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Q4ZZU5 (ARGA_PSEU2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 51. 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:Psyr_0254
OrganismPseudomonas syringae pv. syringae (strain B728a) [Complete proteome] [HAMAP]
Taxonomic identifier205918 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonasPseudomonas syringae

Protein attributes

Sequence length432 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

Subcellular location

Cytoplasm By similarity 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: 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 – 432432Amino-acid acetyltransferase HAMAP MF_01105
PRO_1000084821

Regions

Domain286 – 425140N-acetyltransferase

Sequences

Sequence LengthMass (Da)Tools
Q4ZZU5 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: 831D913FCB1C357A

FASTA43247,916
        10         20         30         40         50         60 
MPEYVNWLRH ASPYINAHRD CTFVVMLPGD GVAHPNFGNI VHDLVLLHSL GVRLVLVHGS 

        70         80         90        100        110        120 
RPQIESRLAQ RGITPRYHRD LRITDTETLE CVIDAVGQLR ISIEARLSMD MAASPMQGSR 

       130        140        150        160        170        180 
LRVTSGNVVT ARPIGVLEGV DYQHTGEVRR VDRKGINRLL DERHIVLLSP LGYSPTGEIF 

       190        200        210        220        230        240 
NLACEDVATR AAIDLAADKL LLFGAETGLL DEQGRLVREL RPQQVPAHLQ RLGANYQAEL 

       250        260        270        280        290        300 
LDAAAEACRG GVARSHIVSY AENGALLTEL FTRDGGGTLV AQEQFELVRE AAIEDVGGLM 

       310        320        330        340        350        360 
DLITPLEEQG ILVRRSREVL EREITQFSVV EREGLIIACA ALYPIADSES GELACLAVNP 

       370        380        390        400        410        420 
EYRHGGRGDE LLERIENRAR ALGIKTLFVL TTRTAHWFRE RGFEPSSVDR LPSARASLYN 

       430 
YQRNSKIFEK AI 

« Hide

References

[1]"Comparison of the complete genome sequences of Pseudomonas syringae pv. syringae B728a and pv. tomato DC3000."
Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A., Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S., Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M., Kyrpides N.C., Ivanova N., Lindow S.E.
Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005) [PubMed: 16043691] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B728a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000075 Genomic DNA. Translation: AAY35327.1.
RefSeqYP_233365.1. NC_007005.1.

3D structure databases

HSSPHSSP built from PDB template 2BUF based on UniProtKB Q9HTN2.
ProteinModelPortalQ4ZZU5.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ4ZZU5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3365730.
GenomeReviewsGene locus Psyr_0254 in contig CP000075_GR.
KEGGpsb:Psyr_0254.
NMPDRfig|205918.4.peg.590.
PATRIC19980895. VBIPseSyr42314_0253.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0548.
HOGENOMHBG545264.
OMAAFNLAME.
ProtClustDBPRK05279.

Enzyme and pathway databases

BioCycPSYR205918:PSYR_0254-MONOMER.

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_PSEU2
AccessionPrimary (citable) accession number: Q4ZZU5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 7, 2005
Last modified: January 25, 2012
This is version 51 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