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Q00267 (NHOA_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 100. 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:
N-hydroxyarylamine O-acetyltransferase

EC=2.3.1.118
Alternative name(s):
Arylamine N-acetyltransferase
Arylhydroxamate N,O-acetyltransferase
NAT101
Gene names
Name:nhoA
Ordered Locus Names:STM1582
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length281 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Acetyl-CoA + an N-hydroxyarylamine = CoA + an N-acetoxyarylamine.

Subunit structure

Monomer and homodimer. Ref.4

Sequence similarities

Belongs to the arylamine N-acetyltransferase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 281281N-hydroxyarylamine O-acetyltransferase
PRO_0000107916

Sites

Active site691Acyl-thioester intermediate
Active site1071
Active site1221

Experimental info

Mutagenesis691C → A: Loss of activity.

Secondary structure

............................................ 281
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q00267 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 5FB3B667BD4D7804

FASTA28132,178
        10         20         30         40         50         60 
MTSFLHAYFT RLHCQPLGVP TVEALRTLHL AHNCAIPFEN LDVLLPREIQ LDETALEEKL 

        70         80         90        100        110        120 
LYARRGGYCF ELNGLFERAL RDIGFNVRSL LGRVILSHPA SLPPRTHRLL LVDVEDEQWI 

       130        140        150        160        170        180 
ADVGFGGQTL TAPLRLQAEI AQQTPHGEYR LMQEGSTWIL QFRHHEHWQS MYCFDLGVQQ 

       190        200        210        220        230        240 
QSDHVMGNFW SAHWPQSHFR HHLLMCRHLP DGGKLTLTNF HFTRYHQGHA VEQVNVPDVP 

       250        260        270        280 
SLYQLLQQQF GLGVNDVKHG FTEAELAAVM AAFDTHPEAG K 

« Hide

References

« Hide 'large scale' references
[1]"Involvement of Cys69 residue in the catalytic mechanism of N-hydroxyarylamine O-acetyltransferase of Salmonella typhimurium. Sequence similarity at the amino acid level suggests a common catalytic mechanism of acetyltransferase for S. typhimurium and higher organisms."
Watanabe M., Sofuni T., Nohmi T.
J. Biol. Chem. 267:8429-8436(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"N-hydroxyarylamine O-acetyltransferase of Salmonella typhimurium: proposal for a common catalytic mechanism of arylamine acetyltransferase enzymes."
Watanabe M., Igarashi T., Kaminuma T., Sofuni T., Nohmi T.
Environ. Health Perspect. 102:83-89(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 29631 / TA 1538.
[3]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[4]"Structure of arylamine N-acetyltransferase reveals a catalytic triad."
Sinclair J.C., Sandy J., Delgoda R., Sim E., Noble M.E.M.
Nat. Struct. Biol. 7:560-564(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), SUBUNIT STRUCTURE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D90301 Genomic DNA. Translation: BAA14331.1.
S76130 Genomic DNA. Translation: AAB33787.1.
AE006468 Genomic DNA. Translation: AAL20500.1.
PIRA38090.
RefSeqNP_460541.1. NC_003197.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E2TX-ray2.80A/B/C/D/E/F/G/H1-281[»]
ProteinModelPortalQ00267.
SMRQ00267. Positions 1-273.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING99287.STM1582.

Proteomic databases

PaxDbQ00267.
PRIDEQ00267.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL20500; AAL20500; STM1582.
GeneID1253100.
KEGGstm:STM1582.
PATRIC32381666. VBISalEnt20916_1673.

Phylogenomic databases

eggNOGCOG2162.
HOGENOMHOG000205436.
KOK00675.
OMAHAGLYES.
OrthoDBEOG6D2KV2.
PhylomeDBQ00267.

Enzyme and pathway databases

BioCycSENT99287:GCTI-1592-MONOMER.

Family and domain databases

InterProIPR001447. Arylamine_N-AcTrfase.
[Graphical view]
PANTHERPTHR11786. PTHR11786. 1 hit.
PfamPF00797. Acetyltransf_2. 1 hit.
[Graphical view]
PRINTSPR01543. ANATRNSFRASE.
ProtoNetSearch...

Other

EvolutionaryTraceQ00267.

Entry information

Entry nameNHOA_SALTY
AccessionPrimary (citable) accession number: Q00267
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: July 9, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references