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P0A6C6 (ARGA_ECOL6) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:c3412
OrganismEscherichia coli O6 [Complete proteome] [HAMAP]
Taxonomic identifier217992 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length443 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Sequence similarities

Belongs to the acetyltransferase family. ArgA subfamily.

Contains 1 N-acetyltransferase domain.

Sequence caution

The sequence AAN81857.1 differs from that shown. Reason: Erroneous initiation.

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: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionacetyl-CoA:L-glutamate N-acetyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 443443Amino-acid acetyltransferase HAMAP MF_01105
PRO_0000186792

Regions

Domain296 – 443148N-acetyltransferase

Sequences

Sequence LengthMass (Da)Tools
P0A6C6 [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

[1]"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli."
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014075 Genomic DNA. Translation: AAN81857.1. Different initiation.
RefSeqNP_755287.2. NC_004431.1.

3D structure databases

ProteinModelPortalP0A6C6.
SMRP0A6C6. Positions 8-442.
ModBaseSearch...

Proteomic databases

PRIDEP0A6C6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000042895; EBESCP00000041244; EBESCG00000041945.
GeneID1039282.
GenomeReviewsGene locus c3412 in contig AE014075_GR.
KEGGecc:c3412.
PATRIC18284652. VBIEscCol75197_3212.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000010674.
OMAAFNLAME.
ProtClustDBPRK05279.

Family and domain databases

HAMAPMF_01105. N-acetyl_glu_synth.
[Tree]
InterProIPR000182. AcTrfase_GCN5-related_dom.
IPR016181. Acyl_CoA_acyltransferase.
IPR001048. Asp/Glu/Uridylate_kinase.
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.
KOK14682.
PfamPF00696. AA_kinase. 1 hit.
PF00583. Acetyltransf_1. 1 hit.
[Graphical view]
PIRSFPIRSF000423. ArgA. 1 hit.
SUPFAMSSF53633. Aa_kinase. 1 hit.
SSF55729. Acyl_CoA_acyltransferase. 1 hit.
TIGRFAMsTIGR01890. N-Ac-Glu-synth. 1 hit.
PROSITEPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameARGA_ECOL6
AccessionPrimary (citable) accession number: P0A6C6
Secondary accession number(s): O68009 expand/collapse secondary AC list , O68010, O68011, O68012, O68013, P08205
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: January 25, 2012
This is version 50 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