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Protein

N-alpha-acetyltransferase

Gene

ard1

Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Displays alpha (N-terminal) acetyltransferase activity. Catalyzes the covalent attachment of an acetyl moiety from acetyl-CoA to the free alpha-amino group at the N-terminus of a protein (PubMed:17511810, PubMed:23959863, PubMed:25728374). NAT is able to acetylate the alpha-amino group of methionine, alanine and serine N-terminal residue substrates, however it has a preference for Ser-N-terminal substrates (PubMed:17511810, PubMed:23959863, PubMed:25728374).3 Publications

Miscellaneous

NAT does not require a binding partner for activity.2 Publications

Catalytic activityi

Acetyl-CoA + an N-terminal-L-alanyl-[protein] = an N-terminal-N(alpha)-acetyl-L-alanyl-[protein] + CoA.2 Publications
Acetyl-CoA + an N-terminal-L-seryl-[protein] = an N-terminal-N(alpha)-acetyl-L-seryl-[protein] + CoA.3 Publications
Acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[protein] = an N-terminal-N(alpha)-acetyl-L-methionyl-L-leucyl-[protein] + CoA.2 Publications
Acetyl-CoA + an N-terminal-L-methionyl-L-glutamyl-[protein] = an N-terminal-N(alpha)-acetyl-L-methionyl-L-glutamyl-[protein] + CoA.1 Publication

Kineticsi

Kcat is 33.57 min(-1) for acetyltransferase activity with acetyl-CoA (at 65 degrees Celsius with Ser-N-terminal peptide (Alba)) (PubMed:25728374). Kcat is 3.3 min(-1) for acetyltransferase activity with Ser-N-terminal peptide (PubMed:23959863). Kcat is 0.73 min(-1) for acetyltransferase activity with Met-N-terminal peptide (PubMed:23959863).2 Publications
  1. KM=54 µM for Ser-N-terminal peptide1 Publication
  2. KM=67.17 µM for acetyl-CoA (at 65 degrees Celsius with Ser-N-terminal peptide (Alba))1 Publication
  3. KM=400 µM for Met-N-terminal peptide1 Publication

    Temperature dependencei

    Thermostable.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sitei35Plays an important role in substrate specificity1 Publication1
    Binding sitei37SubstrateCombined sources1 Publication1
    Sitei75Plays an important role in modulating multiple conformations of loop regions and contributes to protein thermostability1 Publication1
    Sitei82Plays an important role in modulating multiple conformations of loop regions and contributes to protein thermostability1 Publication1
    Metal bindingi88Zinc; via tele nitrogenCombined sources1 Publication1
    Metal bindingi127ZincCombined sources1 Publication1
    Binding sitei132Acetyl-CoACombined sources3 Publications1
    Binding sitei154SubstrateCombined sources1 Publication1

    GO - Molecular functioni

    • metal ion binding Source: UniProtKB-KW
    • peptide alpha-N-acetyltransferase activity Source: UniProtKB

    GO - Biological processi

    Keywordsi

    Molecular functionAcyltransferase, Transferase
    LigandMetal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi2.3.1.88. 6163.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    N-alpha-acetyltransferase1 Publication (EC:2.3.1.2553 Publications, EC:2.3.1.2582 Publications)
    Short name:
    NAT1 Publication
    Alternative name(s):
    Amino-terminal acetyltransferase1 Publication
    N-terminal acetyltransferase1 Publication
    Gene namesi
    Name:ard11 Publication
    Ordered Locus Names:SSO0209
    OrganismiSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
    Taxonomic identifieri273057 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
    Proteomesi
    • UP000001974 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi33L → A: 20- and 2-fold decrease of the catalytic efficiency and affinity for Ser-N-terminal peptide. 11-fold decrease of the catalytic efficiency for Met-N-terminal peptide, but almost same affinity compared to the wild-type. 1 Publication1
    Mutagenesisi34P → A: 20-fold decrease of the catalytic efficiency for Ser-N-terminal peptide, but almost same affinity compared to the wild-type. 18-fold decrease of the catalytic efficiency for Met-N-terminal peptide, but almost same affinity compared to the wild-type. 2 Publications1
    Mutagenesisi35E → A: Slight increase of the catalytic efficiency for Ser-N-terminal peptide, but 4-fold decrease of the affinity compared to the wild-type. 6-fold increase of the catalytic efficiency for Met-N-terminal peptide and slight decrease of the affinity compared to the wild-type. 2 Publications1
    Mutagenesisi35E → F: Strong decrease of the acetyltransferase activity with Ser-N-terminal peptide such as Alba. 2-fold increase of acetyltransferase activity for Ala-N-terminal peptide such as Hjc compared to the wild-type. 1 Publication1
    Mutagenesisi35E → Q: Loss of acetyltransferase activity for Ser and Met-N-terminal peptide; when associated with Gln-127. 1 Publication1
    Mutagenesisi35E → V: Alters the N-terminal substrate specificity and allows large N-terminal end residue of the substrate to be accommodated in a substrate-binding pocket. 4-fold increase of the acetyltransferase activity with Met-N-terminal peptide such as SSB compared to the wild-type. 2-fold increase of acetyltransferase activity with Ala-N-terminal peptide such as Hjc. 1 Publication1
    Mutagenesisi35E → W: Low acetyltransferase activity with Ala-, Met- and Ser-N-terminal peptide. 1 Publication1
    Mutagenesisi37Y → A: 34-fold decrease of the catalytic efficiency for Ser-N-terminal peptide and slight decrease of the affinity compared to the wild-type. Loss of acetyltransferase activity for Met-N-terminal peptide. 1 Publication1
    Mutagenesisi37Y → F: Same catalytic efficiency and slight decrease of the affinity for Ser-N-terminal peptide compared to the wild-type. 3-fold decrease of the catalytic efficiency and 1.3-fold increase of the affinity for Met-N-terminal peptide compared to the wild-type. 1 Publication1
    Mutagenesisi75S → A: Has a melting temperature about 3 degrees Celsius lower than that of the wild-type. 1 Publication1
    Mutagenesisi82S → A: Has a melting temperature about 3 degrees Celsius lower than that of the wild-type. 1 Publication1
    Mutagenesisi88H → A: 2.5- and 1.5-fold decrease of the catalytic efficiency and affinity for Ser-N-terminal peptide compared to the wild-type, respectively. Loss of acetyltransferase activity for Met-N-terminal peptide. 1 Publication1
    Mutagenesisi88H → F: 2.5-fold decrease of the catalytic efficiency for Ser-N-terminal peptide, but almost same affinity compared to the wild-type. Loss of acetyltransferase activity for Met-N-terminal peptide. 1 Publication1
    Mutagenesisi88H → Q: 2.5-fold decrease of the catalytic efficiency for Ser-N-terminal peptide, but 1.5-fold increase of the affinity compared to the wild-type. Loss of acetyltransferase activity for Met-N-terminal peptide. 1 Publication1
    Mutagenesisi100R → A: 7-fold decrease of the affinity, with no significant difference in the catalytic efficiency. Same fold compared to the wild-type. 1 Publication1
    Mutagenesisi105T → A: 3-fold decrease of the affinity, with no significant difference in the catalytic efficiency. Same fold compared to the wild-type. 1 Publication1
    Mutagenesisi125Y → A: Same catalytic efficiency and 1.7-fold decrease of the affinity for Ser-N-terminal peptide compared to the wild-type. 1.5- and 2.5-fold decrease of the catalytic efficiency and affinity for Met-N-terminal peptide compared to the wild-type, respectively. 1 Publication1
    Mutagenesisi127E → A: Same catalytic efficiency and slight decrease of the affinity for Ser-N-terminal peptide compared to the wild-type. Loss of acetyltransferase activity for Met-N-terminal peptide. 1 Publication1
    Mutagenesisi127E → H: 1.3-fold decrease of the catalytic efficiency for Ser-N-terminal peptide, but almost same affinity compared to the wild-type. 1.7-fold decrease of the catalytic efficiency and 1.3-fold increase of the affinity for Met-N-terminal peptide compared to the wild-type. 1 Publication1
    Mutagenesisi127E → Q: 2.3-fold decrease of the catalytic efficiency and 1.3-fold increase of the affinity for Ser-N-terminal peptide compared to the wild-type. 5-fold decrease of the catalytic efficiency and slight decrease of the affinity for Met-N-terminal peptide compared to the wild-type. Loss of acetyltransferase activity for Ser and Met-N-terminal peptide; when associated with Gln-35. 1 Publication1
    Mutagenesisi129R → A: Slight decrease of the catalytic efficiency and of the affinity for Ser-N-terminal peptide compared to teh wild-type. 2.5-fold increase of the catalytic efficiency and almost the same affinity for Met-N-terminal peptide compared to the wild-type. 1 Publication1
    Mutagenesisi132N → A: 4.5-fold decrease of the affinity, with no significant difference in the catalytic efficiency. Same fold compared to the wild-type. 1 Publication1
    Mutagenesisi154Y → A: 1.3-fold decrease of the catalytic efficiency for Ser-N-terminal peptide, but same affinity compared to the wild-type. 6.5-fold decrease of the catalytic efficiency for Met-N-terminal peptide, but same affinity compared to the wild-type. 1 Publication1
    Mutagenesisi154Y → F: Almost same catalytic efficiency for Ser-N-terminal peptide and slight decrease of the affinity compared to the wild-type. 5-fold decrease of the catalytic efficiency for Met-N-terminal peptide and 1.5-fold decrease of the affinity compared to the wild-type. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002816441 – 167N-alpha-acetyltransferaseAdd BLAST167

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi273057.SSO0209.

    Structurei

    Secondary structure

    1167
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi13 – 16Combined sources4
    Helixi19 – 21Combined sources3
    Helixi22 – 32Combined sources11
    Helixi39 – 49Combined sources11
    Helixi50 – 52Combined sources3
    Beta strandi54 – 58Combined sources5
    Beta strandi61 – 74Combined sources14
    Beta strandi76 – 80Combined sources5
    Beta strandi83 – 94Combined sources12
    Helixi96 – 98Combined sources3
    Beta strandi100 – 102Combined sources3
    Helixi103 – 119Combined sources17
    Beta strandi122 – 129Combined sources8
    Helixi133 – 141Combined sources9
    Beta strandi145 – 150Combined sources6
    Beta strandi154 – 157Combined sources4
    Beta strandi160 – 166Combined sources7

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2X7BX-ray1.95A1-167[»]
    4LX9X-ray1.98A1-167[»]
    4R3KX-ray2.13A1-167[»]
    4R3LX-ray1.84A1-167[»]
    5C88X-ray2.49A/B1-167[»]
    ProteinModelPortaliQ980R9.
    SMRiQ980R9.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ980R9.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini12 – 167N-acetyltransferasePROSITE-ProRule annotationAdd BLAST156

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni92 – 94Acetyl-CoA bindingCombined sources4 Publications3
    Regioni100 – 105Acetyl-CoA bindingCombined sources4 Publications6
    Regioni139 – 141Acetyl-CoA bindingCombined sources3 Publications3

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiarCOG00833. Archaea.
    COG0456. LUCA.
    HOGENOMiHOG000078523.
    InParanoidiQ980R9.
    KOiK03789.
    OMAiPWHAHIT.
    OrthoDBiPOG093Z0DQF.

    Family and domain databases

    InterProiView protein in InterPro
    IPR006464. AcTrfase_RimI/Ard1.
    IPR016181. Acyl_CoA_acyltransferase.
    IPR000182. GNAT_dom.
    PfamiView protein in Pfam
    PF00583. Acetyltransf_1. 1 hit.
    SUPFAMiSSF55729. SSF55729. 1 hit.
    TIGRFAMsiTIGR01575. rimI. 1 hit.
    PROSITEiView protein in PROSITE
    PS51186. GNAT. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q980R9-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MELAEKDKGR DFTLRNARMD DIDQIIKINR LTLPENYPYY FFVEHLKEYG
    60 70 80 90 100
    LAFFVAIVDN SVVGYIMPRI EWGFSNIKQL PSLVRKGHVV SIAVLEEYRR
    110 120 130 140 150
    KGIATTLLEA SMKSMKNDYN AEEIYLEVRV SNYPAIALYE KLNFKKVKVL
    160
    KGYYADGEDA YLMARPL
    Length:167
    Mass (Da):19,448
    Last modified:March 20, 2007 - v2
    Checksum:i410D4CA4F7CEA60E
    GO

    Sequence cautioni

    The sequence AAK40554 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE006641 Genomic DNA. Translation: AAK40554.1. Different initiation.
    PIRiC90162.

    Genome annotation databases

    EnsemblBacteriaiAAK40554; AAK40554; SSO0209.
    KEGGisso:SSO0209.
    PATRICifig|273057.12.peg.208.

    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.

    Entry informationi

    Entry nameiNAT_SULSO
    AccessioniPrimary (citable) accession number: Q980R9
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 20, 2007
    Last sequence update: March 20, 2007
    Last modified: June 7, 2017
    This is version 91 of the entry and version 2 of the sequence. See 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