Skip Header

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

Q4J932

- ARGDC_SULAC

UniProt

Q4J932 - ARGDC_SULAC

(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

Saci_1363

Organism
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
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
Sitei77 – 782Cleavage (non-hydrolytic); by autolysisUniRule annotation
Active sitei78 – 781Schiff-base intermediate with substrate; via pyruvic acidUniRule annotation
Active sitei83 – 831Proton acceptor; for processing activityUniRule annotation
Active sitei98 – 981Proton 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

BioCyciSACI330779:GH9J-1341-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:Saci_1363
OrganismiSulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
Taxonomic identifieri330779 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
ProteomesiUP000001018: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7777Arginine decarboxylase beta chainUniRule annotationPRO_0000041966Add
BLAST
Chaini78 – 13053Arginine decarboxylase alpha chainUniRule annotationPRO_0000041967Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei78 – 781Pyruvic 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

STRINGi330779.Saci_1363.

Structurei

3D structure databases

ProteinModelPortaliQ4J932.
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.

Q4J932-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSQQLSSQTP SNQDRIVGKH VFGNLYDIDD KLLMDKDLLE GLVLEAVKIA
60 70 80 90 100
KMNLVEIKSW SFGGKKGGVS VIALVEESHI ALHTWNEYKY ATLDVYTCGV
110 120 130
DSNPQAAFEF IVSNLKPKRH QMFFADRSSE
Length:130
Mass (Da):14,623
Last modified:August 2, 2005 - v1
Checksum:i22A84EFDAD722E9F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000077 Genomic DNA. Translation: AAY80698.1.
RefSeqiYP_255991.1. NC_007181.1.

Genome annotation databases

EnsemblBacteriaiAAY80698; AAY80698; Saci_1363.
GeneIDi3472928.
KEGGisai:Saci_1363.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000077 Genomic DNA. Translation: AAY80698.1 .
RefSeqi YP_255991.1. NC_007181.1.

3D structure databases

ProteinModelPortali Q4J932.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 330779.Saci_1363.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAY80698 ; AAY80698 ; Saci_1363 .
GeneIDi 3472928.
KEGGi sai:Saci_1363.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00186 ; UER00284 .
BioCyci SACI330779:GH9J-1341-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 Sulfolobus acidocaldarius, a model organism of the Crenarchaeota."
    Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E., Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.
    J. Bacteriol. 187:4992-4999(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770.

Entry informationi

Entry nameiARGDC_SULAC
AccessioniPrimary (citable) accession number: Q4J932
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: August 2, 2005
Last modified: November 26, 2014
This is version 59 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