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Reviewed, UniProtKB/Swiss-Prot A4YH98 (ARGDC_METS5)

Last modified November 3, 2009. Version 22. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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: Msed_1645
OrganismMetallosphaera sedula (strain ATCC 51363 / DSM 5348) [Complete proteome] [HAMAP]
Taxonomic identifier399549 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeMetallosphaera

Protein attributes

Sequence length128 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.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7575Arginine decarboxylase beta chain By similarity
PRO_0000364117
Chain76 – 12853Arginine decarboxylase alpha chain By similarity
PRO_0000364118

Sites

Active site761Schiff-base intermediate with substrate; via pyruvic acid By similarity
Active site811Proton acceptor; for processing activity By similarity
Active site961Proton donor; for catalytic activity By similarity
Site75 – 762Cleavage (non-hydrolytic); by autolysis By similarity

Amino acid modifications

Modified residue761Pyruvic acid (Ser); by autocatalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
A4YH98-1 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: 1CAC28ABABA66EE3

FASTA12814,523
        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 

« Hide

References

[1]"Complete sequence of Metallosphaera sedula DSM 5348."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Han C., Detter J.C., Bruce D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Mikhailova N., Maezato Y., Auernik K.S., Kelly R.M., Blum P., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000682 Genomic DNA. Translation: ABP95800.1.
RefSeqYP_001191724.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA4YH98.

Genome annotation databases

GeneID5104850.
GenomeReviewsGene locus Msed_1645 in contig CP000682_GR.
KEGGmse:Msed_1645.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMASHIALHT.

Family and domain databases

HAMAPMF_01298.
[Tree]
InterProIPR003826. S-AdoMet_decarboxylase-bac/arc.
IPR017716. S-AdoMet_deCOase_pro-enz.
[Graphical view]
PfamPF02675. AdoMet_dc. 1 hit.
[Graphical view]
TIGRFAMsTIGR03330. SAM_DCase_Bsu. 1 hit.
ProtoNetSearch...

Entry information

Entry nameARGDC_METS5
AccessionPrimary (citable) accession number: A4YH98
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: May 29, 2007
Last modified: November 3, 2009
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents