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Entry version 11 (11 Dec 2019)
Sequence version 1 (02 Nov 2016)
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Protein

FAD-dependent monooxygenase sdnN

Gene

sdnN

Organism
Sordaria araneosa (Pleurage araneosa)
Status
Reviewed-Annotation score:

Annotation score:3 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

FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of sordarin and hypoxysordarin, glycoside antibiotics with a unique tetracyclic diterpene aglycone structure (PubMed:27072286).

First, the geranylgeranyl diphosphate synthase sdnC constructs GGDP from farnesyl diphosphate and isopentenyl diphosphate (PubMed:27072286).

The diterpene cyclase sdnA then catalyzes the cyclization of GGDP to afford cycloaraneosene (PubMed:27072286).

Cycloaraneosene is then hydroxylated four times by the putative cytochrome P450 monooxygenases sdnB, sdnE, sdnF and sdnH to give a hydroxylated cycloaraneosene derivative such as cycloaraneosene-8,9,13,19-tetraol (PubMed:27072286).

Although the order of the hydroxylations is unclear, at least C8, C9 and C13 of the cycloaraneosene skeleton are hydroxylated before the sordaricin formation (PubMed:27072286).

Dehydration of the 13-hydroxy group of the hydroxylated cycloaraneosene derivative might be catalyzed by an unassigned hypothetical protein such as sdnG and sdnP to construct the cyclopentadiene moiety (PubMed:27072286).

The FAD-dependent oxidoreductase sdnN is proposed to catalyze the oxidation at C9 of the hydroxylated cycloaraneosene derivative and also catalyze the Baeyer-Villiger oxidation to give the lactone intermediate (PubMed:27072286).

The presumed lactone intermediate would be hydrolyzed to give an acrolein moiety and a carboxylate moiety (PubMed:27072286).

Then, [4+2]cycloaddition would occur between the acrolein moiety and the cyclopentadiene moiety to give sordaricin (PubMed:27072286).

SdnN might also be involved in the [4+2]cycloaddition after the hypothesized oxidation to accommodate the oxidized product and prompt the [4+2]cycloaddition (PubMed:27072286).

GDP-6-deoxy-D-altrose may be biosynthesized from GDP-D-mannose by the putative GDP-mannose-4,6-dehydratase sdnI and the short-chain dehydrogenase sdnK (PubMed:27072286).

The glycosyltransferase sdnJ catalyzes the attachment of 6-deoxy-D-altrose onto the 19-hydroxy group of sordaricin to give 4'-O-demethylsordarin (PubMed:27072286).

The methyltransferase sdnD would complete the biosynthesis of sordarin (PubMed:27072286).

Sordarin can be further modified into hypoxysordarin (PubMed:27072286).

The unique acyl chain at the 3'-hydroxy group of hypoxysordarin would be constructed by an iterative type I PKS sdnO and the trans-acting polyketide methyltransferase sdnL. SdnL would be responsible for the introduction of an alpha-methyl group of the polyketide chain (PubMed:27072286).

Alternatively, the beta-lactamase-like protein sdnR might be responsible for the cleavage and transfer of the polyketide chain from the PKS sdnO to sordarin (PubMed:27072286).

Two putative cytochrome P450 monooxygenases, sdnQ and sdnT, might catalyze the epoxidations of the polyketide chain to complete the biosynthesis of hypoxysordarin (PubMed:27072286).

Transcriptional regulators sdnM and sdnS are presumably encoded for the transcriptional regulation of the expression of the sdn gene cluster (PubMed:27072286).

1 Publication

<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

FADCurated

<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: Antibiotic biosynthesis

This protein is involved in Antibiotic biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in Antibiotic biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei294FADBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi34 – 35FADBy similarity2
Nucleotide bindingi304 – 308FADBy similarity5

<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 functionOxidoreductase
Biological processAntibiotic biosynthesis
LigandFAD, Flavoprotein

<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:
FAD-dependent monooxygenase sdnN1 Publication (EC:1.-.-.-1 Publication)
Alternative name(s):
Sordarin/hypoxysordarin biosynthesis cluster protein N1 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:sdnN1 Publication
<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>OrganismiSordaria araneosa (Pleurage araneosa)
<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 identifieri573841 [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 lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeSordaria

<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 19Sequence analysisAdd BLAST19
<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_000044106420 – 432FAD-dependent monooxygenase sdnNAdd BLAST413

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi283N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1

Keywords - PTMi

Glycoprotein

<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

Keywords - Domaini

Signal

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.50.50.60, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR002938, FAD-bd
IPR036188, FAD/NAD-bd_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01494, FAD_binding_3, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51905, SSF51905, 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

A0A1B4XBH7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGSFKVIIVG GGPAGLVAAH ALHQAGIDFV VLERRGSVVD PSGASVVLNP
60 70 80 90 100
PAMRILSQFG LREQLEDAGA ELNHVKSFTN AGYNLGAAQV IYHRPELVRI
110 120 130 140 150
MYEGLPSDAR GKVLTDKKVT TIHQNPDSDT VTVSCSDGST YTGSIAIGAD
160 170 180 190 200
GAHSRTRQQL RQAMIRDGQP LSICDDEKPY ECAYRMLWCS FPRPDSIPPG
210 220 230 240 250
LGGETQGVDR TLALMVGKAS AMIICYEKLS EPTRERVEYS DKDMAQMFES
260 270 280 290 300
FADWPVTETL RFRDVFDSRT AGMANLHEGI VKNFSKGRVC LVSDSCHRYT
310 320 330 340 350
PNAGLGLNNG IQDVVALCNE IQAAVEQAGP ESEPSQEGIT KAFESYLNQR
360 370 380 390 400
LKLMKKDLRG SALLTRLQAW ASTLHYIMAR YLLVPDWVQR LTINYVAVPT
410 420 430
MRQAPVFKYI AAEEPYVGTT AWVHPIKPRT IT
Length:432
Mass (Da):47,494
Last modified:November 2, 2016 - 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:i861668B818631792
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
LC079035 Genomic DNA Translation: BAV32158.1

<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
LC079035 Genomic DNA Translation: BAV32158.1

3D structure databases

Database of comparative protein structure models

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ModBasei
Search...

SWISS-MODEL Interactive Workspace

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SWISS-MODEL-Workspacei
Submit a new modelling project...

Family and domain databases

Gene3Di3.50.50.60, 1 hit
InterProiView protein in InterPro
IPR002938, FAD-bd
IPR036188, FAD/NAD-bd_sf
PfamiView protein in Pfam
PF01494, FAD_binding_3, 1 hit
SUPFAMiSSF51905, SSF51905, 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 nameiSDNN_SORAA
<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: A0A1B4XBH7
<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: August 30, 2017
Last sequence update: November 2, 2016
Last modified: December 11, 2019
This is version 11 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

Documents

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