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Reviewed, UniProtKB/Swiss-Prot A0KLC8 (ARGA_AERHH)

Last modified November 3, 2009. Version 20. 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:
    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: AHA_2569
OrganismAeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / NCIB 9240) [Complete proteome] [HAMAP]
Taxonomic identifier380703 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeAeromonas

Protein attributes

Sequence length442 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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

Subcellular location

Cytoplasm By similarity.

Miscellaneous

In bacteria which possess the bifunctional enzyme ornithine acetyltransferase/N-acetylglutamate synthase (argJ), argA fulfills an anaplerotic role. 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 – 442442Amino-acid acetyltransferase HAMAP MF_01105
PRO_1000084809

Regions

Domain295 – 442148N-acetyltransferase

Sequences

Sequence LengthMass (Da)Tools
A0KLC8-1 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: A5CBF47944BDE782

FASTA44249,230
        10         20         30         40         50         60 
MREREPSLVY AFRQSTPYVN VHRGATFVLM MGGEALCHPN FANIVSDIAL LQTLGIRLVL 

        70         80         90        100        110        120 
VFGSRPQNDE ALARAGIEAQ YHKRIRVTDD ESFAIIKQVC GGLQYDITAQ LSMGLANTPM 

       130        140        150        160        170        180 
QGARISVVSG NFVTAQPLGV DDGIDFCHSG RVRRIDVEGI TRQLDQKSLV LISPIGCSVT 

       190        200        210        220        230        240 
GESFNLSSEE VARRVAVDLK ADKLICFSST QGVMDRHGEA ISELFPEQAE ELLVELEQAG 

       250        260        270        280        290        300 
EEMSGTARYL RAAIASCRGG VPRSHLVSYQ DDGAMLQELF SRDGLGTQIV RESAEQARAA 

       310        320        330        340        350        360 
TIEDIGGILD LIRPLEEEGI LVRRSREQLE MEIDKFTIIE RDGLIIGCAA LYCFMEEAMA 

       370        380        390        400        410        420 
EMACVAIHPD YRNSNRGDQL VAKVAERAKR LGIRRLFVLT TRSIHWFRER GFDPLEVEDL 

       430        440 
PVARQRLYNW QRRSKVLSKT IV 

« Hide

References

[1]"Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades."
Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.
J. Bacteriol. 188:8272-8282(2006) [PubMed: 16980456] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000462 Genomic DNA. Translation: ABK37645.1.
RefSeqYP_857079.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA0KLC8.

Genome annotation databases

GeneID4489709.
GenomeReviewsGene locus AHA_2569 in contig CP000462_GR.
KEGGaha:AHA_2569.
TIGRAHA_2569.

Phylogenomic databases

OMADLIRPLE.

Family and domain databases

HAMAPMF_01105.
[Tree]
InterProIPR001048. Asp/Glu/Uridylate_kinase.
IPR000182. GCN5-rel_AcTrfase.
IPR010167. NH2A_AcTrfase_ArgA.
[Graphical view]
Gene3DG3DSA:3.40.1160.10. Aa_kinase. 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_AERHH
AccessionPrimary (citable) accession number: A0KLC8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: December 12, 2006
Last modified: November 3, 2009
This is version 20 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