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Entry version 69 (02 Jun 2021)
Sequence version 1 (23 Jan 2007)
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Protein

Ophiobolin F synthase oblA

Gene

oblA

Organism
Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
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>
-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

Bifunctional sesterterpene synthase; part of the gene cluster that mediates the biosynthesis of the sesterterpenes ophiobolins, fungal phytotoxins with potential anti-cancer activities (PubMed:23324037, PubMed:27116000, PubMed:28362483).

The first step of the pathway is performed by the sesterterpene synthase oblA that possesses both prenyl transferase and terpene cyclase activity, converting isopentenyl diphosphate and dimethylallyl diphosphate into geranylfarnesyl diphosphate (GFPP) and further converting GFPP into ophiobolin F, respectively (PubMed:23324037).

Other sesterterpenoids (C(25) terpenoids) are found as minor products of oblA (PubMed:23324037).

It is expected that ophiobolin F is then oxidized to ophiobolin A via ophiobolin C and ophiobolin B intermediates by the combined action of the cytochome P450 monooxygenase oblB and the FAD-dependent oxidoreductase oblC (Probable). Although oblB catalyzes multistep oxygenations at C5 and C21/C7 in a relatively efficient manner, it is unable to convert ophiobolin F to ophiobolin C and produces instead several unexpected derivatives (PubMed:27116000).

1 Publication3 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 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+By similarityNote: Binds 4 Mg2+ ions per subunit.By similarity

<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=0.024 µM for geranylgeranyl diphosphate (GGDP)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: terpenoid biosynthesis

    This protein is involved in the pathway terpenoid biosynthesis, which is part of Secondary metabolite biosynthesis.1 Publication
    View all proteins of this organism that are known to be involved in the pathway terpenoid biosynthesis and in Secondary metabolite biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi93Magnesium 1By similarity1
    Metal bindingi93Magnesium 2By similarity1
    Metal bindingi97Magnesium 1By similarity1
    Metal bindingi97Magnesium 2By similarity1
    Metal bindingi468Magnesium 3By similarity1
    Metal bindingi468Magnesium 4By similarity1
    Metal bindingi472Magnesium 3By similarity1
    Metal bindingi472Magnesium 4By 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 functionLyase, Multifunctional enzyme, Transferase
    Biological processIsoprene biosynthesis
    LigandMagnesium, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:MONOMER-19519

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

    More...
    UniPathwayi
    UPA00213

    <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:
    Ophiobolin F synthase oblA1 Publication (EC:2.5.1.292 Publications, EC:2.5.1.812 Publications, EC:4.2.3.1452 Publications)
    Short name:
    acOS1 Publication
    Alternative name(s):
    Bifunctional sesterterpene synthase oblA1 Publication
    Ophiobolin biosynthesis cluster protein A1 Publication
    <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:oblA1 Publication
    ORF Names:ACLA_076850
    <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>OrganismiAspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
    <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 identifieri344612 [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 lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillusAspergillus subgen. Fumigati
    <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
    • UP000006701 <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: Unassembled WGS sequence

    Organism-specific databases

    Eukaryotic Pathogen, Vector and Host Database Resources

    More...
    VEuPathDBi
    FungiDB:ACLA_076850

    <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_00004307451 – 718Ophiobolin F synthase oblAAdd BLAST718

    <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

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    5057.CADACLAP00006804

    <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
    A1C8C3

    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

    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>Regioni1 – 320(7Z)-ophiobola-7,19-dien-3-ol synthase1 PublicationAdd BLAST320
    Regioni321 – 718Geranylfarnesyl diphosphate synthase1 PublicationAdd BLAST398
    Regioni346 – 391DisorderedSequence analysisAdd BLAST46

    Compositional bias

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi346 – 369Basic and acidic residuesSequence analysisAdd BLAST24
    Compositional biasi370 – 391Polar residuesSequence analysisAdd BLAST22

    <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

    In the N-terminal section; belongs to the terpene synthase family.Curated
    In the C-terminal section; belongs to the FPP/GGPP synthase family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG0777, Eukaryota

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_014015_10_0_1

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    HITHYIG

    Database of Orthologous Groups

    More...
    OrthoDBi
    981769at2759

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    1.10.600.10, 2 hits

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR008949, Isoprenoid_synthase_dom_sf
    IPR000092, Polyprenyl_synt
    IPR033749, Polyprenyl_synt_CS

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00348, polyprenyl_synt, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF48576, SSF48576, 2 hits

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00723, POLYPRENYL_SYNTHASE_1, 1 hit
    PS00444, POLYPRENYL_SYNTHASE_2, 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.

    A1C8C3-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MACKYSTLID SSLYDREGLC PGIDLRRHVA GELEEVGAFR AQEDWRRLVG
    60 70 80 90 100
    PLPKPYAGLL GPDFSFITGA VPECHPDRME IVAYALEFGF MHDDVIDTDV
    110 120 130 140 150
    NHASLDEVGH TLDQSRTGKI EDKGSDGKRQ MVTQIIREMM AIDPERAMTV
    160 170 180 190 200
    AKSWASGVRH SSRRKEDTNF KALEQYIPYR ALDVGYMLWH GLVTFGCAIT
    210 220 230 240 250
    IPNEEEEEAK RLIIPALVQA SLLNDLFSFE KEKNDANVQN AVLIVMNEHG
    260 270 280 290 300
    CSEEEARDIL KKRIRLECAN YLRNVKETNA RADVSDELKR YINVMQYTLS
    310 320 330 340 350
    GNAAWSTNCP RYNGPTKFNE LQLLRSEHGL AKYPSRWSQE NRTSGLVEGD
    360 370 380 390 400
    CHESKPNELK RKRNGVSVDD EMRTNGTNGA KKPAHVSQPS TDSIVLEDMV
    410 420 430 440 450
    QLARTCDLPD LSDTVILQPY RYLTSLPSKG FRDQAIDSIN KWLKVPPKSV
    460 470 480 490 500
    KMIKDVVKML HSASLMLDDL EDNSPLRRGK PSTHSIYGMA QTVNSATYQY
    510 520 530 540 550
    ITATDITAQL QNSETFHIFV EELQQLHVGQ SYDLYWTHNT LCPTIAEYLK
    560 570 580 590 600
    MVDMKTGGLF RMLTRMMIAE SPVVDKVPNS DMNLFSCLIG RFFQIRDDYQ
    610 620 630 640 650
    NLASADYAKA KGFAEDLDEG KYSFTLIHCI QTLESKPELA GEMMQLRAFL
    660 670 680 690 700
    MKRRHEGKLS QEAKQEVLVT MKKTESLQYT LSVLRELHSE LEKEVENLEA
    710
    KFGEENFTLR VMLELLKV
    Length:718
    Mass (Da):81,603
    Last modified:January 23, 2007 - 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:iACDF491AA26EFC9C
    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
    DS027045 Genomic DNA Translation: EAW14644.1

    NCBI Reference Sequences

    More...
    RefSeqi
    XP_001276070.1, XM_001276069.1

    Genome annotation databases

    Ensembl fungal genome annotation project

    More...
    EnsemblFungii
    EAW14644; EAW14644; ACLA_076850

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    4708281

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    act:ACLA_076850

    <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
    DS027045 Genomic DNA Translation: EAW14644.1
    RefSeqiXP_001276070.1, XM_001276069.1

    3D structure databases

    SMRiA1C8C3
    ModBaseiSearch...

    Protein-protein interaction databases

    STRINGi5057.CADACLAP00006804

    Genome annotation databases

    EnsemblFungiiEAW14644; EAW14644; ACLA_076850
    GeneIDi4708281
    KEGGiact:ACLA_076850

    Organism-specific databases

    VEuPathDBiFungiDB:ACLA_076850

    Phylogenomic databases

    eggNOGiKOG0777, Eukaryota
    HOGENOMiCLU_014015_10_0_1
    OMAiHITHYIG
    OrthoDBi981769at2759

    Enzyme and pathway databases

    UniPathwayiUPA00213
    BioCyciMetaCyc:MONOMER-19519

    Family and domain databases

    Gene3Di1.10.600.10, 2 hits
    InterProiView protein in InterPro
    IPR008949, Isoprenoid_synthase_dom_sf
    IPR000092, Polyprenyl_synt
    IPR033749, Polyprenyl_synt_CS
    PfamiView protein in Pfam
    PF00348, polyprenyl_synt, 1 hit
    SUPFAMiSSF48576, SSF48576, 2 hits
    PROSITEiView protein in PROSITE
    PS00723, POLYPRENYL_SYNTHASE_1, 1 hit
    PS00444, POLYPRENYL_SYNTHASE_2, 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 nameiOBLA_ASPCL
    <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: A1C8C3
    <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: October 29, 2014
    Last sequence update: January 23, 2007
    Last modified: June 2, 2021
    This is version 69 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 programFungal 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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