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Reviewed, UniProtKB/Swiss-Prot B4F2F5 (ARGA_PROMH)

Last modified November 3, 2009. Version 8. 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: PMI2307
OrganismProteus mirabilis (strain HI4320) [Complete proteome] [HAMAP]
Taxonomic identifier529507 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProteus

Protein attributes

Sequence length444 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

Subunit structure

Homohexamer By similarity.

Subcellular location

Cytoplasm By similarity.

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 – 444444Amino-acid acetyltransferase HAMAP MF_01105
PRO_1000137051

Regions

Domain295 – 434140N-acetyltransferase

Sequences

Sequence LengthMass (Da)Tools
B4F2F5-1 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 58C3705E0DD2684B

FASTA44449,390
        10         20         30         40         50         60 
MKERSTELVD GFRHSVPYIN AHRGKTFVIM LGGEAIAHEN FPSIINDIGL LHSLGIRLVV 

        70         80         90        100        110        120 
VYGARPQIDV ALEEQKISPL YHKHTRITDS KTLEVVKQSA GTLQLDITAR LSMSLSNTPL 

       130        140        150        160        170        180 
QGAHINVVSG NFVIAQPLGV DDGVDYCHSG KIRRIDEEAI HRQLDNHAIV LIGPVAVSVT 

       190        200        210        220        230        240 
GESFNLTSEE VATQLAIKLK AQKLIGFCSS QGVVDASGQI VSELLPNQAE ERIQALQTTG 

       250        260        270        280        290        300 
DYHSGTVRFL RGAVTACRRG VERSHLLSYQ ADGAIVQELF SRDGIGTQIV MESAEKVRRA 

       310        320        330        340        350        360 
NINDIGGILE LIRPLEQQGI LVRRSREQLE MEIDQFTIIE RDNLTIACAA LYPYQSEKIG 

       370        380        390        400        410        420 
EMACVAVHPD YRSSCRGEVL LQRISTQAKQ MGLDKLFVLT TRSIHWFQEK GFTPAEIDKL 

       430        440 
PIEKQALYNY QRRSKILILD LHKE 

« Hide

References

[1]"Complete genome sequence of uropathogenic Proteus mirabilis, a master of both adherence and motility."
Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S., Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T., Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., Walker D., Whithead S. expand/collapse author list , Thomson N.R., Rather P.N., Parkhill J., Mobley H.L.T.
J. Bacteriol. 190:4027-4037(2008) [PubMed: 18375554] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AM942759 Genomic DNA. Translation: CAR44559.1.
RefSeqYP_002152025.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID6803060.
GenomeReviewsGene locus PMI2307 in contig AM942759_GR.

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_PROMH
AccessionPrimary (citable) accession number: B4F2F5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 23, 2008
Last modified: November 3, 2009
This is version 8 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