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UniProtKB - P0A6R0 (FABH_ECOLI)

Entry version 138 (07 Apr 2021)
Sequence version 1 (10 May 2005)
Previous versions | rss
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Protein

3-oxoacyl-[acyl-carrier-protein] synthase 3

Gene

fabH

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

Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for acetyl-CoA. Its substrate specificity determines the biosynthesis of straight-chain of fatty acids instead of branched-chain (PubMed:7592873, PubMed:8631920, PubMed:8910376, PubMed:10629181). Can also use propionyl-CoA, with lower efficiency (PubMed:8631920, PubMed:10629181).4 Publications

Miscellaneous

Inhibited by the SB418011 antibiotic. Not inhibited by cerulenin and thiolactomycin.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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%5Fsection">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

Negatively regulated by acyl-ACP, possibly by binding to either the free enzyme or the acyl-enzyme intermediate.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=40 µM for acetyl-CoA1 Publication
  2. KM=5 µM for malonyl-[ACP]1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: fatty acid biosynthesis

    This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.UniRule annotation
    View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei1123 Publications1
    Active sitei2443 Publications1
    Active sitei2743 Publications1

    <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

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    • fatty acid biosynthetic process Source: UniProtKB-UniRule
    • fatty acid metabolic process Source: CACAO
    Complete GO annotation on QuickGO ...

    <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, Multifunctional enzyme, Transferase
    Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

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

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		2.3.1.180, 2026

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

    More...    UniPathwayi    		UPA00094

    Chemistry databases

    SwissLipids knowledge resource for lipid biology

    More...    SwissLipidsi    		SLP:000000852

    <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%5Fand%5Ftaxonomy%5Fsection">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:
    3-oxoacyl-[acyl-carrier-protein] synthase 3UniRule annotation (EC:2.3.1.180UniRule annotation4 Publications)
    Alternative name(s):
    3-oxoacyl-[acyl-carrier-protein] synthase IIIUniRule annotation
    Beta-ketoacyl-ACP synthase IIIUniRule annotation
    Short name:
    KAS IIIUniRule annotation
    EcFabH
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:fabH
    Ordered Locus Names:b1091, JW1077
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi112C → S: Loss of activity. 1
    Mutagenesisi214K → E or A: Strongly reduces the binding to malonyl-ACP but not that of the substrate. 1 Publication1
    Mutagenesisi244H → A: Loss of activity. 1
    Mutagenesisi249R → E or A: Abolishes the binding to malonyl-ACP but not that of the substrate. 1 Publication1
    Mutagenesisi253A → Y: Abolishes both binding to malonyl-ACP and binding to substrate. 1 Publication1
    Mutagenesisi256 – 257KK → AA: Strongly reduces both binding to malonyl-ACP and binding to substrate. 1 Publication2
    Mutagenesisi256 – 257KK → EE: Abolishes the binding to malonyl-ACP but not that of the substrate. 1 Publication2
    Mutagenesisi274N → A: Loss of activity. 1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...    ChEMBLi    		CHEMBL4914

    Drug and drug target database

    More...    DrugBanki    		DB02316, 1-(5-Carboxypentyl)-5-[(2,6-Dichlorobenzyl)Oxy]-1 H-Indole-2-Carboxylic Acid
    DB01034, Cerulenin
    DB01992, Coenzyme A
    DB03661, L-cysteic acid
    DB04524, Malonyl-CoA
    DB02039, S-Acetyl-Cysteine

    DrugCentral

    More...    DrugCentrali    		P0A6R0

    <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_00001104241 – 3173-oxoacyl-[acyl-carrier-protein] synthase 3Add BLAST317

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		P0A6R0

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

    More...    PaxDbi    		P0A6R0

    PRoteomics IDEntifications database

    More...    PRIDEi    		P0A6R0

    PTM databases

    CarbonylDB database of protein carbonylation sites

    More...    CarbonylDBi    		P0A6R0

    <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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer.

    UniRule annotation

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...    BioGRIDi    		4261031, 467 interactors

    Database of interacting proteins

    More...    DIPi    		DIP-48255N

    Protein interaction database and analysis system

    More...    IntActi    		P0A6R0, 5 interactors

    STRING: functional protein association networks

    More...    STRINGi    		511145.b1091

    <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

    1317
    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    		P0A6R0

    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    		P0A6R0

    <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

    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>Regioni245 – 249ACP-binding5

    <p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH.UniRule annotation1 Publication

    <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 thiolase-like superfamily. FabH family.UniRule annotationCurated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		COG0332, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		CLU_039592_4_1_6

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P0A6R0

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P0A6R0

    Family and domain databases

    Conserved Domains Database

    More...    CDDi    		cd00830, KAS_III, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		3.40.47.10, 1 hit

    HAMAP database of protein families

    More...    HAMAPi    		MF_01815, FabH, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR013751, ACP_syn_III
    IPR013747, ACP_syn_III_C
    IPR004655, FabH_synth
    IPR016039, Thiolase-like

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF08545, ACP_syn_III, 1 hit
    PF08541, ACP_syn_III_C, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF53901, SSF53901, 1 hit

    TIGRFAMs; a protein family database

    More...    TIGRFAMsi    		TIGR00747, fabH, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

    P0A6R0-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MYTKIIGTGS YLPEQVRTNA DLEKMVDTSD EWIVTRTGIR ERHIAAPNET 
            60         70         80         90        100
    VSTMGFEAAT RAIEMAGIEK DQIGLIVVAT TSATHAFPSA ACQIQSMLGI 
           110        120        130        140        150
    KGCPAFDVAA ACAGFTYALS VADQYVKSGA VKYALVVGSD VLARTCDPTD 
           160        170        180        190        200
    RGTIIIFGDG AGAAVLAASE EPGIISTHLH ADGSYGELLT LPNADRVNPE 
           210        220        230        240        250
    NSIHLTMAGN EVFKVAVTEL AHIVDETLAA NNLDRSQLDW LVPHQANLRI 
           260        270        280        290        300
    ISATAKKLGM SMDNVVVTLD RHGNTSAASV PCALDEAVRD GRIKPGQLVL 
           310 
    LEAFGGGFTW GSALVRF
    Length:317
    Mass (Da):33,515
    Last modified:May 10, 2005 - 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:iBF3192CFF36023D3
    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
    		M77744 Genomic DNA Translation: AAA23749.1
    M96793 Genomic DNA Translation: AAB59065.1
    U00096 Genomic DNA Translation: AAC74175.1
    AP009048 Genomic DNA Translation: BAA35899.2
    M87040 Genomic DNA Translation: AAA23741.1
    Z11565 Genomic DNA Translation: CAA77659.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		A42431

    NCBI Reference Sequences

    More...    RefSeqi    		NP_415609.1, NC_000913.3
    WP_000288132.1, NZ_STEB01000016.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAC74175; AAC74175; b1091
    BAA35899; BAA35899; BAA35899

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		58461211
    946003

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ecj:JW1077
    eco:b1091

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|1411691.4.peg.1177

    <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
    		M77744 Genomic DNA Translation: AAA23749.1
    M96793 Genomic DNA Translation: AAB59065.1
    U00096 Genomic DNA Translation: AAC74175.1
    AP009048 Genomic DNA Translation: BAA35899.2
    M87040 Genomic DNA Translation: AAA23741.1
    Z11565 Genomic DNA Translation: CAA77659.1
    PIRiA42431
    RefSeqiNP_415609.1, NC_000913.3
    WP_000288132.1, NZ_STEB01000016.1

    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
    1EBLX-ray1.80A/B1-317[»]
    1HN9X-ray2.00A/B1-317[»]
    1HNDX-ray1.60A1-317[»]
    1HNHX-ray1.90A1-317[»]
    1HNJX-ray1.46A1-317[»]
    1HNKX-ray1.90A1-317[»]
    1MZSX-ray2.10A1-317[»]
    2EFTX-ray2.00A/B1-317[»]
    2GYOX-ray2.00A/B1-317[»]
    3IL9X-ray1.85A/B1-317[»]
    4Z8DX-ray2.00A/B1-317[»]
    5BNMX-ray1.70A/B1-317[»]
    5BNRX-ray1.89A1-317[»]
    5BNSX-ray2.20A/B1-317[»]
    SMRiP0A6R0
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi4261031, 467 interactors
    DIPiDIP-48255N
    IntActiP0A6R0, 5 interactors
    STRINGi511145.b1091

    Chemistry databases

    ChEMBLiCHEMBL4914
    DrugBankiDB02316, 1-(5-Carboxypentyl)-5-[(2,6-Dichlorobenzyl)Oxy]-1 H-Indole-2-Carboxylic Acid
    DB01034, Cerulenin
    DB01992, Coenzyme A
    DB03661, L-cysteic acid
    DB04524, Malonyl-CoA
    DB02039, S-Acetyl-Cysteine
    DrugCentraliP0A6R0
    SwissLipidsiSLP:000000852

    PTM databases

    CarbonylDBiP0A6R0

    Proteomic databases

    jPOSTiP0A6R0
    PaxDbiP0A6R0
    PRIDEiP0A6R0

    Genome annotation databases

    EnsemblBacteriaiAAC74175; AAC74175; b1091
    BAA35899; BAA35899; BAA35899
    GeneIDi58461211
    946003
    KEGGiecj:JW1077
    eco:b1091
    PATRICifig|1411691.4.peg.1177

    Organism-specific databases

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

    More...    EchoBASEi    		EB0273

    Phylogenomic databases

    eggNOGiCOG0332, Bacteria
    HOGENOMiCLU_039592_4_1_6
    InParanoidiP0A6R0
    PhylomeDBiP0A6R0

    Enzyme and pathway databases

    UniPathwayiUPA00094
    BioCyciEcoCyc:FABH-MONOMER
    MetaCyc:FABH-MONOMER
    BRENDAi2.3.1.180, 2026

    Miscellaneous databases

    EvolutionaryTraceiP0A6R0

    Protein Ontology

    More...    PROi    		PR:P0A6R0

    Family and domain databases

    CDDicd00830, KAS_III, 1 hit
    Gene3Di3.40.47.10, 1 hit
    HAMAPiMF_01815, FabH, 1 hit
    InterProiView protein in InterPro
    IPR013751, ACP_syn_III
    IPR013747, ACP_syn_III_C
    IPR004655, FabH_synth
    IPR016039, Thiolase-like
    PfamiView protein in Pfam
    PF08545, ACP_syn_III, 1 hit
    PF08541, ACP_syn_III_C, 1 hit
    SUPFAMiSSF53901, SSF53901, 1 hit
    TIGRFAMsiTIGR00747, fabH, 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 nameiFABH_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: P0A6R0
    Secondary accession number(s): P24249
    <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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 10, 2005
    Last sequence update: May 10, 2005
    Last modified: April 7, 2021
    This is version 138 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

    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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