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A2BM05 (ARGDC_HYPBU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arginine decarboxylase proenzyme

Short name=ADC
Short name=ArgDC
EC=4.1.1.19
Alternative name(s):
Pyruvoyl-dependent arginine decarboxylase
Gene names
Ordered Locus Names:Hbut_1182
OrganismHyperthermus butylicus (strain DSM 5456 / JCM 9403) [Reference proteome] [HAMAP]
Taxonomic identifier415426 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiDesulfurococcalesPyrodictiaceaeHyperthermus

Protein attributes

Sequence length142 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred 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-Rule MF_01298

Catalytic activity

L-arginine = agmatine + CO2. HAMAP-Rule MF_01298

Cofactor

Pyruvoyl group By similarity. HAMAP-Rule MF_01298

Pathway

Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1. HAMAP-Rule 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-Rule MF_01298

Sequence similarities

Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.

Ontologies

Keywords
   Biological processPolyamine biosynthesis
   LigandPyruvate
Schiff base
   Molecular functionDecarboxylase
Lyase
   PTMAutocatalytic cleavage
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processarginine catabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

polyamine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionarginine decarboxylase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 8080Arginine decarboxylase beta chain By similarity
PRO_0000364113
Chain81 – 14262Arginine decarboxylase alpha chain By similarity
PRO_0000364114

Sites

Active site811Schiff-base intermediate with substrate; via pyruvic acid By similarity
Active site861Proton acceptor; for processing activity By similarity
Active site1011Proton donor; for catalytic activity By similarity
Site80 – 812Cleavage (non-hydrolytic); by autolysis By similarity

Amino acid modifications

Modified residue811Pyruvic acid (Ser); by autocatalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
A2BM05 [UniParc].

Last modified February 20, 2007. Version 1.
Checksum: A85E0FA247A6D17E

FASTA14216,010
        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 

« Hide

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(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 5456 / JCM 9403.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000493 Genomic DNA. Translation: ABM81016.1.
RefSeqYP_001013361.1. NC_008818.1.

3D structure databases

ProteinModelPortalA2BM05.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING415426.Hbut_1182.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM81016; ABM81016; Hbut_1182.
GeneID4782734.
KEGGhbu:Hbut_1182.

Phylogenomic databases

eggNOGCOG1586.
HOGENOMHOG000216579.
KOK01611.
OMACGEHSDP.
ProtClustDBCLSK964544.

Enzyme and pathway databases

BioCycHBUT415426:GC56-1182-MONOMER.
UniPathwayUPA00186; UER00284.

Family and domain databases

Gene3D3.60.90.10. 1 hit.
HAMAPMF_00464. AdoMetDC_1.
MF_01298. ArgDC.
InterProIPR003826. AdoMetDC_fam_prok.
IPR027549. ArgDC.
IPR016067. S-AdoMet_deCO2ase_core.
IPR017716. S-AdoMet_deCOase_pro-enz.
[Graphical view]
PfamPF02675. AdoMet_dc. 1 hit.
[Graphical view]
SUPFAMSSF56276. SSF56276. 1 hit.
TIGRFAMsTIGR03330. SAM_DCase_Bsu. 1 hit.
ProtoNetSearch...

Entry information

Entry nameARGDC_HYPBU
AccessionPrimary (citable) accession number: A2BM05
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: February 20, 2007
Last modified: February 19, 2014
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways