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Reviewed, UniProtKB/Swiss-Prot Q7VLN8 (ARGA_HAEDU)

Last modified November 3, 2009. Version 41. 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: HD_1384
OrganismHaemophilus ducreyi [Complete proteome] [HAMAP]
Taxonomic identifier730 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length437 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 Probable.

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 – 437437Amino-acid acetyltransferase HAMAP MF_01105
PRO_0000186793

Regions

Domain289 – 437149N-acetyltransferase

Sequences

Sequence LengthMass (Da)Tools
Q7VLN8-1 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 12CE064EDBADD241

FASTA43749,314
        10         20         30         40         50         60 
MRNTELIEWF RQSAPYVNMH RHKTFVIMLD GNAIAHPNFI NITNDISLLH SLGIKLVIVF 

        70         80         90        100        110        120 
GARCQIENLL KQNNISSSYH HNIRVTDSNM LEIIKQAVGG LHYDIFSRLS LRLPHSPVLN 

       130        140        150        160        170        180 
VVSSNAILAQ PLGVIDGVDY GLSGKIRRIN IEAIQQQLAQ NAIVVIGPIA PSVTGKMFNL 

       190        200        210        220        230        240 
AFEEIATQLA IKLKVDKLIA FCDRQGLLDE QGKVISDIHP REAKQHLKKF IQQGDYHHSA 

       250        260        270        280        290        300 
ARFLQAAIDV CHAGIKRSHL ISYQTDGSLL QELFSRDGVG TQLSEASSEC IRLATSFDIA 

       310        320        330        340        350        360 
GLLNLIRPLE DQGLLVKRSR EQLEMEISQY TIIERDGIVI ACAALIHYPA EKMAEMACVA 

       370        380        390        400        410        420 
VHPDYRDSAR GDILLEAIKR RAYKLNIEKL FVLTTQTIQW FQERGFVQIQ PTDLPVEKQR 

       430 
HYNYQRMSKV LMLALDN 

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References

[1]"The complete genome sequence of Haemophilus ducreyi."
Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L., Nguyen D., Wang J., Forst C., Hood L.
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 35000HP / ATCC 700724.

Cross-references

Sequence databases

AE017143 Genomic DNA. Translation: AAP96197.1.
RefSeqNP_873808.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID1491276.
GenomeReviewsGene locus HD_1384 in contig AE017143_GR.
KEGGhdu:HD1384.
NMPDRfig|233412.1.peg.1173.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ7VLN8.
OMADLIRPLE.

Enzyme and pathway databases

BioCycHDUC233412:HD_1384-MON.
BRENDA2.3.1.1. 265031.

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_HAEDU
AccessionPrimary (citable) accession number: Q7VLN8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: October 1, 2003
Last modified: November 3, 2009
This is version 41 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