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Protein

Aminoglycoside N(6')-acetyltransferase type 1

Gene
N/A
Organism
Salmonella enteritidis
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of an acetyl group from acetyl-CoA to the 6'-amino group of aminoglycoside molecules conferring resistance to antibiotics containing the purpurosamine ring including amikacin, tobramycin, dibekacin and ribostamycin. Able to acetylate eukaryotic histone proteins.2 Publications

Catalytic activityi

Acetyl-CoA + kanamycin-B = CoA + N(6')-acetylkanamycin-B.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei22 – 221Substrate1 Publication
Binding sitei25 – 251Substrate2 Publications
Binding sitei66 – 661Substrate2 Publications
Binding sitei79 – 791Substrate2 Publications
Binding sitei115 – 1151Substrate2 Publications
Binding sitei120 – 1201Acetyl-CoA2 Publications
Binding sitei136 – 1361Substrate2 Publications

GO - Molecular functioni

  • aminoglycoside 6'-N-acetyltransferase activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • acetyl-CoA metabolic process Source: UniProtKB
  • histone acetylation Source: UniProtKB
  • response to antibiotic Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Antibiotic resistance

Names & Taxonomyi

Protein namesi
Recommended name:
Aminoglycoside N(6')-acetyltransferase type 1By similarity (EC:2.3.1.822 Publications)
Alternative name(s):
AAC(6')-IyBy similarity
Aminoglycoside resistance proteinBy similarity
OrganismiSalmonella enteritidis
Taxonomic identifieri149539 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Pathology & Biotechi

Chemistry

DrugBankiDB03615. Ribostamycin.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 145145Aminoglycoside N(6')-acetyltransferase type 1PRO_0000416829Add
BLAST

Interactioni

Subunit structurei

Homodimer.2 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Structurei

Secondary structure

145
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1 – 55Combined sources
Helixi8 – 103Combined sources
Helixi11 – 2111Combined sources
Helixi27 – 3913Combined sources
Beta strandi41 – 5010Combined sources
Beta strandi53 – 6311Combined sources
Beta strandi71 – 8313Combined sources
Helixi85 – 873Combined sources
Beta strandi89 – 913Combined sources
Helixi92 – 10615Combined sources
Beta strandi110 – 1167Combined sources
Helixi121 – 1299Combined sources
Beta strandi133 – 14412Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S3ZX-ray2.00A/B1-145[»]
1S5KX-ray2.40A/B1-145[»]
1S60X-ray3.00A1-145[»]
2VBQX-ray2.00A/B1-145[»]
ProteinModelPortaliQ9R381.
SMRiQ9R381. Positions 1-145.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9R381.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 145145N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni81 – 833Acetyl-CoA binding2 Publications
Regioni89 – 946Acetyl-CoA binding2 Publications

Sequence similaritiesi

Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

KOiK18816.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR024170. Aminoglycoside_N6-AcTrfrase.
IPR000182. GNAT_dom.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000452. 6-N-acetyltransf. 1 hit.
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9R381-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDIRQMNKTH LEHWRGLRKQ LWPGHPDDAH LADGEEILQA DHLASFIAMA
60 70 80 90 100
DGVAIGFADA SIRHDYVNGC DSSPVVFLEG IFVLPSFRQR GVAKQLIAAV
110 120 130 140
QRWGTNKGCR EMASDTSPEN TISQKVHQAL GFEETERVIF YRKRC
Length:145
Mass (Da):16,362
Last modified:May 1, 2000 - v1
Checksum:i9CD8BBFD48BC43A2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF144880 Genomic DNA. Translation: AAF03531.1.
AF144881 Genomic DNA. Translation: AAF03532.1.
RefSeqiWP_000354853.1. NZ_JYXI01000003.1.

Genome annotation databases

KEGGiag:AAF03531.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF144880 Genomic DNA. Translation: AAF03531.1.
AF144881 Genomic DNA. Translation: AAF03532.1.
RefSeqiWP_000354853.1. NZ_JYXI01000003.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S3ZX-ray2.00A/B1-145[»]
1S5KX-ray2.40A/B1-145[»]
1S60X-ray3.00A1-145[»]
2VBQX-ray2.00A/B1-145[»]
ProteinModelPortaliQ9R381.
SMRiQ9R381. Positions 1-145.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

DrugBankiDB03615. Ribostamycin.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAF03531.

Phylogenomic databases

KOiK18816.

Miscellaneous databases

EvolutionaryTraceiQ9R381.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR024170. Aminoglycoside_N6-AcTrfrase.
IPR000182. GNAT_dom.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000452. 6-N-acetyltransf. 1 hit.
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAAC6_SALEN
AccessioniPrimary (citable) accession number: Q9R381
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2012
Last sequence update: May 1, 2000
Last modified: March 16, 2016
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Strain BM4361 does not express or weakly expresses aminoglycoside resistance gene and is thus aminoglycoside-sensitive. Strain BM4362 expresses it due to a chromosomal deletion leading to aminoglycoside resistance.1 Publication

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.