Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 99 (11 Dec 2019)
Sequence version 2 (20 Mar 2007)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

N-alpha-acetyltransferase

Gene

ard1

Organism
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei35Plays an important role in substrate specificity1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>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
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi88Zinc; via tele nitrogenCombined sources1 Publication1
    Metal bindingi127ZincCombined sources1 Publication1
    Binding sitei132Acetyl-CoACombined sources3 Publications1
    Binding sitei154SubstrateCombined sources1 Publication1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

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

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionAcyltransferase, Transferase
    LigandMetal-binding, Zinc

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.3.1.88 6163

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:ard11 Publication
    Ordered Locus Names:SSO0209
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri273057 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSaccharolobus
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000001974 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002816441 – 167N-alpha-acetyltransferaseAdd BLAST167

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q980R9

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer.

    1 Publication

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    273057.SSO0209

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1167
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    Q980R9

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    Q980R9

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini12 – 167N-acetyltransferasePROSITE-ProRule annotationAdd BLAST156

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni92 – 94Acetyl-CoA bindingCombined sources4 Publications3
    Regioni100 – 105Acetyl-CoA bindingCombined sources4 Publications6
    Regioni139 – 141Acetyl-CoA bindingCombined sources3 Publications3

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    arCOG00833 Archaea
    COG0456 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000078523

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q980R9

    KEGG Orthology (KO)

    More...
    KOi
    K03789

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    SGEIMGY

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR006464 AcTrfase_RimI/Ard1
    IPR016181 Acyl_CoA_acyltransferase
    IPR000182 GNAT_dom

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00583 Acetyltransf_1, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF55729 SSF55729, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR01575 rimI, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51186 GNAT, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i410D4CA4F7CEA60E
    GO

    <p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence AAK40554 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    AE006641 Genomic DNA Translation: AAK40554.1 Different initiation.

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    C90162

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAK40554; AAK40554; SSO0209

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    sso:SSO0209

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|273057.12.peg.208

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

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

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    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[»]
    6AG4X-ray2.26A1-167[»]
    6AG5X-ray2.32A1-167[»]
    SMRiQ980R9
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    STRINGi273057.SSO0209

    Proteomic databases

    PRIDEiQ980R9

    Protocols and materials databases

    The DNASU plasmid repository

    More...
    DNASUi
    1455364

    Genome annotation databases

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

    Phylogenomic databases

    eggNOGiarCOG00833 Archaea
    COG0456 LUCA
    HOGENOMiHOG000078523
    InParanoidiQ980R9
    KOiK03789
    OMAiSGEIMGY

    Enzyme and pathway databases

    BRENDAi2.3.1.88 6163

    Miscellaneous databases

    EvolutionaryTraceiQ980R9

    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

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiNAT_SACS2
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q980R9
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 20, 2007
    Last sequence update: March 20, 2007
    Last modified: December 11, 2019
    This is version 99 of the entry and version 2 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again