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A2BM05

- ARGDC_HYPBU

UniProt

A2BM05 - ARGDC_HYPBU

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Protein
Arginine decarboxylase proenzyme
Gene
Hbut_1182
Organism
Hyperthermus butylicus (strain DSM 5456 / JCM 9403)
Status
Reviewed - 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 By similarity.UniRule annotation

Catalytic activityi

L-arginine = agmatine + CO2.UniRule annotation

Cofactori

Pyruvoyl group By similarity.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei80 – 812Cleavage (non-hydrolytic); by autolysis By similarity
Active sitei81 – 811Schiff-base intermediate with substrate; via pyruvic acid By similarity
Active sitei86 – 861Proton acceptor; for processing activity By similarity
Active sitei101 – 1011Proton donor; for catalytic activity By similarity

GO - Molecular functioni

  1. arginine decarboxylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. arginine catabolic process Source: UniProtKB-HAMAP
  2. polyamine biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Polyamine biosynthesis

Keywords - Ligandi

Pyruvate, Schiff base

Enzyme and pathway databases

BioCyciHBUT415426:GC56-1182-MONOMER.
UniPathwayiUPA00186; UER00284.

Names & Taxonomyi

Protein namesi
Recommended name:
Arginine decarboxylase proenzyme (EC:4.1.1.19)
Short name:
ADC
Short name:
ArgDC
Alternative name(s):
Pyruvoyl-dependent arginine decarboxylase
Cleaved into the following 2 chains:
Gene namesi
Ordered Locus Names:Hbut_1182
OrganismiHyperthermus butylicus (strain DSM 5456 / JCM 9403)
Taxonomic identifieri415426 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiDesulfurococcalesPyrodictiaceaeHyperthermus
ProteomesiUP000002593: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8080Arginine decarboxylase beta chain By similarity
PRO_0000364113Add
BLAST
Chaini81 – 14262Arginine decarboxylase alpha chain By similarity
PRO_0000364114Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei81 – 811Pyruvic acid (Ser); by autocatalysis By similarity

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 By similarity.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 By similarity.

Protein-protein interaction databases

STRINGi415426.Hbut_1182.

Structurei

3D structure databases

ProteinModelPortaliA2BM05.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1586.
HOGENOMiHOG000216579.
KOiK01611.
OMAiHIANMHL.

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.

A2BM05-1 [UniParc]FASTAAdd to Basket

« Hide

MAVQQNVKKG GREAGGDLIV GKHVYGNLYG VDEEKLWDEE LLKDIVVEAA    50
RVANMNLVDI KTWKFTGFHG GVSVIALVLE SHISIHTWPD YGYATVDVYT 100
CGANSDPWKA FNYIVLKLKP RYYIVHYADR SSIPGYTESE KR 142
Length:142
Mass (Da):16,010
Last modified:February 20, 2007 - v1
Checksum:iA85E0FA247A6D17E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000493 Genomic DNA. Translation: ABM81016.1.
RefSeqiWP_011822334.1. NC_008818.1.
YP_001013361.1. NC_008818.1.

Genome annotation databases

EnsemblBacteriaiABM81016; ABM81016; Hbut_1182.
GeneIDi4782734.
KEGGihbu:Hbut_1182.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000493 Genomic DNA. Translation: ABM81016.1 .
RefSeqi WP_011822334.1. NC_008818.1.
YP_001013361.1. NC_008818.1.

3D structure databases

ProteinModelPortali A2BM05.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 415426.Hbut_1182.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABM81016 ; ABM81016 ; Hbut_1182 .
GeneIDi 4782734.
KEGGi hbu:Hbut_1182.

Phylogenomic databases

eggNOGi COG1586.
HOGENOMi HOG000216579.
KOi K01611.
OMAi HIANMHL.

Enzyme and pathway databases

UniPathwayi UPA00186 ; UER00284 .
BioCyci HBUT415426:GC56-1182-MONOMER.

Family and domain databases

Gene3Di 3.60.90.10. 1 hit.
HAMAPi MF_00464. AdoMetDC_1.
MF_01298. ArgDC.
InterProi IPR003826. AdoMetDC_fam_prok.
IPR027549. ArgDC.
IPR016067. S-AdoMet_deCO2ase_core.
IPR017716. S-AdoMet_deCOase_pro-enz.
[Graphical view ]
Pfami PF02675. AdoMet_dc. 1 hit.
[Graphical view ]
SUPFAMi SSF56276. SSF56276. 1 hit.
TIGRFAMsi TIGR03330. SAM_DCase_Bsu. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C."
    Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M., She Q., Garrett R.A., Klenk H.-P.
    Archaea 2:127-135(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 5456 / JCM 9403.

Entry informationi

Entry nameiARGDC_HYPBU
AccessioniPrimary (citable) accession number: A2BM05
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: February 20, 2007
Last modified: September 3, 2014
This is version 52 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

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