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Q00267

- NHOA_SALTY

UniProt

Q00267 - NHOA_SALTY

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Protein

N-hydroxyarylamine O-acetyltransferase

Gene
nhoA, STM1582
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei69 – 691Acyl-thioester intermediate
Active sitei107 – 1071
Active sitei122 – 1221

GO - Molecular functioni

  1. N-hydroxyarylamine O-acetyltransferase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BioCyciSENT99287:GCTI-1592-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
N-hydroxyarylamine O-acetyltransferase (EC:2.3.1.118)
Alternative name(s):
Arylamine N-acetyltransferase
Arylhydroxamate N,O-acetyltransferase
NAT101
Gene namesi
Name:nhoA
Ordered Locus Names:STM1582
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000001014: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi69 – 691C → A: Loss of activity.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 281281N-hydroxyarylamine O-acetyltransferasePRO_0000107916Add
BLAST

Proteomic databases

PaxDbiQ00267.
PRIDEiQ00267.

Interactioni

Subunit structurei

Monomer and homodimer.1 Publication

Protein-protein interaction databases

STRINGi99287.STM1582.

Structurei

Secondary structure

1
281
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 119
Helixi22 – 3514
Helixi41 – 444
Helixi55 – 606
Turni61 – 633
Helixi69 – 8214
Beta strandi87 – 948
Beta strandi107 – 1148
Beta strandi117 – 1215
Beta strandi134 – 1363
Beta strandi142 – 1443
Beta strandi147 – 1526
Beta strandi157 – 17418
Helixi181 – 19313
Helixi198 – 2003
Beta strandi204 – 2085
Beta strandi210 – 2123
Beta strandi214 – 2185
Beta strandi221 – 2266
Helixi239 – 24810
Turni257 – 2593
Helixi263 – 2719

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E2TX-ray2.80A/B/C/D/E/F/G/H1-281[»]
ProteinModelPortaliQ00267.
SMRiQ00267. Positions 1-273.

Miscellaneous databases

EvolutionaryTraceiQ00267.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2162.
HOGENOMiHOG000205436.
KOiK00675.
OMAiHAGLYES.
OrthoDBiEOG6D2KV2.
PhylomeDBiQ00267.

Family and domain databases

InterProiIPR001447. Arylamine_N-AcTrfase.
[Graphical view]
PANTHERiPTHR11786. PTHR11786. 1 hit.
PfamiPF00797. Acetyltransf_2. 1 hit.
[Graphical view]
PRINTSiPR01543. ANATRNSFRASE.

Sequencei

Sequence statusi: Complete.

Q00267-1 [UniParc]FASTAAdd to Basket

« Hide

MTSFLHAYFT RLHCQPLGVP TVEALRTLHL AHNCAIPFEN LDVLLPREIQ    50
LDETALEEKL LYARRGGYCF ELNGLFERAL RDIGFNVRSL LGRVILSHPA 100
SLPPRTHRLL LVDVEDEQWI ADVGFGGQTL TAPLRLQAEI AQQTPHGEYR 150
LMQEGSTWIL QFRHHEHWQS MYCFDLGVQQ QSDHVMGNFW SAHWPQSHFR 200
HHLLMCRHLP DGGKLTLTNF HFTRYHQGHA VEQVNVPDVP SLYQLLQQQF 250
GLGVNDVKHG FTEAELAAVM AAFDTHPEAG K 281
Length:281
Mass (Da):32,178
Last modified:December 1, 1992 - v1
Checksum:i5FB3B667BD4D7804
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D90301 Genomic DNA. Translation: BAA14331.1.
S76130 Genomic DNA. Translation: AAB33787.1.
AE006468 Genomic DNA. Translation: AAL20500.1.
PIRiA38090.
RefSeqiNP_460541.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL20500; AAL20500; STM1582.
GeneIDi1253100.
KEGGistm:STM1582.
PATRICi32381666. VBISalEnt20916_1673.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D90301 Genomic DNA. Translation: BAA14331.1 .
S76130 Genomic DNA. Translation: AAB33787.1 .
AE006468 Genomic DNA. Translation: AAL20500.1 .
PIRi A38090.
RefSeqi NP_460541.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1E2T X-ray 2.80 A/B/C/D/E/F/G/H 1-281 [» ]
ProteinModelPortali Q00267.
SMRi Q00267. Positions 1-273.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 99287.STM1582.

Proteomic databases

PaxDbi Q00267.
PRIDEi Q00267.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL20500 ; AAL20500 ; STM1582 .
GeneIDi 1253100.
KEGGi stm:STM1582.
PATRICi 32381666. VBISalEnt20916_1673.

Phylogenomic databases

eggNOGi COG2162.
HOGENOMi HOG000205436.
KOi K00675.
OMAi HAGLYES.
OrthoDBi EOG6D2KV2.
PhylomeDBi Q00267.

Enzyme and pathway databases

BioCyci SENT99287:GCTI-1592-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q00267.

Family and domain databases

InterProi IPR001447. Arylamine_N-AcTrfase.
[Graphical view ]
PANTHERi PTHR11786. PTHR11786. 1 hit.
Pfami PF00797. Acetyltransf_2. 1 hit.
[Graphical view ]
PRINTSi PR01543. ANATRNSFRASE.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiNHOA_SALTY
AccessioniPrimary (citable) accession number: Q00267
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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