Skip Header

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

Q8FYE2 (ARGJ_BRUSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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=AGS
Gene names
Name:argJ
Ordered Locus Names:BR1941, BS1330_I1935
OrganismBrucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP]
Taxonomic identifier204722 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

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 – 194194Arginine biosynthesis bifunctional protein ArgJ alpha chain By similarity
PRO_0000002139
Chain195 – 413219Arginine biosynthesis bifunctional protein ArgJ beta chain By similarity
PRO_0000002140

Sites

Site194 – 1952Cleavage; by autolysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8FYE2 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 44C1DEF0E4A63B04

FASTA41343,244
        10         20         30         40         50         60 
MSASVSPLAP KHYPAMPVIH GVRIATAAAG IKYKGRTDLM LMVFDRPAEA AGVFTRSLCP 

        70         80         90        100        110        120 
SAPVDFCRRN LVHGKARAVV VNSGNANAFT GLKGREATQA TAEAAAKAIG CATTDIFLAS 

       130        140        150        160        170        180 
TGVIGEPLDA GKFSHLLGDM AESATEDFWT EAAKAIMTTD TYPKVATETV LLGQVPVTIN 

       190        200        210        220        230        240 
GIAKGAGMIA PDMATMLSFV VTDAPIKADA LQSLLSKGVG STFNSVTVDS DTSTSDTLML 

       250        260        270        280        290        300 
FATGTAAERG APEITDAADK RLADFKKALG RVLKSLALQV VRDGEGARKM VEVEVTGAKS 

       310        320        330        340        350        360 
AASAKKIALS IANSPLVKTA VAGEDANWGR VVMAVGKAGE PADRDRLAIW FGDIRVAHQG 

       370        380        390        400        410 
ERDPAYSEDA TSAYMEGEDI RIRVDLGIGR GKATVWTCDL TKEYVAINGD YRS 

« Hide

References

[1]"The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts."
Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. expand/collapse author list , Shetty J., Malek J.A., Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.
Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed: 12271122] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1330.
[2]"Revised genome sequence of Brucella suis 1330."
Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.
J. Bacteriol. 193:6410-6410(2011) [PubMed: 22038969] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1330.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014291 Genomic DNA. Translation: AAN30833.1.
CP002997 Genomic DNA. Translation: AEM19250.1.
RefSeqNP_698918.1. NC_004310.3.

3D structure databases

ProteinModelPortalQ8FYE2.
ModBaseSearch...

Protein family/group databases

MEROPST05.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1167641.
GenomeReviewsGene locus BR1941 in contig AE014291_GR.
KEGGbms:BR1941.
PATRIC17792301. VBIBruSui107850_1975.
TIGRBR1941.

Phylogenomic databases

HOGENOMHBG284202.
OMAFPKLATR.
PhylomeDBQ8FYE2.
ProtClustDBPRK05388.

Enzyme and pathway databases

BioCycBSUI204722:BR_1941-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_BRUSU
AccessionPrimary (citable) accession number: Q8FYE2
Secondary accession number(s): G0K884
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: March 1, 2003
Last modified: January 25, 2012
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Brucella suis

Brucella suis (strain 1330): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families