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Q9K8V3 (ARGJ_BACHD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:BH2899
OrganismBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]
Taxonomic identifier272558 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length411 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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

Enzyme regulation

Feedback inhibition by L-arginine By similarity. 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_0000002113
Chain197 – 411215Arginine biosynthesis bifunctional protein ArgJ beta chain By similarity
PRO_0000002114

Sites

Site196 – 1972Cleavage; by autolysis By similarity

Secondary structure

1 ............................................................ 411
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9K8V3 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 0D2D057189397A27

FASTA41143,479
        10         20         30         40         50         60 
MNVINETANV LKLETGSVTS AKGFSAVGIH TGVKRKRKDL GAIVCEVPAS SAAVYTLNKV 

        70         80         90        100        110        120 
QAAPLKVTQE SIAVEGKLQA MIVNSGIANA CTGKRGLDDA YTMRAVGAET FHIPEHYVAV 

       130        140        150        160        170        180 
TSTGVIGEFL PMDVITNGIR QLKPEATIEG AHAFNEAILT TDTVEKHTCY QTIVNGKTVT 

       190        200        210        220        230        240 
VGGVAKGSGM IHPNMATMLS FVTTDANIDH GHLQGALSAI TNETFNRITV DGDTSTNDMV 

       250        260        270        280        290        300 
VVMASGLAEN EALTPEHPDW ANFYKALQLA CEDLAKQIAR DGEGATKLIE VEVTGAANDQ 

       310        320        330        340        350        360 
EAGMVAKQIV GSDLVKTAIY GADANWGRII CAIGYSGCEV NQETIDIAIG PIVTLKQSEP 

       370        380        390        400        410 
TGFSEEEATA YLKEADPVKI SVNLHIGNGT GKAWGCDLTY DYVRINAGYR T

« Hide

References

[1]"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
Nucleic Acids Res. 28:4317-4331(2000) [PubMed: 11058132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000004 Genomic DNA. Translation: BAB06618.1.
PIRC84012.
RefSeqNP_243765.1. NC_002570.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1VRAX-ray2.00A1-196[»]
B197-411[»]
ProteinModelPortalQ9K8V3.
SMRQ9K8V3. Positions 6-409.
ModBaseSearch...

Protein family/group databases

MEROPST05.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000053002; EBBACP00000051641; EBBACG00000052993.
GeneID893093.
GenomeReviewsGene locus BH2899 in contig BA000004_GR.
KEGGbha:BH2899.
NMPDRfig|272558.1.peg.2899.
PATRIC18943030. VBIBacHal18977_3016.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000002382.
HOGENOMHBG284202.
OMAGRDPNWG.
PhylomeDBQ9K8V3.
ProtClustDBPRK05388.

Enzyme and pathway databases

BioCycBHAL272558:BH2899-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_BACHD
AccessionPrimary (citable) accession number: Q9K8V3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 73 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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