Skip Header

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

A4YH98

- ARGDC_METS5

UniProt

A4YH98 - ARGDC_METS5

(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

Msed_1645

Organism
Metallosphaera sedula (strain ATCC 51363 / DSM 5348)
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 group.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

  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

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: 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.
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.

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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
CP000682 Genomic DNA. Translation: ABP95800.1 .
RefSeqi WP_012021587.1. NC_009440.1.
YP_001191724.1. NC_009440.1.

3D structure databases

ProteinModelPortali A4YH98.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 399549.Msed_1645.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABP95800 ; ABP95800 ; Msed_1645 .
GeneIDi 5104850.
KEGGi mse:Msed_1645.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00186 ; UER00284 .
BioCyci MSED399549:GH1O-1665-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 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: October 29, 2014
This is version 51 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