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Reviewed, UniProtKB/Swiss-Prot Q82SU1 (ARGJ_NITEU)

Last modified February 9, 2010. Version 47. 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: NE2213
OrganismNitrosomonas europaea [Complete proteome] [HAMAP]
Taxonomic identifier915 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosomonas

Protein attributes

Sequence length409 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 – 192192Arginine biosynthesis bifunctional protein argJ alpha chain By similarity
PRO_0000002203
Chain193 – 409217Arginine biosynthesis bifunctional protein argJ beta chain By similarity
PRO_0000002204

Sites

Site192 – 1932Cleavage; by autolysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q82SU1-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 853F31CFEA2F6F87

FASTA40943,340
        10         20         30         40         50         60 
MPVNIPPLLP EQLLPIPGLS LGTAEASIKR PGRKDILVIT LAENTRVAGV FTRNRFCAAP 

        70         80         90        100        110        120 
VTVARSHLTG SLPIRALVIN TGNANAGTGQ SGIDHAHATC ASLARLIGCQ TQQVLPFSTG 

       130        140        150        160        170        180 
VIMEPLPVEK IITHLPQALA NLAPDNWFAA AQAIMTTDIV PKGVSRQIQI NGTTVTITGI 

       190        200        210        220        230        240 
AKGSGMIHPN MATMLGYIAT DAAVTQPLLD DLVRYATDRS FNCVTVDGDT STNDALILMA 

       250        260        270        280        290        300 
TGQAGNTPIT VSTDPAFISL QAAITEVAAL LAQMIVRDGE GATKFITVQV ESGKTREECT 

       310        320        330        340        350        360 
KVAYAIAHSP LIKTACFASD PNLGRILAAI GYAGIEDLDV NLVQLYLGNI LVAEHGGRAA 

       370        380        390        400 
SYREEDGQRI MQAPEITIQV KLNRGNASTT VWTCDLSYDY VKINADYRS 

« Hide

References

[1]"Complete genome sequence of the ammonia-oxidizing bacterium and obligate chemolithoautotroph Nitrosomonas europaea."
Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L., Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A., Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.
J. Bacteriol. 185:2759-2773(2003) [PubMed: 12700255] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 19718 / IFO 14298.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL954747 Genomic DNA. Translation: CAD86125.1.
RefSeqNP_842215.1.

3D structure databases

SMRQ82SU1. Positions 5-192, 17-406, 193-407.
ModBaseSearch...

Protein family/group databases

MEROPST05.001.

Genome annotation databases

GeneID1083178.
GenomeReviewsGene locus NE2213 in contig AL954747_GR.
KEGGneu:NE2213.
NMPDRfig|228410.1.peg.2114.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG284202.
OMAQNRFCAA.

Enzyme and pathway databases

BioCycNEUR228410:NE2213-MONOMER.
BRENDA2.3.1.1. 444.
2.3.1.35. 444.

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_NITEU
AccessionPrimary (citable) accession number: Q82SU1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: June 1, 2003
Last modified: February 9, 2010
This is version 47 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