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Reviewed, UniProtKB/Swiss-Prot P0A6C5 (ARGA_ECOLI)

Last modified June 16, 2009. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
    Amino-acid acetyltransferase
    EC=2.3.1.1
Alternative name(s):
    N-acetylglutamate synthase
      Short name=AGS
      Short name=NAGS
Gene names
Name: argA
Ordered Locus Names: b2818, JW2786
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length443 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate. HAMAP MF_01105

Enzyme regulation

Feedback inhibition by L-arginine. HAMAP MF_01105

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4. HAMAP MF_01105

Subunit structure

Homohexamer Probable.

Subcellular location

Cytoplasm Probable.

Miscellaneous

The mutant strains shown below are all feedback-resistant (fbr) strains exhibiting enhanced arginine biosynthesis. HAMAP MF_01105

Sequence similarities

Belongs to the acetyltransferase family. ArgA subfamily.

Contains 1 N-acetyltransferase domain.

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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 443443Amino-acid acetyltransferase HAMAP MF_01105
PRO_0000186790

Regions

Domain296 – 443148N-acetyltransferase

Experimental info

Mutagenesis151H → Y in EE17. Ref.2
Mutagenesis191Y → C in EE51. Ref.2
Mutagenesis541S → N in PT2M217. Ref.2
Mutagenesis581R → H in EE11. Ref.2
Mutagenesis2871G → S in PT2M216. Ref.2
Mutagenesis4321Q → R in PT2M217. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P0A6C5-1 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: AE0D84902456797A

FASTA44349,195
        10         20         30         40         50         60 
MVKERKTELV EGFRHSVPYI NTHRGKTFVI MLGGEAIEHE NFSSIVNDIG LLHSLGIRLV 

        70         80         90        100        110        120 
VVYGARPQID ANLAAHHHEP LYHKNIRVTD AKTLELVKQA AGTLQLDITA RLSMSLNNTP 

       130        140        150        160        170        180 
LQGAHINVVS GNFIIAQPLG VDDGVDYCHS GRIRRIDEDA IHRQLDSGAI VLMGPVAVSV 

       190        200        210        220        230        240 
TGESFNLTSE EIATQLAIKL KAEKMIGFCS SQGVTNDDGD IVSELFPNEA QARVEAQEEK 

       250        260        270        280        290        300 
GDYNSGTVRF LRGAVKACRS GVRRCHLISY QEDGALLQEL FSRDGIGTQI VMESAEQIRR 

       310        320        330        340        350        360 
ATINDIGGIL ELIRPLEQQG ILVRRSREQL EMEIDKFTII QRDNTTIACA ALYPFPEEKI 

       370        380        390        400        410        420 
GEMACVAVHP DYRSSSRGEV LLERIAAQAK QSGLSKLFVL TTRSIHWFQE RGFTPVDIDL 

       430        440 
LPESKKQLYN YQRKSKVLMA DLG 

« Hide

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of the Escherichia coli argA gene."
Brown K., Finch P.W., Hickson I.D., Emmerson P.T.
Nucleic Acids Res. 15:10586-10586(1987) [PubMed: 3320971] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Use of inducible feedback-resistant N-acetylglutamate synthetase (argA) genes for enhanced arginine biosynthesis by genetically engineered Escherichia coli K-12 strains."
Rajagopal B.S., Deponte J. III, Tuchman M., Malamy M.H.
Appl. Environ. Microbiol. 64:1805-1811(1998) [PubMed: 9572954] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF HIS-15; TYR-19; SER-54; ARG-58; GLY-287 AND GLN-432.
Strain: K12 / Various isolates.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"N-acetylglutamate synthase of Escherichia coli: purification, characterization, and molecular properties."
Marvil D.K., Leisinger T.
J. Biol. Chem. 252:3295-3303(1977) [PubMed: 16890] [Abstract]
Cited for: CHARACTERIZATION.
Strain: K12.

Cross-references

Sequence databases

Y00492 Genomic DNA. Translation: CAA68547.1.
AF008115 Genomic DNA. Translation: AAC23443.1.
AF008116 Genomic DNA. Translation: AAC23444.1.
AF008117 Genomic DNA. Translation: AAC23445.1.
AF008118 Genomic DNA. Translation: AAC23446.1.
AF008119 Genomic DNA. Translation: AAC23447.1.
U29581 Genomic DNA. Translation: AAB40465.1.
U00096 Genomic DNA. Translation: AAC75857.1.
AP009048 Genomic DNA. Translation: BAE76887.1.
PIRXYECAA. A30372.
RefSeqAP_003381.1.
NP_417295.1.

3D structure databases

ModBaseSearch...

2-D gel databases

ECO2DBASEH052.7. 6TH EDITION.

Genome annotation databases

GeneID947289.
GenomeReviewsGene locus JW2786 in contig AP009048_GR.
Gene locus b2818 in contig U00096_GR.
KEGGecj:JW2786.
eco:b2818.

Organism-specific databases

EchoBASEEB0061.
EcoGeneEG10063. argA.
CMRSearch...

Phylogenomic databases

OMAP0A6C5. DLIRPLE.

Enzyme and pathway databases

BioCycEcoCyc:N-ACETYLTRANSFER-MON.
MetaCyc:N-ACETYLTRANSFER-MON.

Family and domain databases

HAMAPMF_01105.
[Tree]
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR000182. GCN5-rel_AcTrfase.
IPR010167. NH2A_AcTrfase_ArgA.
[Graphical view]
Gene3DG3DSA:3.40.1160.10. Aa_kinase. 1 hit.
G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.
PfamPF00696. AA_kinase. 1 hit.
PF00583. Acetyltransf_1. 1 hit.
[Graphical view]
PIRSFPIRSF000423. ArgA. 1 hit.
TIGRFAMsTIGR01890. N-Ac-Glu-synth. 1 hit.
PROSITEPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameARGA_ECOLI
AccessionPrimary (citable) accession number: P0A6C5
Secondary accession number(s): O68009 expand/collapse secondary AC list , O68010, O68011, O68012, O68013, P08205, Q2MA19
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: June 16, 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

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

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