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Protein

Arginine biosynthesis bifunctional protein ArgJ

Gene

argJ

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.UniRule annotation

Catalytic activityi

N(2)-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L-glutamate.UniRule annotation
Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate.UniRule annotation

Pathwayi: L-arginine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic).UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Arginine biosynthesis bifunctional protein ArgJ (argJ)
This subpathway is part of the pathway L-arginine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic), the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

Pathwayi: L-arginine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes N(2)-acetyl-L-ornithine from L-glutamate.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Arginine biosynthesis bifunctional protein ArgJ (argJ)
  2. Acetylglutamate kinase (argB)
  3. N-acetyl-gamma-glutamyl-phosphate reductase (argC)
  4. Acetylornithine aminotransferase (argD)
This subpathway is part of the pathway L-arginine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes N(2)-acetyl-L-ornithine from L-glutamate, the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei109 – 1091Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion holeUniRule annotation
Sitei110 – 1101Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion holeUniRule annotation
Binding sitei146 – 1461SubstrateUniRule annotation
Binding sitei168 – 1681SubstrateUniRule annotation
Active sitei179 – 1791NucleophileUniRule annotation
Binding sitei179 – 1791SubstrateUniRule annotation
Binding sitei259 – 2591SubstrateUniRule annotation
Binding sitei378 – 3781SubstrateUniRule annotation
Binding sitei383 – 3831SubstrateUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00068; UER00106.
UPA00068; UER00111.

Protein family/group databases

MEROPSiT05.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Arginine biosynthesis bifunctional protein ArgJUniRule annotation
Cleaved into the following 2 chains:
Arginine biosynthesis bifunctional protein ArgJ alpha chainUniRule annotation
Arginine biosynthesis bifunctional protein ArgJ beta chainUniRule annotation
Including the following 2 domains:
Glutamate N-acetyltransferaseUniRule annotation (EC:2.3.1.35UniRule annotation)
Alternative name(s):
Ornithine acetyltransferaseUniRule annotation
Short name:
OATaseUniRule annotation
Ornithine transacetylaseUniRule annotation
Amino-acid acetyltransferaseUniRule annotation (EC:2.3.1.1UniRule annotation)
Alternative name(s):
N-acetylglutamate synthaseUniRule annotation
Short name:
AGSaseUniRule annotation
Gene namesi
Name:argJUniRule annotation
Ordered Locus Names:SCO1579
ORF Names:SCI35.01c, SCL24.15c
OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Taxonomic identifieri100226 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
Proteomesi
  • UP000001973 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 178178Arginine biosynthesis bifunctional protein ArgJ alpha chainUniRule annotationPRO_0000002247Add
BLAST
Chaini179 – 383205Arginine biosynthesis bifunctional protein ArgJ beta chainUniRule annotationPRO_0000002248Add
BLAST

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei178 – 1792Cleavage; by autolysisUniRule annotation

Keywords - PTMi

Autocatalytic cleavage

Proteomic databases

PRIDEiQ8CK24.

Interactioni

Subunit structurei

Heterotetramer of two alpha and two beta chains.UniRule annotation

Protein-protein interaction databases

STRINGi100226.SCO1579.

Structurei

3D structure databases

ProteinModelPortaliQ8CK24.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ArgJ family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C5V. Bacteria.
COG1364. LUCA.
HOGENOMiHOG000022797.
InParanoidiQ8CK24.
KOiK00620.
OMAiWTCDLTH.
OrthoDBiEOG6P8TQQ.
PhylomeDBiQ8CK24.

Family and domain databases

Gene3Di3.60.70.12. 1 hit.
HAMAPiMF_01106. ArgJ.
InterProiIPR002813. Arg_biosynth_ArgJ.
IPR016117. ArgJ-like_dom.
[Graphical view]
PANTHERiPTHR23100. PTHR23100. 1 hit.
PfamiPF01960. ArgJ. 1 hit.
[Graphical view]
SUPFAMiSSF56266. SSF56266. 1 hit.
TIGRFAMsiTIGR00120. ArgJ. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8CK24-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVTAAKGFT AAGITAGIKE SGSPDLALVV NTGPRRSAAG VFTSNRVKAA
60 70 80 90 100
PVLWSEQVLK SGEVTAVVLN SGGANACTGP KGFQDTHATA EKAADVLGTG
110 120 130 140 150
AGEVAVCSTG LIGVLLPMDK LLPGVEAAAG QLSEHGGEKA AIAIKTTDTV
160 170 180 190 200
HKTSVVTRDG WTVGGMAKGA GMLAPGLATM LVVITTDADL ETEALDRALR
210 220 230 240 250
AATRVTFDRV DSDGCMSTND TVLLLSSGSS GVTPEYDAFA EAVRTVCDDL
260 270 280 290 300
GQQLIRDAEG ASKDIKVEVV NAATEDEAVQ VGRTIARNNL LKCAIHGEDP
310 320 330 340 350
NWGRVLSAIG TTDAAFEPDR LNVAINGVWV CKNGGVGEDR ELVDMRYREV
360 370 380
HIVADLAAGD ATATIWTNDL TADYVHENSA YSS
Length:383
Mass (Da):39,512
Last modified:March 1, 2003 - v1
Checksum:i4A7345A0A7754B3E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL939109 Genomic DNA. Translation: CAD55284.1.
RefSeqiNP_733539.1. NC_003888.3.
WP_011027859.1. NC_003888.3.

Genome annotation databases

EnsemblBacteriaiCAD55284; CAD55284; CAD55284.
GeneIDi1097010.
KEGGisco:SCO1579.
PATRICi23732754. VBIStrCoe124346_1591.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL939109 Genomic DNA. Translation: CAD55284.1.
RefSeqiNP_733539.1. NC_003888.3.
WP_011027859.1. NC_003888.3.

3D structure databases

ProteinModelPortaliQ8CK24.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi100226.SCO1579.

Protein family/group databases

MEROPSiT05.001.

Proteomic databases

PRIDEiQ8CK24.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAD55284; CAD55284; CAD55284.
GeneIDi1097010.
KEGGisco:SCO1579.
PATRICi23732754. VBIStrCoe124346_1591.

Phylogenomic databases

eggNOGiENOG4105C5V. Bacteria.
COG1364. LUCA.
HOGENOMiHOG000022797.
InParanoidiQ8CK24.
KOiK00620.
OMAiWTCDLTH.
OrthoDBiEOG6P8TQQ.
PhylomeDBiQ8CK24.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00106.
UPA00068; UER00111.

Family and domain databases

Gene3Di3.60.70.12. 1 hit.
HAMAPiMF_01106. ArgJ.
InterProiIPR002813. Arg_biosynth_ArgJ.
IPR016117. ArgJ-like_dom.
[Graphical view]
PANTHERiPTHR23100. PTHR23100. 1 hit.
PfamiPF01960. ArgJ. 1 hit.
[Graphical view]
SUPFAMiSSF56266. SSF56266. 1 hit.
TIGRFAMsiTIGR00120. ArgJ. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-471 / A3(2) / M145.
  2. "Cloning and expression in Escherichia coli of a Streptomyces coelicolor A3(2) argCJB gene cluster."
    Hindle Z., Callis R., Dowden S., Rudd B.A.M., Baumberg S.
    Microbiology 140:311-320(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: A3(2) / NRRL B-16638.

Entry informationi

Entry nameiARGJ_STRCO
AccessioniPrimary (citable) accession number: Q8CK24
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: March 1, 2003
Last modified: December 9, 2015
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Some bacteria possess a monofunctional ArgJ, i.e. capable of catalyzing only the fifth step of the arginine biosynthetic pathway.

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.