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Entry version 39 (07 Apr 2021)
Sequence version 1 (16 Apr 2014)
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Protein

3-oxoacyl-[acyl-carrier-protein] synthase 1

Gene

kasA

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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 mycobacterial fatty acid elongation system FAS-II, which is involved in mycolic acid biosynthesis. Catalyzes the elongation of long chain acyl-ACP substrates by the addition of two carbons from malonyl-ACP to an acyl acceptor (PubMed:11600501, PubMed:12023885, PubMed:12464486, PubMed:16873379, PubMed:22017312, PubMed:24108128). Involved in the initial extension of the mycolate chain and forms monounsaturated fatty acids that averaged 40 carbons in length (PubMed:12464486).6 Publications

Miscellaneous

Identified as a drug target (PubMed:10747933, PubMed:12023885, PubMed:22076471, PubMed:27581223, PubMed:32196311, PubMed:32197094). Inhibited by isoniazid (INH), thiolactomycin (TLM) and related analogs (PubMed:10747933, PubMed:12464486, PubMed:19604480, PubMed:24108128). Highly sensitive to cerulenin (PubMed:12023885). Is the biological target of GSK3011724A, an indazole sulfonamide (PubMed:27581223). Inhibited by the indazole JSF-3285, which is a promising preclinical candidate for tuberculosis (PubMed:32197094).9 Publications

<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

Phosphorylation decreases the condensation activity.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

kcat is 5.3 min(-1) with hexadecanoyl-[ACP] as substrate. kcat is 4.5 min(-1) with eicosanoyl-[ACP] as substrate. kcat is 4.8 min(-1) with malonyl-[ACP] as substrate (PubMed:11600501). kcat is 21 min(-1) with malonyl-CoA as substrate. kcat is 28 min(-1) with malonyl-AcpM as substrate. kcat is 5 min(-1) with hexadecanoyl-CoA as substrate (PubMed:22017312).2 Publications
  1. KM=3.2 µM for hexadecanoyl-[ACP]1 Publication
  2. KM=18.7 µM for hexadecanoyl-[ACP]1 Publication
  3. KM=2.5 µM for eicosanoyl-[ACP]1 Publication
  4. KM=13.5 µM for malonyl-[ACP]1 Publication
  5. KM=11.8 µM for malonyl-[ACP]1 Publication
  6. KM=5.8 µM for malonyl-AcpM (in the presence of hexadecanoyl-AcpM)1 Publication
  7. KM=0.4 µM for hexadecanoyl-CoA (in the presence of malonyl-AcpM)1 Publication
  8. KM=9.0 µM for malonyl-CoA (in the presence of hexadecanoyl-AcpM)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: mycolic acid biosynthesis

    This protein is involved in the pathway mycolic acid biosynthesis, which is part of Lipid metabolism.2 Publications2 Publications
    View all proteins of this organism that are known to be involved in the pathway mycolic 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 sitei1713 Publications1
    <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>Sitei171Interacts with the inhibitor thiolactomycin2 Publications1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei311Substrate2 Publications1
    Sitei311Interacts with the inhibitor thiolactomycin2 Publications1
    Binding sitei345Substrate2 Publications1
    Sitei345Interacts with the inhibitor thiolactomycin2 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

    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 processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:G185E-6461-MONOMER

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

    More...
    UniPathwayi
    UPA00915

    Chemistry databases

    SwissLipids knowledge resource for lipid biology

    More...
    SwissLipidsi
    SLP:000000962

    <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 1 (EC:2.3.1.2933 Publications)
    Alternative name(s):
    Beta-ketoacyl-ACP synthase 1
    Short name:
    KAS 1
    Beta-ketoacyl-acyl carrier protein synthase KasA1 Publication
    Meromycolic acid 3-oxoacyl-(acyl carrier protein) synthase I
    <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:kasA1 Publication
    Ordered Locus Names:Rv2245
    ORF Names:MTCY427.26
    <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>OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
    <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 identifieri83332 [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 lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
    <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
    • UP000001584 <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

    Organism-specific databases

    Mycobacterium tuberculosis strain H37Rv genome database

    More...
    TubercuListi
    Rv2245

    <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>Mutagenesisi66D → N: Increases resistance to isoniazid. 1 Publication1
    Mutagenesisi171C → A: Loss of activity with hexadecanoyl-CoA. 1 Publication1
    Mutagenesisi171C → Q: Mimics structural changes caused by acyl-enzyme formation. 1 Publication1
    Mutagenesisi269G → S: Increases resistance to isoniazid. 1 Publication1
    Mutagenesisi311H → A: Loss of activity with hexadecanoyl-CoA. 1 Publication1
    Mutagenesisi312G → S: Increases resistance to isoniazid. 1 Publication1
    Mutagenesisi340K → A: Loss of activity with hexadecanoyl-CoA. 1 Publication1
    Mutagenesisi345H → A: Loss of activity with hexadecanoyl-CoA. 1 Publication1
    Mutagenesisi413F → L: Increases resistance to isoniazid. 1 Publication1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL4544

    Drug and drug target database

    More...
    DrugBanki
    DB04302, 4-Hydroxy-3,5-Dimethyl-5-(2-Methyl-Buta-1,3-Dienyl)-5h-Thiophen-2-One

    <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_00001803331 – 4163-oxoacyl-[acyl-carrier-protein] synthase 1Add BLAST416

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    Phosphorylated in vitro by several Ser/Thr protein kinases (STPKs). Highly phosphorylated in vivo on threonines. Can be dephosphorylated by the Ser/Thr phosphatase PstP.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

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

    More...
    PaxDbi
    P9WQD9

    <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.

    1 Publication

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    P9WQD9
    With#Exp.IntAct
    itself2EBI-15793653,EBI-15793653

    GO - Molecular functioni

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    83332.Rv2245

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P9WQD9

    <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

    1416
    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
    P9WQD9

    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

    <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

    Phe-404 residue probably plays a key role in the activation of the enzyme at the beginning of the catalytic cycle. A conformational change of Phe-404, possibly triggered by the substrate, is central for the activation because it switches KasA to the sufficiently reactive zwitterionic state.1 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

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    COG0304, Bacteria

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    YAYLSMQ

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P9WQD9

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00834, KAS_I_II, 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
    IPR000794, Beta-ketoacyl_synthase
    IPR014031, Ketoacyl_synth_C
    IPR014030, Ketoacyl_synth_N
    IPR020841, PKS_Beta-ketoAc_synthase_dom
    IPR016039, Thiolase-like

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR11712, PTHR11712, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00109, ketoacyl-synt, 1 hit
    PF02801, Ketoacyl-synt_C, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00825, PKS_KS, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF53901, SSF53901, 2 hits

    <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.

    P9WQD9-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSQPSTANGG FPSVVVTAVT ATTSISPDIE STWKGLLAGE SGIHALEDEF
    60 70 80 90 100
    VTKWDLAVKI GGHLKDPVDS HMGRLDMRRM SYVQRMGKLL GGQLWESAGS
    110 120 130 140 150
    PEVDPDRFAV VVGTGLGGAE RIVESYDLMN AGGPRKVSPL AVQMIMPNGA
    160 170 180 190 200
    AAVIGLQLGA RAGVMTPVSA CSSGSEAIAH AWRQIVMGDA DVAVCGGVEG
    210 220 230 240 250
    PIEALPIAAF SMMRAMSTRN DEPERASRPF DKDRDGFVFG EAGALMLIET
    260 270 280 290 300
    EEHAKARGAK PLARLLGAGI TSDAFHMVAP AADGVRAGRA MTRSLELAGL
    310 320 330 340 350
    SPADIDHVNA HGTATPIGDA AEANAIRVAG CDQAAVYAPK SALGHSIGAV
    360 370 380 390 400
    GALESVLTVL TLRDGVIPPT LNYETPDPEI DLDVVAGEPR YGDYRYAVNN
    410
    SFGFGGHNVA LAFGRY
    Length:416
    Mass (Da):43,316
    Last modified:April 16, 2014 - 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:iD2187BE2F0B56C7F
    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
    AL123456 Genomic DNA Translation: CCP45025.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A70779

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_216761.1, NC_000962.3
    WP_003411571.1, NZ_NVQJ01000008.1

    Genome annotation databases

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    45426225
    887269

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    mtu:Rv2245

    <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
    AL123456 Genomic DNA Translation: CCP45025.1
    PIRiA70779
    RefSeqiNP_216761.1, NC_000962.3
    WP_003411571.1, NZ_NVQJ01000008.1

    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
    2WGDX-ray2.01A1-416[»]
    2WGEX-ray1.80A1-416[»]
    2WGFX-ray2.15A/B/C/D/E/F/G/H1-416[»]
    2WGGX-ray2.00A/B/C/D/E/F/G/H1-416[»]
    5LD8X-ray2.13A/B2-416[»]
    6P9KX-ray1.70A3-416[»]
    6P9LX-ray2.31A3-416[»]
    6P9MX-ray2.26A3-416[»]
    6Y2IX-ray1.53AAA/BBB2-416[»]
    6Y2JX-ray2.89AAA/BBB/CCC/DDD/EEE/FFF/GGG/HHH2-416[»]
    SMRiP9WQD9
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    STRINGi83332.Rv2245

    Chemistry databases

    BindingDBiP9WQD9
    ChEMBLiCHEMBL4544
    DrugBankiDB04302, 4-Hydroxy-3,5-Dimethyl-5-(2-Methyl-Buta-1,3-Dienyl)-5h-Thiophen-2-One
    SwissLipidsiSLP:000000962

    Proteomic databases

    PaxDbiP9WQD9

    Genome annotation databases

    GeneIDi45426225
    887269
    KEGGimtu:Rv2245

    Organism-specific databases

    TubercuListiRv2245

    Phylogenomic databases

    eggNOGiCOG0304, Bacteria
    OMAiYAYLSMQ
    PhylomeDBiP9WQD9

    Enzyme and pathway databases

    UniPathwayiUPA00915
    BioCyciMetaCyc:G185E-6461-MONOMER

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:P9WQD9

    Family and domain databases

    CDDicd00834, KAS_I_II, 1 hit
    Gene3Di3.40.47.10, 2 hits
    InterProiView protein in InterPro
    IPR000794, Beta-ketoacyl_synthase
    IPR014031, Ketoacyl_synth_C
    IPR014030, Ketoacyl_synth_N
    IPR020841, PKS_Beta-ketoAc_synthase_dom
    IPR016039, Thiolase-like
    PANTHERiPTHR11712, PTHR11712, 1 hit
    PfamiView protein in Pfam
    PF00109, ketoacyl-synt, 1 hit
    PF02801, Ketoacyl-synt_C, 1 hit
    SMARTiView protein in SMART
    SM00825, PKS_KS, 1 hit
    SUPFAMiSSF53901, SSF53901, 2 hits

    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 nameiKASA_MYCTU
    <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: P9WQD9
    Secondary accession number(s): L0T991, P63454, Q10524
    <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: April 16, 2014
    Last sequence update: April 16, 2014
    Last modified: April 7, 2021
    This is version 39 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, 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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