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Q92BB8 (ARGJ_LISIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 63. 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:lin1632
OrganismListeria innocua [Complete proteome] [HAMAP]
Taxonomic identifier1642 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Listeriaceae › Listeria

Protein attributes

Sequence length398 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 – 184184Arginine biosynthesis bifunctional protein ArgJ alpha chain By similarity
PRO_0000002183
Chain185 – 398214Arginine biosynthesis bifunctional protein ArgJ beta chain By similarity
PRO_0000002184

Sites

Site184 – 1852Cleavage; by autolysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q92BB8 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 86760EF9FF50A46C

FASTA39842,693
        10         20         30         40         50         60 
MELIKGNIAS PKGFYADGKH AGLKRKRNDI GWIYSEVPAN SAAVYTMNQM QAAPIFVTKD 

        70         80         90        100        110        120 
SFKNSAKLQA IIVNSGNANA VTGNQGMLDA LSMRAKTAEK LAIPMDTVAV ASTGIIGEML 

       130        140        150        160        170        180 
PMDKIMTGID LLEKQTGNAA DFEEAILTTD TFQKQISFQT EIGGKTVTMS GVAKGSGMIH 

       190        200        210        220        230        240 
PNMATMLAFI TTDAAIPAEL LQKLLKIKVD KTFNQITVDG DTSTNDMVVV MANGCAENPL 

       250        260        270        280        290        300 
IQEGTADFEK FAAMFQAVTE HLAKSIARDG EGATKLIEVQ VKGATKTEDA RMIAKKIVSS 

       310        320        330        340        350        360 
SLVKTAAFGG DGNWGRIICA IGYSGGRFAP DNITIKIGGI EILNHSSQTI FNQQALDAYL 

       370        380        390 
EEEHIVIEVD LHIGLESGTA WGCDLSYEYV KINACYRT

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL596169 Genomic DNA. Translation: CAC96863.1.
PIRAG1636.
RefSeqNP_470968.1. NC_003212.1.

3D structure databases

ProteinModelPortalQ92BB8.
SMRQ92BB8. Positions 1-396.
ModBaseSearch...

Protein family/group databases

MEROPST05.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1130257.
GenomeReviewsGene locus lin1632 in contig AL592022_GR.
KEGGlin:lin1632.
NMPDRfig|272626.1.peg.1621.
PATRIC20300001. VBILisInn102668_1667.

Organism-specific databases

GenoListLIN1632.
CMRSearch...

Phylogenomic databases

HOGENOMHBG284202.
OMAGRDPNWG.
ProtClustDBPRK05388.

Enzyme and pathway databases

BioCycLINN272626:LIN1632-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_LISIN
AccessionPrimary (citable) accession number: Q92BB8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: December 1, 2001
Last modified: January 25, 2012
This is version 63 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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