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Protein

Arginine decarboxylase proenzyme

Gene

Pars_0747

Organism
Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321)
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

Pathway:iagmatine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes agmatine from L-arginine.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Arginine decarboxylase proenzyme (Pars_0747)
This subpathway is part of the pathway agmatine biosynthesis, which is itself part of Amine and polyamine biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes agmatine from L-arginine, the pathway agmatine biosynthesis and in Amine and polyamine biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei80 – 812Cleavage (non-hydrolytic); by autolysisUniRule annotation
Active sitei81 – 811Schiff-base intermediate with substrate; via pyruvic acidUniRule annotation
Active sitei86 – 861Proton acceptor; for processing activityUniRule annotation
Active sitei101 – 1011Proton 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

BioCyciPARS340102:GHGQ-754-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:Pars_0747
OrganismiPyrobaculum arsenaticum (strain DSM 13514 / JCM 11321)
Taxonomic identifieri340102 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum
ProteomesiUP000001567 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8080Arginine decarboxylase beta chainUniRule annotationPRO_0000364119Add
BLAST
Chaini81 – 13353Arginine decarboxylase alpha chainUniRule annotationPRO_0000364120Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei81 – 811Pyruvic 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

Structurei

3D structure databases

ProteinModelPortaliA4WIW6.
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.

A4WIW6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARGGMEARA QTQVKTPVVG KHVYGELYGV DEKLLQDEGR LRQIVIEAAH
60 70 80 90 100
IANMHLVEVN SWRFKGGDKE GVSVIALVLE SHIAIHTWPT YKFATVDVYT
110 120 130
CGEHSDPMSA FRYIVSQLSP KRFTVNYSDR SYK
Length:133
Mass (Da):15,028
Last modified:May 29, 2007 - v1
Checksum:i42904AD3A9496C7E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000660 Genomic DNA. Translation: ABP50333.1.
RefSeqiWP_011900240.1. NC_009376.1.
YP_001152985.1. NC_009376.1.

Genome annotation databases

EnsemblBacteriaiABP50333; ABP50333; Pars_0747.
GeneIDi5054680.
KEGGipas:Pars_0747.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000660 Genomic DNA. Translation: ABP50333.1.
RefSeqiWP_011900240.1. NC_009376.1.
YP_001152985.1. NC_009376.1.

3D structure databases

ProteinModelPortaliA4WIW6.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABP50333; ABP50333; Pars_0747.
GeneIDi5054680.
KEGGipas:Pars_0747.

Phylogenomic databases

eggNOGiCOG1586.
HOGENOMiHOG000216579.
KOiK01611.
OMAiCGEHSDP.

Enzyme and pathway databases

UniPathwayiUPA00186; UER00284.
BioCyciPARS340102:GHGQ-754-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 13514 / JCM 11321.

Entry informationi

Entry nameiARGDC_PYRAR
AccessioniPrimary (citable) accession number: A4WIW6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: May 29, 2007
Last modified: June 24, 2015
This is version 58 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

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.