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Reviewed, UniProtKB/Swiss-Prot Q59280 (ARGJ_CORGL)

Last modified February 9, 2010. Version 67. 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: Cgl1395, cg1581
OrganismCorynebacterium glutamicum (Brevibacterium flavum) [Complete proteome] [HAMAP]
Taxonomic identifier1718 [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. HAMAP MF_01106

Subcellular location

Cytoplasm 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.

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 functionacetyl-CoA:L-glutamate 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_0000002161
Chain183 – 388206Glutamate N-acetyltransferase beta chain By similarity
PRO_0000002162

Sites

Site182 – 1832Cleavage; by autolysis By similarity

Experimental info

Sequence conflict135 – 1362GA → AP Ref.1
Sequence conflict135 – 1362GA → AP Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q59280-1 [UniParc].

Last modified July 11, 2002. Version 2.
Checksum: 031643D9D320A433

FASTA38839,714
        10         20         30         40         50         60 
MAEKGITAPK GFVASATTAG IKASGNPDMA LVVNQGPEFS AAAVFTRNRV FAAPVKVSRE 

        70         80         90        100        110        120 
NVADGQIRAV LYNAGNANAC NGLQGEKDAR ESVSHLAQNL GLEDSDIGVC STGLIGELLP 

       130        140        150        160        170        180 
MDKLNAGIDQ LTAEGALGDN GAAAAKAIMT TDTVDKETVV FADGWTVGGM GKGVGMMAPS 

       190        200        210        220        230        240 
LATMLVCLTT DASVTQEMAQ IALANATAVT FDTLDIDGST STNDTVFLLA SGASGITPTQ 

       250        260        270        280        290        300 
DELNDAVYAA CSDIAAKLQA DAEGVTKRVA VTVVGTTNNE QAINAARTVA RDNLFKCAMF 

       310        320        330        340        350        360 
GSDPNWGRVL AAVGMADADM EPEKISVFFN GQAVCLDSTG APGAREVDLS GADIDVRIDL 

       370        380 
GTSGEGQATV RTTDLSFSYV EINSAYSS 

« Hide

References

« Hide 'large scale' references
[1]"Genes and enzymes of the acetyl cycle of arginine biosynthesis in Corynebacterium glutamicum: enzyme evolution in the early steps of the arginine pathway."
Sakanyan V., Petrosyan P., Lecocq M., Boyen A., Legrain C., Demarez M.N., Hallet J.-N., Glansdorff N.
Microbiology 142:99-108(1996) [PubMed: 8581175] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]"Molecular cloning of the arginine biosynthetic genes from Corynebacterium glutamicum."
Park M.Y., Chun J.Y., Ko S.-Y., Lee M.-S.
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613.
[3]"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."
Nakagawa S.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[4]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X86157 Genomic DNA. Translation: CAA60097.1.
AF049897 Genomic DNA. Translation: AAC24813.1.
BA000036 Genomic DNA. Translation: BAB98788.1.
BX927152 Genomic DNA. Translation: CAF21406.1.
RefSeqNP_600614.1.
YP_225682.1.

3D structure databases

SMRQ59280. Positions 3-182, 8-384, 183-386.
ModBaseSearch...

Protein family/group databases

MEROPST05.001.

Genome annotation databases

GeneID1019371.
3343818.
GenomeReviewsGene locus Cgl1395 in contig BA000036_GR.
KEGGcgb:cg1581.
cgl:NCgl1341.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG284202.
OMAVHENSAY.
PhylomeDBQ59280.

Enzyme and pathway databases

BioCycCGLU196627:CG1581-MONOMER.
BRENDA2.3.1.35. 812.

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_CORGL
AccessionPrimary (citable) accession number: Q59280
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 11, 2002
Last modified: February 9, 2010
This is version 67 of the entry and version 2 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