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Entry version 124 (11 Dec 2019)
Sequence version 2 (15 Feb 2017)
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Protein

Acetyl-CoA acetyltransferase

Gene

phaA

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Status
Reviewed-Annotation score:

Annotation score:4 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>
-Protein inferred from homologyi <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

When expressed in E.coli with Synechocystis PhaB, PhaC and PhaE confers the ability to synthesize up to 12% (w/w) poly(3-hydroxybutyrate) (PHB) depending on the carbon source.1 Publication

Miscellaneous

Nitrogen-free medium induces chlorosis in Synechocystis, leading to the degradation of the photosynthetic apparatus and concomitant accumulation of cytoplasmic polyhydroxyalkanoic acid (PHA) granules which in this cyanobacterium are composed of PHB.Curated

<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 the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: poly-(R)-3-hydroxybutanoate biosynthesis

This protein is involved in the pathway poly-(R)-3-hydroxybutanoate biosynthesis, which is part of Biopolymer metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway poly-(R)-3-hydroxybutanoate biosynthesis and in Biopolymer metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei88Acyl-thioester intermediateBy similarity1
Active sitei352Proton acceptorBy similarity1
Active sitei382Proton acceptorBy similarity1

<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 processPHB biosynthesis

Enzyme and pathway databases

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

More...
UniPathwayi
UPA00917

<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:
Acetyl-CoA acetyltransferasePROSITE-ProRule annotation (EC:2.3.1.9PROSITE-ProRule annotation)
Alternative name(s):
Beta-ketothiolase PhaA1 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:phaA1 Publication
Ordered Locus Names:slr1993
<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>OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
<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 identifieri1111708 [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 lineageiBacteriaCyanobacteriaSynechococcalesMerismopediaceaeSynechocystisunclassified Synechocystis
<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
  • UP000001425 <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 use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

Poly(3-hydroxyalkanoic acids) (PHA), of which PHB is among the most common compounds, are prokaryotic intracellular storage compounds with potential uses as renewable, biodegradable thermoplastics. Cyanobacterial PHB synthesis is particularly attractive as cyanobacteria use CO2 as the carbon source.Curated

<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

Double deletion of phaA and phaB leads to loss of synthesis of PHB, no visible growth phenotype.1 Publication

<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_00004388301 – 396Acetyl-CoA acetyltransferaseAdd BLAST396

Proteomic databases

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

More...
PaxDbi
P73825

PRoteomics IDEntifications database

More...
PRIDEi
P73825

<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

Homotetramer (By similarity).

By similarity

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P73825, 1 interactor

STRING: functional protein association networks

More...
STRINGi
1148.1652965

<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
P73825

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

<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

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000012238

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P73825

KEGG Orthology (KO)

More...
KOi
K00626

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P73825

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00751 thiolase, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.47.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR002155 Thiolase
IPR016039 Thiolase-like
IPR020610 Thiolase_AS
IPR020617 Thiolase_C
IPR020613 Thiolase_CS
IPR020616 Thiolase_N

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02803 Thiolase_C, 1 hit
PF00108 Thiolase_N, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000429 Ac-CoA_Ac_transf, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53901 SSF53901, 2 hits

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01930 AcCoA-C-Actrans, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00737 THIOLASE_2, 1 hit
PS00099 THIOLASE_3, 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.

P73825-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRDVFIVAAK RTPLGRFGGS LTNFSAADLG AHVMKSVLAQ AGVGGDQLDL
60 70 80 90 100
YIMGNVLRAG HGQLIPRQAA LKAEIPDTVD GYAVDMVCSS AMMSVINAAL
110 120 130 140 150
TIRAGEGDLI LAGGTESMSQ TGFYLSHRAR WGYKFLMGAP ENLTDLLLHD
160 170 180 190 200
GLTDSTNGEG MGEQTEKLAA EHGFSRIELD EVACLSQQRA AHATESGYFD
210 220 230 240 250
SEIAPIEITS RKGTQVLASD EGIRSDTTVE SLGKLRSAFA KDGVLTAGNC
260 270 280 290 300
SQITDGAAAL LLASGEAVEK YQLKPLAKIL GGSWAAGTPS RFPELPITAS
310 320 330 340 350
QKLLAKLDKT LADFDLFENN EAFSVSNLLF ERRLGVDRDK LNVNGGAIAL
360 370 380 390
GHPIGASGAR IMVTLLYALQ QRDKTLGLAA LCHGTGGGTA IALERV
Length:396
Mass (Da):41,710
Last modified:February 15, 2017 - 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:i418BC995D54F8776
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 BAA17882 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
BA000022 Genomic DNA Translation: BAA17882.1 Different initiation.

Protein sequence database of the Protein Information Resource

More...
PIRi
S75020

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
BAA17882; BAA17882; BAA17882

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
syn:slr1993

<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
BA000022 Genomic DNA Translation: BAA17882.1 Different initiation.
PIRiS75020

3D structure databases

SMRiP73825
ModBaseiSearch...

Protein-protein interaction databases

IntActiP73825, 1 interactor
STRINGi1148.1652965

Proteomic databases

PaxDbiP73825
PRIDEiP73825

Genome annotation databases

EnsemblBacteriaiBAA17882; BAA17882; BAA17882
KEGGisyn:slr1993

Phylogenomic databases

HOGENOMiHOG000012238
InParanoidiP73825
KOiK00626
PhylomeDBiP73825

Enzyme and pathway databases

UniPathwayiUPA00917

Family and domain databases

CDDicd00751 thiolase, 1 hit
Gene3Di3.40.47.10, 2 hits
InterProiView protein in InterPro
IPR002155 Thiolase
IPR016039 Thiolase-like
IPR020610 Thiolase_AS
IPR020617 Thiolase_C
IPR020613 Thiolase_CS
IPR020616 Thiolase_N
PfamiView protein in Pfam
PF02803 Thiolase_C, 1 hit
PF00108 Thiolase_N, 1 hit
PIRSFiPIRSF000429 Ac-CoA_Ac_transf, 1 hit
SUPFAMiSSF53901 SSF53901, 2 hits
TIGRFAMsiTIGR01930 AcCoA-C-Actrans, 1 hit
PROSITEiView protein in PROSITE
PS00737 THIOLASE_2, 1 hit
PS00099 THIOLASE_3, 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 nameiTHIL_SYNY3
<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: P73825
<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 15, 2017
Last sequence update: February 15, 2017
Last modified: December 11, 2019
This is version 124 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

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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