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Reviewed, UniProtKB/Swiss-Prot Q8FTN4 (ARGJ_COREF)

Last modified November 3, 2009. Version 42. 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:
    Glutamate N-acetyltransferase
    EC=2.3.1.35
Alternative name(s):
    Ornithine acetyltransferase
    Ornithine transacetylase
      Short name=OATase
Cleaved into the following 2 chains:
    1- Recommended name:
            Glutamate N-acetyltransferase alpha chain
    2- Recommended name:
            Glutamate N-acetyltransferase beta chain
Gene names
Name: argJ
Ordered Locus Names: CE1527
OrganismCorynebacterium efficiens [Complete proteome] [HAMAP]
Taxonomic identifier152794 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length388 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

N(2)-acetyl-L-ornithine + L-glutamate = L-ornithine + 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

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 MF_01106

Sequence similarities

Belongs to the argJ family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Arginine biosynthesis
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processarginine biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionamino-acid N-acetyltransferase activity

Inferred from electronic annotation. Source: HAMAP

glutamate N-acetyltransferase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 182182Glutamate N-acetyltransferase alpha chain By similarity
PRO_0000002159
Chain183 – 388206Glutamate N-acetyltransferase beta chain By similarity
PRO_0000002160

Sites

Site182 – 1832Cleavage; by autolysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8FTN4-1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 3C298BFD2466730E

FASTA38839,543
        10         20         30         40         50         60 
MAQTGITAPK GFVASATTAG IKPSGKPDMA LVVNQGPEYT AAAVFTRNRV IASPVKVSRE 

        70         80         90        100        110        120 
NVADGQLKAV LYNAGNANAC NGTQGDADAR ESVNTLATKL GLAPEDIGVC STGLIGELLP 

       130        140        150        160        170        180 
MDKVTAGIEA LTAEGALGDN GAAAAQAIMT TDTVDKETVV FADGWTVGAM GKGVGMMAPS 

       190        200        210        220        230        240 
LATMLVCLTT DASITPAMAR IALAKATAVT FETLDIDGST STNDTVFLLA SGASGVKPTQ 

       250        260        270        280        290        300 
DELNDAVFAA CSDLAEQMQA DAEGVTKRVS VTVTGTTTDE MAINAARTIA RDNLFKCAMF 

       310        320        330        340        350        360 
GSDPNWGRVL AAVGMADADM DPDHIAVYFN DQAVCLDSTG APGAREVDLS GADIAVRVDL 

       370        380 
GAGGEGQATV RTTDLSYSYV EINSAYST 

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References

[1]"Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
Genome Res. 13:1572-1579(2003) [PubMed: 12840036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Cross-references

Sequence databases

BA000035 Genomic DNA. Translation: BAC18337.1.
RefSeqNP_738137.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

MEROPST05.001.

Genome annotation databases

GeneID1031984.
GenomeReviewsGene locus CE1527 in contig BA000035_GR.
KEGGcef:CE1527.
NMPDRfig|196164.1.peg.1527.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8FTN4.
OMAVHENSAY.

Enzyme and pathway databases

BioCycCEFF196164:CE1527-MON.
BRENDA2.3.1.35. 277326.

Family and domain databases

HAMAPMF_01106.
[Tree]
InterProIPR002813. Arg_biosynth_ArgJ.
[Graphical view]
PANTHERPTHR23100. ArgJ. 1 hit.
PfamPF01960. ArgJ. 1 hit.
[Graphical view]
ProDomPD004193. ArgJ. 2 hits.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00120. ArgJ. 1 hit.
ProtoNetSearch...

Entry information

Entry nameARGJ_COREF
AccessionPrimary (citable) accession number: Q8FTN4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: March 1, 2003
Last modified: November 3, 2009
This is version 42 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