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Entry version 123 (29 Sep 2021)
Sequence version 2 (23 Jan 2007)
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Protein

Spermidine N(1)-acetyltransferase

Gene

speG

Organism
Escherichia coli (strain K12)
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

Involved in the protection against polyamine toxicity by regulating their concentration (PubMed:7642535, PubMed:10986239).

Catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to the primary amino groups of spermidine to yield N1- and N8-acetylspermidine (PubMed:8077207, PubMed:7052085, PubMed:6297970).

It can also use spermine, but not putrescine (PubMed:7052085).

5 Publications

In addition, may act as a modulator of transcription through its ability to interact with the two-component response regulator RcsB. Inhibits transcription of the small RNA regulator rprA in an acetylation-independent manner. Interaction with the DNA-binding domain of RcsB might be responsible for SpeG-dependent inhibition of RcsB-dependent rprA transcription (PubMed:30562360).

SpeG does not acetylate RcsB in vitro (PubMed:30562360).

1 Publication

Miscellaneous

Acetylation neutralizes the charge of the polyamine, which is then typically excreted from the cell.1 Publication

<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 <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Heat shock, alkaline shift, ethanol treatment and poor nutrient availability produce increased concentrations of monoacetylated spermidine (PubMed:2061318). Inhibited by alkaline phosphatase, N1,N8-bis(ethyl)spermidine (BESPD) and N1,N(12)-bis(ethyl)spermidine (BESPM) (PubMed:8077207, PubMed:6297970).3 Publications

<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

  1. KM=2 µM for AcCoA (in the presence of 3 mM spermidine at pH 7.5 and 37 degrees Celsius)1 Publication
  2. KM=220 µM for spermine (in the presence of 10 µM AcCoA at pH 7.5 and 37 degrees Celsius)1 Publication
  3. KM=183 µM for spermine1 Publication
  4. KM=1290 µM for spermidine (in the presence of 10 µM AcCoA at pH 7.5 and 37 degrees Celsius)1 Publication
  5. KM=328 µM for spermidine1 Publication

Temperature dependencei

The level of spermidine acetyltransferase activity increases at low temperature to prevent spermidine toxicity.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: spermidine degradation

This protein is involved in the pathway spermidine degradation, which is part of Amine and polyamine degradation.2 Publications
View all proteins of this organism that are known to be involved in the pathway spermidine degradation and in Amine and polyamine degradation.

Pathwayi: spermine degradation

This protein is involved in the pathway spermine degradation, which is part of Amine and polyamine degradation.2 Publications
View all proteins of this organism that are known to be involved in the pathway spermine degradation and in Amine and polyamine degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei30SpermineBy similarity1
<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 bindingi35MagnesiumCombined sources1 Publication1
Binding sitei35SpermidineBy similarity1
Binding sitei35SpermineBy similarity1
Binding sitei43SpermidineBy similarity1
Binding sitei43SpermineBy similarity1
Metal bindingi76MagnesiumCombined sources1 Publication1
<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>Sitei85Could be important for selectivity toward long polyaminesBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei135Proton donor1 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

GO - Biological processi

  • polyamine catabolic process Source: UniProtKB

<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
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:SPERMACTRAN-MONOMER
MetaCyc:SPERMACTRAN-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.3.1.57, 2026

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00211
UPA00250

<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:
Spermidine N(1)-acetyltransferase1 Publication (EC:2.3.1.573 Publications)
Short name:
SAT1 Publication
Alternative name(s):
Spermidine/spermine N(1)-acetyltransferase1 Publication
Short name:
SSAT1 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:speG
Ordered Locus Names:b1584, JW1576
<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>OrganismiEscherichia coli (strain K12)
<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 identifieri83333 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<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
  • UP000000318 <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
  • UP000000625 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

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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Cells lacking this gene accumulate spermidine at late stationary phase and show a reduced cell viability due to a decrease in protein biosynthesis (PubMed:7642535). At 37 degrees Celsius, growth of mutant is normal in the presence of 0.5 or 1 mM spermidine. However, following a shift to 7 degrees Celsius, the addition of 0.5 or 1 mM spermidine results in inhibition of cellular growth or cell lysis, respectively. Furthermore, at 7 degrees Celsius, spermidine accumulation resulted in a decrease in total protein synthesis accompanied by an increase in the synthesis of the major cold shock proteins CspA, CspB, and CspG (PubMed:10986239).2 Publications

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>Mutagenesisi135Y → A: 300-fold decrease in activity with spermine as substrate. Retains the ability to inhibit PrprA activity. 2 Publications1
Mutagenesisi135Y → C or F: 100-fold decrease in activity with spermine as substrate. 1 Publication1
Mutagenesisi135Y → S: Loss of activity with spermine as substrate. 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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000745882 – 186Spermidine N(1)-acetyltransferaseAdd BLAST185

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0A951

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P0A951

PRoteomics IDEntifications database

More...
PRIDEi
P0A951

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Constitutively expressed throughout log and plateau phases of growth.1 Publication

<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

Homododecamer (PubMed:31205017). Ligand-free SpeG forms closed symmetric dodecamers in the crystal and open asymmetric dodecamers in solution (PubMed:31205017). In the absence of ligand, also exists in solution as hexamers and tetramers, but not dimers (PubMed:23908034, PubMed:8077207, PubMed:31205017). Can interact with the DNA-binding carboxyl domain of RcsB in the presence or absence of spermidine (PubMed:30562360).

4 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4260234, 7 interactors
850477, 1 interactor

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-2133, Spermidine N(1)-acetyltransferase complex

Protein interaction database and analysis system

More...
IntActi
P0A951, 11 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b1584

<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

1186
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
P0A951

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<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>Domaini7 – 167N-acetyltransferasePROSITE-ProRule annotationAdd BLAST161

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>Regioni51 – 54Spermine bindingBy similarity4
Regioni85 – 87Spermine bindingBy similarity3
Regioni88 – 90Acetyl-CoA bindingBy similarity3
Regioni95 – 101Acetyl-CoA bindingBy similarity7
Regioni128 – 137Acetyl-CoA bindingBy similarity10

<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

Belongs to the acetyltransferase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG1670, Bacteria

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0A951

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0A951

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR016181, Acyl_CoA_acyltransferase
IPR000182, GNAT_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF13302, Acetyltransf_3, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF55729, SSF55729, 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P0A951-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPSAHSVKLR PLEREDLRYV HQLDNNASVM RYWFEEPYEA FVELSDLYDK
60 70 80 90 100
HIHDQSERRF VVECDGEKAG LVELVEINHV HRRAEFQIII SPEYQGKGLA
110 120 130 140 150
TRAAKLAMDY GFTVLNLYKL YLIVDKENEK AIHIYRKLGF SVEGELMHEF
160 170 180
FINGQYRNAI RMCIFQHQYL AEHKTPGQTL LKPTAQ
Length:186
Mass (Da):21,887
Last modified:January 23, 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:i27297083B93B3752
GO

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
D25276 Genomic DNA Translation: BAA04966.1
U00096 Genomic DNA Translation: AAC74656.1
AP009048 Genomic DNA Translation: BAA15286.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A55345

NCBI Reference Sequences

More...
RefSeqi
NP_416101.1, NC_000913.3
WP_001138581.1, NZ_STEB01000003.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC74656; AAC74656; b1584
BAA15286; BAA15286; BAA15286

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
61753249
946117

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW1576
eco:b1584

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.678

<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
D25276 Genomic DNA Translation: BAA04966.1
U00096 Genomic DNA Translation: AAC74656.1
AP009048 Genomic DNA Translation: BAA15286.1
PIRiA55345
RefSeqiNP_416101.1, NC_000913.3
WP_001138581.1, NZ_STEB01000003.1

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
4R9MX-ray2.90A/B/C1-186[»]
6CY6X-ray1.75A1-186[»]
SMRiP0A951
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4260234, 7 interactors
850477, 1 interactor
ComplexPortaliCPX-2133, Spermidine N(1)-acetyltransferase complex
IntActiP0A951, 11 interactors
STRINGi511145.b1584

Proteomic databases

jPOSTiP0A951
PaxDbiP0A951
PRIDEiP0A951

Genome annotation databases

EnsemblBacteriaiAAC74656; AAC74656; b1584
BAA15286; BAA15286; BAA15286
GeneIDi61753249
946117
KEGGiecj:JW1576
eco:b1584
PATRICifig|1411691.4.peg.678

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB2341

Phylogenomic databases

eggNOGiCOG1670, Bacteria
InParanoidiP0A951
PhylomeDBiP0A951

Enzyme and pathway databases

UniPathwayiUPA00211
UPA00250
BioCyciEcoCyc:SPERMACTRAN-MONOMER
MetaCyc:SPERMACTRAN-MONOMER
BRENDAi2.3.1.57, 2026

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P0A951

Family and domain databases

InterProiView protein in InterPro
IPR016181, Acyl_CoA_acyltransferase
IPR000182, GNAT_dom
PfamiView protein in Pfam
PF13302, Acetyltransf_3, 1 hit
SUPFAMiSSF55729, SSF55729, 1 hit
PROSITEiView protein in PROSITE
PS51186, GNAT, 1 hit

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 nameiATDA_ECOLI
<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: P0A951
Secondary accession number(s): P37354
<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: July 19, 2005
Last sequence update: January 23, 2007
Last modified: September 29, 2021
This is version 123 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, Direct protein sequencing, Reference proteome

Documents

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