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Protein

Arginine decarboxylase proenzyme

Gene

Msed_1645

Organism
Metallosphaera sedula (strain ATCC 51363 / DSM 5348)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity.UniRule annotation

Catalytic activityi

L-arginine = agmatine + CO2.UniRule annotation

Cofactori

pyruvateUniRule annotationNote: Binds 1 pyruvoyl group covalently per subunit.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei75 – 762Cleavage (non-hydrolytic); by autolysisUniRule annotation
Active sitei76 – 761Schiff-base intermediate with substrate; via pyruvic acidUniRule annotation
Active sitei81 – 811Proton acceptor; for processing activityUniRule annotation
Active sitei96 – 961Proton donor; for catalytic activityUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Polyamine biosynthesis

Keywords - Ligandi

Pyruvate, Schiff base

Enzyme and pathway databases

BioCyciMSED399549:GH1O-1665-MONOMER.
UniPathwayiUPA00186; UER00284.

Names & Taxonomyi

Protein namesi
Recommended name:
Arginine decarboxylase proenzymeUniRule annotation (EC:4.1.1.19UniRule annotation)
Short name:
ADCUniRule annotation
Short name:
ArgDCUniRule annotation
Alternative name(s):
Pyruvoyl-dependent arginine decarboxylaseUniRule annotation
Cleaved into the following 2 chains:
Arginine decarboxylase beta chainUniRule annotation
Arginine decarboxylase alpha chainUniRule annotation
Gene namesi
Ordered Locus Names:Msed_1645
OrganismiMetallosphaera sedula (strain ATCC 51363 / DSM 5348)
Taxonomic identifieri399549 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeMetallosphaera
ProteomesiUP000000242 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7575Arginine decarboxylase beta chainUniRule annotationPRO_0000364117Add
BLAST
Chaini76 – 12853Arginine decarboxylase alpha chainUniRule annotationPRO_0000364118Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei76 – 761Pyruvic acid (Ser); by autocatalysisUniRule annotation

Post-translational modificationi

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.UniRule annotation

Keywords - PTMi

Autocatalytic cleavage, Zymogen

Interactioni

Subunit structurei

Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers.UniRule annotation

Protein-protein interaction databases

STRINGi399549.Msed_1645.

Structurei

3D structure databases

ProteinModelPortaliA4YH98.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG1586.
HOGENOMiHOG000216579.
KOiK01611.
OMAiCGEHSDP.

Family and domain databases

Gene3Di3.60.90.10. 1 hit.
HAMAPiMF_00464. AdoMetDC_1.
MF_01298. ArgDC.
InterProiIPR003826. AdoMetDC_fam_prok.
IPR027549. ArgDC.
IPR016067. S-AdoMet_deCO2ase_core.
IPR017716. S-AdoMet_deCOase_pro-enz.
[Graphical view]
PfamiPF02675. AdoMet_dc. 1 hit.
[Graphical view]
SUPFAMiSSF56276. SSF56276. 1 hit.
TIGRFAMsiTIGR03330. SAM_DCase_Bsu. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

A4YH98-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEQVTFQSH EDRIVGKHVF GNLYDIDPED LNNEQLLKDL VLKAVEIAHM
60 70 80 90 100
NLVEAKSWSF GGKKGGVSVI ALIEESHIAL HTWNEYNYAT LDVYTCGEDS
110 120
DPQAAFKFIV EALKPRRYQV FFADRSSS
Length:128
Mass (Da):14,523
Last modified:May 29, 2007 - v1
Checksum:i1CAC28ABABA66EE3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000682 Genomic DNA. Translation: ABP95800.1.
RefSeqiWP_012021587.1. NC_009440.1.
YP_001191724.1. NC_009440.1.

Genome annotation databases

EnsemblBacteriaiABP95800; ABP95800; Msed_1645.
GeneIDi5104850.
KEGGimse:Msed_1645.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000682 Genomic DNA. Translation: ABP95800.1.
RefSeqiWP_012021587.1. NC_009440.1.
YP_001191724.1. NC_009440.1.

3D structure databases

ProteinModelPortaliA4YH98.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi399549.Msed_1645.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABP95800; ABP95800; Msed_1645.
GeneIDi5104850.
KEGGimse:Msed_1645.

Phylogenomic databases

eggNOGiCOG1586.
HOGENOMiHOG000216579.
KOiK01611.
OMAiCGEHSDP.

Enzyme and pathway databases

UniPathwayiUPA00186; UER00284.
BioCyciMSED399549:GH1O-1665-MONOMER.

Family and domain databases

Gene3Di3.60.90.10. 1 hit.
HAMAPiMF_00464. AdoMetDC_1.
MF_01298. ArgDC.
InterProiIPR003826. AdoMetDC_fam_prok.
IPR027549. ArgDC.
IPR016067. S-AdoMet_deCO2ase_core.
IPR017716. S-AdoMet_deCOase_pro-enz.
[Graphical view]
PfamiPF02675. AdoMet_dc. 1 hit.
[Graphical view]
SUPFAMiSSF56276. SSF56276. 1 hit.
TIGRFAMsiTIGR03330. SAM_DCase_Bsu. 1 hit.
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 51363 / DSM 5348.

Entry informationi

Entry nameiARGDC_METS5
AccessioniPrimary (citable) accession number: A4YH98
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: May 29, 2007
Last modified: May 27, 2015
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.