Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

C3NEW5 (ARGDC_SULIY) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 30. 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:YG5714_1592
OrganismSulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1) [Complete proteome] [HAMAP]
Taxonomic identifier439386 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

Protein attributes

Sequence length134 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
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 – 8181Arginine decarboxylase beta chain By similarity
PRO_1000214235
Chain82 – 13453Arginine decarboxylase alpha chain By similarity
PRO_1000214236

Sites

Active site821Schiff-base intermediate with substrate; via pyruvic acid By similarity
Active site871Proton acceptor; for processing activity By similarity
Active site1021Proton donor; for catalytic activity By similarity
Site81 – 822Cleavage (non-hydrolytic); by autolysis By similarity

Amino acid modifications

Modified residue821Pyruvic acid (Ser); by autocatalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
C3NEW5 [UniParc].

Last modified June 16, 2009. Version 1.
Checksum: B1489B1B0017E590

FASTA13415,219
        10         20         30         40         50         60 
MSEQEVLQKN NSPEGKEDRI IGKHVFGNLY DIDAERLNDK EFLEKLVLEA VNIAHMKLVE 

        70         80         90        100        110        120 
IKAWSFGGKK GGVSVIALVE ESHIALHTWN EYNYATLDVY TCGEDSDPQS AFAHIVNALN 

       130 
PKRYQMFYAD RSSQ 

« Hide

References

[1]"Biogeography of the Sulfolobus islandicus pan-genome."
Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.
Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Y.G.57.14 / Yellowstone #1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001403 Genomic DNA. Translation: ACP45854.1.
RefSeqYP_002837776.1. NC_012622.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING439386.YG5714_1592.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACP45854; ACP45854; YG5714_1592.
GeneID7806104.
KEGGsiy:YG5714_1592.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1586.
HOGENOMHOG000216579.
KOK01611.
OMAHIANMHL.

Enzyme and pathway databases

BioCycSISL439386:GHF0-1649-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_SULIY
AccessionPrimary (citable) accession number: C3NEW5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: June 16, 2009
Last modified: May 14, 2014
This is version 30 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