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Q00267

- NHOA_SALTY

UniProt

Q00267 - NHOA_SALTY

Protein

N-hydroxyarylamine O-acetyltransferase

Gene

nhoA

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 Dec 1992)
      Previous versions | rss
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    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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    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: October 1, 2014
    This is version 101 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