Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot A6VMR4 (ARGA_ACTSZ)

Last modified November 3, 2009. Version 15. 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: Asuc_0891
OrganismActinobacillus succinogenes (strain ATCC 55618 / 130Z) [Complete proteome] [HAMAP]
Taxonomic identifier339671 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeActinobacillus

Protein attributes

Sequence length440 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 – 440440Amino-acid acetyltransferase HAMAP MF_01105
PRO_1000084808

Regions

Domain289 – 429141N-acetyltransferase

Sequences

Sequence LengthMass (Da)Tools
A6VMR4-1 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: CBC69A07381735E5

FASTA44050,161
        10         20         30         40         50         60 
MRSTELVQWF RQSTPYVNMH RGKTFVIMLD GDTIASENFI NIISDIRLLH SLGIKLIIVF 

        70         80         90        100        110        120 
GARFQINDLL MKNHIRPVYH KNIRVTDLRT LELVKQAAGQ LNYDIMSRLS MRLPHSPLLN 

       130        140        150        160        170        180 
VVSSNFILAQ PIGVDDGVDY MLSGKLRRIE VENIKQQLEN DAIVLIGPVA PSVTGESFNL 

       190        200        210        220        230        240 
PFEEVATQVA IKLKAEKLIG FSNTQGILDK DGVSIPDLLP QQAANYLQQF IERDQYHSSQ 

       250        260        270        280        290        300 
ARFLQAAIDV CRAGVHRSHL LSYEEDGSLL QELFTRDGVG TQLSMESSED IRIATARDIP 

       310        320        330        340        350        360 
SLLELIHPLE QQGILVKRSR EQLEMDIEKY TIIDRDGVII ACAALNVYED EKMAEMACVA 

       370        380        390        400        410        420 
VHPDYRSSSR GDVLLAEIRK RAKNLDIEKL FVLTTRTVHW FQERGFHMAN VEDLPKDKRD 

       430        440 
HYNYQRRSKI LIQNLTEPSE 

« Hide

References

[1]"Complete sequence of Actinobacillus succinogenes 130Z."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Vieille C., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000746 Genomic DNA. Translation: ABR74261.1.
RefSeqYP_001344196.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA6VMR4.

Genome annotation databases

GeneID5348802.
GenomeReviewsGene locus Asuc_0891 in contig CP000746_GR.
KEGGasu:Asuc_0891.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMADLIRPLE.

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_ACTSZ
AccessionPrimary (citable) accession number: A6VMR4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: August 21, 2007
Last modified: November 3, 2009
This is version 15 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