Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

B1YD10

- ARGDC_PYRNV

UniProt

B1YD10 - ARGDC_PYRNV

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Arginine decarboxylase proenzyme

Gene

Tneu_0734

Organism
Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / V24Sta) (Thermoproteus neutrophilus)
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.UniRule annotation

Catalytic activityi

L-arginine = agmatine + CO2.UniRule annotation

Cofactori

pyruvoyl groupUniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei73 – 742Cleavage (non-hydrolytic); by autolysisUniRule annotation
Active sitei74 – 741Schiff-base intermediate with substrate; via pyruvic acidUniRule annotation
Active sitei79 – 791Proton acceptor; for processing activityUniRule annotation
Active sitei94 – 941Proton donor; for catalytic activityUniRule annotation

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

BioCyciTNEU444157:GHL2-740-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:Tneu_0734
OrganismiPyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / V24Sta) (Thermoproteus neutrophilus)
Taxonomic identifieri444157 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum
ProteomesiUP000001694: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7373Arginine decarboxylase beta chainUniRule annotationPRO_0000364127Add
BLAST
Chaini74 – 12653Arginine decarboxylase alpha chainUniRule annotationPRO_0000364128Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei74 – 741Pyruvic 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

STRINGi444157.Tneu_0734.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1586.
HOGENOMiHOG000216579.
KOiK01611.

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.

B1YD10-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQTTTQVKTP VVGKHVYGEL YGVDEELLRD QEKLRKIVIE AAHIAKMHLV
60 70 80 90 100
EVNSWKFKGG DKEGVSVIAL VLESHIAIHT WPTYNYATVD VYTCGEHSDP
110 120
MAAFRYIVSQ LAPKRFTVNY SDRSYR
Length:126
Mass (Da):14,386
Last modified:February 10, 2009 - v2
Checksum:iD0D16AF6B802F535
GO

Sequence cautioni

The sequence ACB39673.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001014 Genomic DNA. Translation: ACB39673.1. Different initiation.
RefSeqiYP_001794119.1. NC_010525.1.

Genome annotation databases

EnsemblBacteriaiACB39673; ACB39673; Tneu_0734.
GeneIDi6165201.
KEGGitne:Tneu_0734.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001014 Genomic DNA. Translation: ACB39673.1 . Different initiation.
RefSeqi YP_001794119.1. NC_010525.1.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 444157.Tneu_0734.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACB39673 ; ACB39673 ; Tneu_0734 .
GeneIDi 6165201.
KEGGi tne:Tneu_0734.

Phylogenomic databases

eggNOGi COG1586.
HOGENOMi HOG000216579.
KOi K01611.

Enzyme and pathway databases

UniPathwayi UPA00186 ; UER00284 .
BioCyci TNEU444157:GHL2-740-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 2338 / JCM 9278 / V24Sta.

Entry informationi

Entry nameiARGDC_PYRNV
AccessioniPrimary (citable) accession number: B1YD10
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: February 10, 2009
Last modified: November 26, 2014
This is version 42 of the entry and version 2 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