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P62057 (ARGJ_BACC1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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=AGSase
Gene names
Name:argJ
Ordered Locus Names:BCE_4202
OrganismBacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP]
Taxonomic identifier222523 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length407 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 N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate By similarity. HAMAP-Rule MF_01106

Catalytic activity

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

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

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

Subunit structure

Heterotetramer of two alpha and two beta chains By similarity.

Subcellular location

Cytoplasm By similarity.

Miscellaneous

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

Sequence similarities

Belongs to the ArgJ family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 193193Arginine biosynthesis bifunctional protein ArgJ alpha chain By similarity
PRO_0000002107
Chain194 – 407214Arginine biosynthesis bifunctional protein ArgJ beta chain By similarity
PRO_0000002108

Sites

Active site1941Nucleophile By similarity
Binding site1571Substrate By similarity
Binding site1831Substrate By similarity
Binding site1941Substrate By similarity
Binding site2801Substrate By similarity
Binding site4021Substrate By similarity
Binding site4071Substrate By similarity
Site1201Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole By similarity
Site1211Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole By similarity
Site193 – 1942Cleavage; by autolysis By similarity

Sequences

Sequence LengthMass (Da)Tools
P62057 [UniParc].

Last modified June 21, 2004. Version 1.
Checksum: 0DD6BDAE57041021

FASTA40743,899
        10         20         30         40         50         60 
MIKVASITKV ENGSIVTPKG FSAIGTAIGL KKEKKDLGAI VCDTPASCAA VYTTNQIQAA 

        70         80         90        100        110        120 
PLQVTKDSIA TEGKLQAIIV NSGNANACTG MKGLQDAYEM RALGAEHFGL KENYVAVAST 

       130        140        150        160        170        180 
GVIGVPLPMD IIRNGIATLI PAKEEREAHS FSEAILTTDL ITKETCYEMV IDGEKVLIAG 

       190        200        210        220        230        240 
VAKGSGMIHP NMATMLSFIT TDAHIEHDVL QTTLSQITNH TFNQITIDGD TSTNDMVIVM 

       250        260        270        280        290        300 
ASGLSETKPI NMEHADWETF VFALQKVCED LAKKIAQDGE GATKLIEVNV LGARTNEEAK 

       310        320        330        340        350        360 
KIAKQIVGSS LVKTAIHGED PNWGRIISTI GQSEVAINPN TIDITLQSIA VLKNSEPQMF 

       370        380        390        400 
SEEEMKMRLQ EHEIMIDVNL HLGEETGSAW GCDLSYEYVK INACYRT 

« Hide

References

[1]"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
Nucleic Acids Res. 32:977-988(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10987.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017194 Genomic DNA. Translation: AAS43103.1.
RefSeqNP_980495.1. NC_003909.8.

3D structure databases

ProteinModelPortalP62057.
SMRP62057. Positions 3-405.
ModBaseSearch...

Protein-protein interaction databases

STRING222523.BCE_4202.

Protein family/group databases

MEROPST05.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS43103; AAS43103; BCE_4202.
GeneID2747976.
KEGGbca:BCE_4202.
PATRIC18857051. VBIBacCer118379_4024.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1364.
HOGENOMHOG000022797.
KOK00620.
OMAPNMGTML.
ProtClustDBPRK05388.

Enzyme and pathway databases

UniPathwayUPA00068; UER00106.
UPA00068; UER00111.

Family and domain databases

Gene3D3.60.70.12. 1 hit.
HAMAPMF_01106. ArgJ.
InterProIPR002813. Arg_biosynth_ArgJ.
IPR016117. ArgJ-like_dom.
[Graphical view]
PANTHERPTHR23100. PTHR23100. 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_BACC1
AccessionPrimary (citable) accession number: P62057
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: June 21, 2004
Last modified: May 1, 2013
This is version 72 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