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Entry version 124 (02 Jun 2021)
Sequence version 1 (01 Feb 1995)
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Protein

Acetoin utilization protein AcuA

Gene

acuA

Organism
Bacillus subtilis (strain 168)
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

Part of the acuABC operon, which is possibly involved in the breakdown of acetoin and butanediol. Acts as an acetyltransferase inactivating acetyl-CoA synthetase AcsA via acetylation at a Lys residue.

4 Publications

<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

Activity is sensitive to salt concentration, a high concentration of KCL (500 mM) is needed for complete inactivation.1 Publication

<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=22 mM for acetyl-CoA2 Publications
  1. Vmax=0.8 mmol/min/mg enzyme2 Publications

pH dependencei

Optimum pH is 7.5.2 Publications

Temperature dependencei

Optimum temperature 37 degrees Celsius. Thermostable. Retains 93, 78 and 15 % of its protein acetyltransferase activity after heating to 100 degrees Celsius for 5, 30 and 60 minutes, respectively.2 Publications

<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: acetoin degradation

This protein is involved in the pathway acetoin degradation, which is part of Ketone degradation.
View all proteins of this organism that are known to be involved in the pathway acetoin degradation and in Ketone degradation.

<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

<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
Biological processAcetoin catabolism, Sporulation

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
BSUB:BSU29690-MONOMER

BRENDA Comprehensive Enzyme Information System

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BRENDAi
2.3.1.B34, 658

SABIO-RK: Biochemical Reaction Kinetics Database

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SABIO-RKi
P39065

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

More...
UniPathwayi
UPA00040

<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:
Acetoin utilization protein AcuA (EC:2.3.1.-)
Alternative name(s):
Protein acetyltransferase AcuA
<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:acuA
Ordered Locus Names:BSU29690
<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>OrganismiBacillus subtilis (strain 168)
<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 identifieri224308 [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 lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
<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
  • UP000001570 <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 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

Does not impair growth on acetate. Disruption together with other acetoin utilization genes acuB and acuC results in poor growth and sporulation on acetoin or butanediol. Triple deletion of acuA, acuC and srtN improves the growth on acetate but it does not reach that of wild-type under low-acetate conditions.3 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>Mutagenesisi43R → H: 25% retention of activity. Two to three-fold reduction in KM for acetyl-CoA. Three-fold slower turnover number. Retains 54% of the activity of the wild-type after heating it to 100 degrees Celsius for 30 minutes. 1 Publication1
Mutagenesisi170T → A: 25% retention of activity. Two to three fold reduction in KM for acetyl-CoA. Three-fold slower turnover number. Retains 60% of the activity of the wild-type after heating it to 100 degrees Celsius for 30 minutes. 1 Publication1
Mutagenesisi178H → P: Inactive. Leads to a rapid turnover of the enzyme. 1 Publication1
Mutagenesisi188G → E: Inactive. Leads to a rapid turnover of the enzyme. 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000745711 – 210Acetoin utilization protein AcuAAdd BLAST210

Proteomic databases

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

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PaxDbi
P39065

PRoteomics IDEntifications database

More...
PRIDEi
P39065

<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

Expression is maximal in stationary phase and is repressed by the addition of glucose to the growth medium. CcpA protein is required for glucose repression. Acetoin does not act as an inducer. Up-regulated during the 80 to 100 minutes of spore germination and into the outgrowth phase.2 Publications

<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

Monomer.

1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
224308.BSU29690

<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

3D structure databases

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

More...
SMRi
P39065

Database of comparative protein structure models

More...
ModBasei
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>Domaini20 – 161N-acetyltransferasePROSITE-ProRule annotationAdd BLAST142

<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

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eggNOGi
COG0454, Bacteria

Identification of Orthologs from Complete Genome Data

More...
OMAi
KIMEKMM

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P39065

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR024699, AcuA
IPR016181, Acyl_CoA_acyltransferase
IPR000182, GNAT_dom

Pfam protein domain database

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

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF021278, AcuA, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF55729, SSF55729, 1 hit

PROSITE; a protein domain and family database

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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.

P39065-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEHHKTYHSA NIKTATGSLL IEGPVSPEDL AGYEFHKDLT AFRPPREQHE
60 70 80 90 100
ALVDIAGLPE GRIIIARDGR TIVGYVTYLY PDPLERWSEG NMEDLIELGA
110 120 130 140 150
IEVAPDYRGC AVGKTLLTVS MMDEQMENYI VMTTEYYWHW DLKGMKKDVW
160 170 180 190 200
EYRKIMEKMM NAGGLVWFAT DEPEISSHPA NCLMARIGKN VSQESIEQFD
210
RLRFYHRYMY
Length:210
Mass (Da):24,333
Last modified:February 1, 1995 - v1
<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:i74DB94A46E8556DA
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
L17309 Genomic DNA Translation: AAA68286.1
AF008220 Genomic DNA Translation: AAC00396.1
AL009126 Genomic DNA Translation: CAB14947.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S39645

NCBI Reference Sequences

More...
RefSeqi
NP_390847.1, NC_000964.3
WP_003229296.1, NZ_JNCM01000036.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CAB14947; CAB14947; BSU_29690

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
937633

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bsu:BSU29690

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|224308.179.peg.3227

<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
L17309 Genomic DNA Translation: AAA68286.1
AF008220 Genomic DNA Translation: AAC00396.1
AL009126 Genomic DNA Translation: CAB14947.1
PIRiS39645
RefSeqiNP_390847.1, NC_000964.3
WP_003229296.1, NZ_JNCM01000036.1

3D structure databases

SMRiP39065
ModBaseiSearch...

Protein-protein interaction databases

STRINGi224308.BSU29690

Proteomic databases

PaxDbiP39065
PRIDEiP39065

Genome annotation databases

EnsemblBacteriaiCAB14947; CAB14947; BSU_29690
GeneIDi937633
KEGGibsu:BSU29690
PATRICifig|224308.179.peg.3227

Phylogenomic databases

eggNOGiCOG0454, Bacteria
OMAiKIMEKMM
PhylomeDBiP39065

Enzyme and pathway databases

UniPathwayiUPA00040
BioCyciBSUB:BSU29690-MONOMER
BRENDAi2.3.1.B34, 658
SABIO-RKiP39065

Family and domain databases

InterProiView protein in InterPro
IPR024699, AcuA
IPR016181, Acyl_CoA_acyltransferase
IPR000182, GNAT_dom
PfamiView protein in Pfam
PF00583, Acetyltransf_1, 1 hit
PIRSFiPIRSF021278, AcuA, 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 nameiACUA_BACSU
<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: P39065
<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: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 2, 2021
This is version 124 of the entry and version 1 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

Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
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