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A8MBV3 (ARGDC_CALMQ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 44. 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:Cmaq_0451
OrganismCaldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 / IC-167) [Complete proteome] [HAMAP]
Taxonomic identifier397948 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaeCaldivirga

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 8181Arginine decarboxylase beta chain By similarity
PRO_0000364111
Chain82 – 13453Arginine decarboxylase alpha chain By similarity
PRO_0000364112

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
A8MBV3 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: BFFCD14C36EE792E

FASTA13415,053
        10         20         30         40         50         60 
MLQQQESPIP RLGVGEEGVV GRHVFGEVWG VNDKLLQDDE YLKNLVIKAA EVANMHLVDV 

        70         80         90        100        110        120 
KVWRFGGGDK GGVSVIALVL ESHIAIHTWP AYNYATIDVY TCGEHSRPWD AYDYIIKQLN 

       130 
PKTFTKTIVD RSSK 

« Hide

References

[1]"Complete sequence of Caldivirga maquilingensis IC-167."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Ivanova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M., Saltikov C., House C.H., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700844 / DSM 13496 / JCM 10307 / IC-167.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000852 Genomic DNA. Translation: ABW01296.1.
RefSeqYP_001540286.1. NC_009954.1.

3D structure databases

ProteinModelPortalA8MBV3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING397948.Cmaq_0451.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABW01296; ABW01296; Cmaq_0451.
GeneID5709779.
KEGGcma:Cmaq_0451.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1586.
HOGENOMHOG000216579.
KOK01611.
OMAAYNYATI.
ProtClustDBPRK00458.

Enzyme and pathway databases

BioCycCMAQ397948:GH9M-462-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_CALMQ
AccessionPrimary (citable) accession number: A8MBV3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: December 4, 2007
Last modified: February 19, 2014
This is version 44 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