Skip Header

Contribute Send feedback
Read comments (?) or add your own

P96426 (ARGJ_RHOFA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arginine biosynthesis bifunctional protein ArgJ

Including the following 2 domains:

  1. Glutamate N-acetyltransferase
    EC=2.3.1.35
    Alternative name(s):
    Ornithine acetyltransferase
    Short name=OATase
    Ornithine transacetylase
  2. Amino-acid acetyltransferase
    EC=2.3.1.1
    Alternative name(s):
    N-acetylglutamate synthase
    Short name=AGSase
Gene names
Name:argJ
Synonyms:attH
OrganismRhodococcus fascians
Taxonomic identifier1828 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

Protein attributes

Sequence length403 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_01106

Catalytic activity

N(2)-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L-glutamate. HAMAP-Rule MF_01106

Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate. HAMAP-Rule MF_01106

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1. HAMAP-Rule MF_01106

Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4. HAMAP-Rule MF_01106

Subunit structure

Heterotetramer of two alpha and two beta chains By similarity.

Subcellular location

Cytoplasm By similarity.

Miscellaneous

Some bacteria possess a monofunctional ArgJ, i.e. capable of catalyzing only the fifth step of the arginine biosynthetic pathway. HAMAP-Rule MF_01106

Sequence similarities

Belongs to the ArgJ family.

Sequence caution

The sequence CAC43342.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 193193Arginine biosynthesis bifunctional protein ArgJ alpha chain By similarity
PRO_0000002227
Chain194 – 403210Arginine biosynthesis bifunctional protein ArgJ beta chain By similarity
PRO_0000002228

Sites

Active site1941Nucleophile By similarity
Binding site1611Substrate By similarity
Binding site1831Substrate By similarity
Binding site1941Substrate By similarity
Binding site2731Substrate By similarity
Binding site3981Substrate By similarity
Binding site4031Substrate By similarity
Site1251Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole By similarity
Site1261Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole By similarity
Site193 – 1942Cleavage; by autolysis By similarity

Sequences

Sequence LengthMass (Da)Tools
P96426 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: B596508AD60FD900

FASTA40342,800
        10         20         30         40         50         60 
MVQSVLSSTS HGSERADMSA ASPQGFHCWT THLGLADEGK DDFSMVISDR PCTSSVVFTK 

        70         80         90        100        110        120 
SLFAGPCVTL SKTSIEQTSP RGVLVLAKNA NVATGAEGLR NASEIRASVA RTVGIEPDAL 

       130        140        150        160        170        180 
IMASTGVIGV QYPMDTIRAG LDGLGQGTPL DAHAVARAIM TTDTRAKVSE RAVGTSTIVG 

       190        200        210        220        230        240 
IAKGVGMIEP DMATMLSFVF TDADVPQDTL NRIFRDVVDR TYNSVSIDTD TSTSDTAAVF 

       250        260        270        280        290        300 
ANGSAGPVPD TEFEQALEEV CTDLVKMIAS DGEGATKLIV TTVSGASSER QARVVGKSII 

       310        320        330        340        350        360 
NSPLVKTMIH GEDPNWGRVL MAIGKCSNEV DIEPDRIRVA FADIDVYPSS SLDQHDTVEV 

       370        380        390        400 
VREHLATVTV EINVDLGIGT DTWRVFGCDL TDEYIRINAD YTT 

« Hide

References

[1]"Leafy gall formation is controlled by fasR, an AraC-type regulatory gene in Rhodococcus fascians."
Temmerman W., Vereecke D., Dreesen R., Van Montagu M., Holsters M., Goethals K.
J. Bacteriol. 182:5832-5840(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: D188.
[2]"The att locus of Rhodococcus fascians strain D188 is essential for full virulence on tobacco through the production of an autoregulatory compound."
Maes T., Vereecke D., Ritsema T., Cornelis K., Thu H.N., Van Montagu M., Holsters M., Goethals K.
Mol. Microbiol. 42:13-28(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: D188.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y09820 Genomic DNA. Translation: CAA70949.1.
AJ311775 Genomic DNA. Translation: CAC43342.1. Different initiation.

3D structure databases

ProteinModelPortalP96426.
SMRP96426. Positions 22-400.
ModBaseSearch...

Protein family/group databases

MEROPST05.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00068; UER00106.
UPA00068; UER00111.

Family and domain databases

Gene3D3.60.70.12. 1 hit.
HAMAPMF_01106. ArgJ.
InterProIPR002813. Arg_biosynth_ArgJ.
IPR016117. ArgJ-like_dom.
[Graphical view]
PANTHERPTHR23100. PTHR23100. 1 hit.
PfamPF01960. ArgJ. 1 hit.
[Graphical view]
ProDomPD004193. Arg_biosynth_ArgJ. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF56266. Pept_S58_DmpA/Arg_biosyn_ArgJ. 1 hit.
TIGRFAMsTIGR00120. ArgJ. 1 hit.
ProtoNetSearch...

Entry information

Entry nameARGJ_RHOFA
AccessionPrimary (citable) accession number: P96426
Secondary accession number(s): Q93JQ2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: May 1, 1997
Last modified: April 3, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families