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Q6HE29 (ARGJ_BACHK) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 56. 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

Cleaved into the following 2 chains:

  1. Arginine biosynthesis bifunctional protein ArgJ alpha chain
  2. Arginine biosynthesis bifunctional protein ArgJ beta chain

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:BT9727_3878
OrganismBacillus thuringiensis subsp. konkukian (strain 97-27) [Complete proteome] [HAMAP]
Taxonomic identifier281309 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length408 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_0000002115
Chain195 – 408214Arginine biosynthesis bifunctional protein ArgJ beta chain By similarity
PRO_0000002116

Sites

Site194 – 1952Cleavage; by autolysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6HE29 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 279F49EF2AAC4103

FASTA40844,024
        10         20         30         40         50         60 
MMIKIASITK VENGSIVTPK GFSAIGTAIG LKKEKKDLGA IVCDVPASCA AVYTTNQIQA 

        70         80         90        100        110        120 
APLQVTKDSI TTERKLQAII VNSGNANACT GMKGLQDAYE MRVLGAEHFG VKENYVAVAS 

       130        140        150        160        170        180 
TGVIGVPLPM DIIRKGIATL IPAKEENEAH SFSEAILTTD LITKETCYEM SIDGKKVMIA 

       190        200        210        220        230        240 
GVAKGSGMIH PNMATMLSFI TTDAHIEHDV LQTALSQITN HTFNQITVDG DTSTNDMVIA 

       250        260        270        280        290        300 
MASGLSETKP INMEHADWET FVFALQKVCE DLAKKIAQDG EGATKLIEVN VLGAQTNEEA 

       310        320        330        340        350        360 
KKIAKQIVGS SLVKTAIHGE DPNWGRIISS IGQSEVAINP NTIEITLQSI AVLKNSEPQT 

       370        380        390        400 
FSEEEMKERL QEDEIVINVY LHLGEETGSA WGCDLSYEYV KINACYRT

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE017355 Genomic DNA. Translation: AAT60754.1.
RefSeqYP_038197.1. NC_005957.1.

3D structure databases

ProteinModelPortalQ6HE29.
SMRQ6HE29. Positions 4-406.
ModBaseSearch...

Protein family/group databases

MEROPST05.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000072265; EBBACP00000070351; EBBACG00000072256.
GeneID2854843.
GenomeReviewsGene locus BT9727_3878 in contig AE017355_GR.
KEGGbtk:BT9727_3878.
NMPDRfig|281309.1.peg.3837.
PATRIC18988820. VBIBacThu119411_4136.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000002382.
HOGENOMHBG284202.
OMAGRDPNWG.
ProtClustDBPRK05388.

Enzyme and pathway databases

BioCycBTHU281309:BT9727_3878-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_BACHK
AccessionPrimary (citable) accession number: Q6HE29
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: July 19, 2004
Last modified: January 25, 2012
This is version 56 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

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