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Q635F1 (ARGJ_BACCZ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 57. 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:BCE33L3886
OrganismBacillus cereus (strain ZK / E33L) [Complete proteome] [HAMAP]
Taxonomic identifier288681 [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_0000002111
Chain195 – 408214Arginine biosynthesis bifunctional protein ArgJ beta chain By similarity
PRO_0000002112

Sites

Site194 – 1952Cleavage; by autolysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q635F1 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: A08F36DF4680B82F

FASTA40843,924
        10         20         30         40         50         60 
MMVKVASITK LEDGSIVTPK GFSAIGTAIG LKKGKKDLGA IVCDTPASCA AVYTTNQIQA 

        70         80         90        100        110        120 
APLQVTKDSI ATEGKLQAII VNSGNANACT GMKGLQDAYE MRALGAEHFG VKENYVAVAS 

       130        140        150        160        170        180 
TGVIGVPLPM EIIRKGIVTL IPAKEENEAH SFSEAILTTD LITKETCYEM IIDGKKVTIA 

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

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

       310        320        330        340        350        360 
KKIAKQIVGS SLVKTAIHGE DPNWGRIISS IGQSEVAINP NTIDITLQSI VVLKNSEPQM 

       370        380        390        400 
FSEEEMKMRL QEHEIMIDVY LHLGEETGSA WGCDLSYEYV KINACYRT

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000001 Genomic DNA. Translation: AAU16382.1.
RefSeqYP_085466.1. NC_006274.1.

3D structure databases

ProteinModelPortalQ635F1.
SMRQ635F1. Positions 4-406.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ635F1.

Protein family/group databases

MEROPST05.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000044308; EBBACP00000043209; EBBACG00000044299.
GeneID3022217.
GenomeReviewsGene locus BCE33L3886 in contig CP000001_GR.
KEGGbcz:BCZK3886.
PATRIC18891552. VBIBacCer95304_4114.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1364.
GeneTreeEBGT00050000002382.
HOGENOMHBG284202.
OMAGRDPNWG.
ProtClustDBPRK05388.

Enzyme and pathway databases

BioCycBCER288681:BCE33L3886-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_BACCZ
AccessionPrimary (citable) accession number: Q635F1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: October 25, 2004
Last modified: January 25, 2012
This is version 57 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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