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Reviewed, UniProtKB/Swiss-Prot Q5WEW8 (ARGJ_BACSK)

Last modified February 9, 2010. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Arginine biosynthesis bifunctional protein argJ
Cleaved into the following 2 chains:
    1- Recommended name:
            Arginine biosynthesis bifunctional protein argJ alpha chain
    2- Recommended name:
            Arginine biosynthesis bifunctional protein argJ beta chain
Including the following 2 domains:
    1- Recommended name:
            Glutamate N-acetyltransferase
              EC=2.3.1.35
        Alternative name(s):
            Ornithine acetyltransferase
              Short name=OATase
            Ornithine transacetylase
    2- Recommended name:
            Amino-acid acetyltransferase
              EC=2.3.1.1
        Alternative name(s):
            N-acetylglutamate synthase
              Short name=AGS
Gene names
Name: argJ
Ordered Locus Names: ABC2557
OrganismBacillus clausii (strain KSM-K16) [Complete proteome] [HAMAP]
Taxonomic identifier66692 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

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. HAMAP MF_01106

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_0000002117
Chain195 – 408214Arginine biosynthesis bifunctional protein argJ beta chain By similarity
PRO_0000002118

Sites

Site194 – 1952Cleavage; by autolysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5WEW8-1 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 45C55C81659F1AEB

FASTA40842,826
        10         20         30         40         50         60 
MLTKQTTGQA WKQIKGSITD VKGFTTAGAH CGLKRKRLDI GAIFCDVPAN AAGVFTLNQI 

        70         80         90        100        110        120 
QAAPLKVTKE SLAHSNGKLQ AVLVNSGNAN ACTGASGLVD AYEMRALAAA KFAVPEEMVA 

       130        140        150        160        170        180 
VTSTGVIGEK MPMEKVRSGI EDLVLSKEST PFAEAILTTD TGTKEVCVEV VIDQKTVRIA 

       190        200        210        220        230        240 
GVAKGSGMIH PNMATMLGFI TTDANIETAA LKRALAKATD ETFNRITVDG DTSTNDMVLV 

       250        260        270        280        290        300 
LASGLADNQP LDETHPDWAN FYGALSACAE SLAKKIAKDG EGATKLIEVQ VAGAVSDEEA 

       310        320        330        340        350        360 
GKVAKAIVGS DLVKTAAYGK DGNWGRIICA IGYSGCTLDP DTIDIAIGPY ETLVQSEPVV 

       370        380        390        400 
VDDAAISKYM EAETIVIKAD LHQGQGVGKA WGCDLTYDYV RINAGYRT 

« Hide

References

[1]"The complete genome sequence of the alkaliphilic Bacillus clausii KSM-K16."
Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., Kawai S., Ito S., Horikoshi K.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006627 Genomic DNA. Translation: BAD65092.1.
RefSeqYP_176053.1.

3D structure databases

SMRQ5WEW8. Positions 7-194, 21-405, 195-406.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5WEW8.

Genome annotation databases

GeneID3201719.
GenomeReviewsGene locus ABC2557 in contig AP006627_GR.
KEGGbcl:ABC2557.
NMPDRfig|66692.3.peg.2245.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1364.
HOGENOMHBG284202.
OMAVHENSAY.

Enzyme and pathway databases

BioCycBCLA66692:ABC2557-MONOMER.

Family and domain databases

HAMAPMF_01106. ArgJ.
[Tree]
InterProIPR002813. Arg_biosynth_ArgJ.
IPR016117. Pept_S58_DmpA/Arg_biosyn_ArgJ.
[Graphical view]
PANTHERPTHR23100. ArgJ. 1 hit.
PfamPF01960. ArgJ. 1 hit.
[Graphical view]
TIGRFAMsTIGR00120. ArgJ. 1 hit.
ProtoNetSearch...

Entry information

Entry nameARGJ_BACSK
AccessionPrimary (citable) accession number: Q5WEW8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: November 23, 2004
Last modified: February 9, 2010
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents