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Q39JW0 (ARGJ_BURS3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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=AGS
Gene names
Name:argJ
Ordered Locus Names:Bcep18194_A3655
OrganismBurkholderia sp. (strain 383) (Burkholderia cepacia (strain ATCC 17760 / NCIB 9086 / R18194)) [Complete proteome] [HAMAP]
Taxonomic identifier269483 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length413 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 acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate By similarity. HAMAP MF_01106

Catalytic activity

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

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

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

Subunit structure

Heterotetramer of two alpha and two beta chains By similarity.

Subcellular location

Cytoplasm Probable HAMAP MF_01106.

Miscellaneous

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

Sequence similarities

Belongs to the ArgJ family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 196196Arginine biosynthesis bifunctional protein ArgJ alpha chain By similarity
PRO_0000227212
Chain197 – 413217Arginine biosynthesis bifunctional protein ArgJ beta chain By similarity
PRO_0000227213

Sites

Site196 – 1972Cleavage; by autolysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q39JW0 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: FDB83C5811068DA5

FASTA41343,560
        10         20         30         40         50         60 
MAVNFPSIDP AQLHPVAGVT LGWAEANIRK PNRKDVLVIS VDESATVAGV FTENRFCAAP 

        70         80         90        100        110        120 
VIVCREHLAK VRAGGAGIRA LVVNTGNANA GTGEPGLVNA RETCAELARL AGIEPAQVLP 

       130        140        150        160        170        180 
FSTGVILEPL PIDRLKAGLP AALANRKAAN WFDAAQAIMT TDTLPKATSR QVTIDGHTVT 

       190        200        210        220        230        240 
LTGISKGAGM IKPNMATMLG FLAFDANVAQ PVLDTLVKEV ADRSFNCITI DGDTSTNDSF 

       250        260        270        280        290        300 
ILIASGKSTL PAITSTDSPA YAALRDAVTE VAQVLSQLIV RDGEGATKFM TVQVEGGKSV 

       310        320        330        340        350        360 
AECRQIAYAI GHSPLVKTAF YASDPNLGRI LAAIGYAGVA DLDVDKIDLY LDDVLVAKAG 

       370        380        390        400        410 
GRNPAYQEED GQRVMKQSEI TIRVQLGRGD AQATIWTCDL SHDYVSINAD YRS 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia sp. 383."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 383.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000151 Genomic DNA. Translation: ABB07256.1.
RefSeqYP_367900.1. NC_007510.1.

3D structure databases

ProteinModelPortalQ39JW0.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ39JW0.

Protein family/group databases

MEROPST05.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3748838.
GenomeReviewsGene locus Bcep18194_A3655 in contig CP000151_GR.
KEGGbur:Bcep18194_A3655.
NMPDRfig|269483.3.peg.5197.
PATRIC19284595. VBIBurSp120713_1732.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1364.
HOGENOMHBG284202.
OMAGRDPNWG.
ProtClustDBPRK05388.

Enzyme and pathway databases

BioCycBSP36773:BCEP18194_A3655-MONOMER.

Family and domain databases

HAMAPMF_01106. ArgJ.
[Tree]
InterProIPR002813. Arg_biosynth_ArgJ.
IPR016117. Pept_S58_DmpA/Arg_biosyn_ArgJ.
[Graphical view]
KOK00620.
PANTHERPTHR23100. ArgJ. 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_BURS3
AccessionPrimary (citable) accession number: Q39JW0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: November 22, 2005
Last modified: January 25, 2012
This is version 45 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