AdoMet_dc. 1 hit. [Graphical view]
SUPFAM	SSF56276. S-AdenosylMet_decarbase_core. 1 hit.
TIGRFAMs	TIGR03330. SAM_DCase_Bsu. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ARGDC_METS5

Accession

Primary (citable) accession number: A4YH98

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 10, 2009
Last sequence update:	May 29, 2007
Last modified:	November 16, 2011
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program