Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 18 (02 Jun 2021)
Sequence version 1 (07 Sep 2016)
Previous versions | rss
Add a publicationFeedback

Acyl-CoA ligase lcsD



Purpureocillium lilacinum (Paecilomyces lilacinus)
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>
-Experimental evidence at transcript 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

Acyl-CoA ligase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic (PubMed:27416025).

Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and lcsC, have been identified in the cluster and it is not clear which is the one that assembles 4-methylhex-2-enoic acid since both contain KS, AT, DH, cMT, ER, KR and ACP domains (Probable). The polyketide residue might be transferred to the NRPS lcsA, mediated by two additional enzymes, the acyl-CoA ligase lcsD and the thioesterase lcsE. The linear polyketide carboxylic acid, which is released from PKS, is converted to a CoA thioester by lcsD, and then lcsE hydrolyzes the thiol bond and shuttles the polyketide intermediate to lcsA (Probable). The C domain of the first module catalyzed the condensation of 4-methylhex-2-enoic acid and MePro carried by domain A1, followed by successive condensations of nine amino acids to trigger the elongation of the linear peptide. A5 and A6 domains of lcsA are proposed to incorporate leucine, A2 AHyMeOA, and A3 incorporates HyLeu. A4, A7 and A8 incorporate AIB (Probable). The AHyMeOA in leucinostatin A activated by the A2 might be produced by the second PKS (lcsB or lcsC) present within the cluster (Probable). The MePro is probably produced via leucine cyclization and may originate from a separate pathway, independent of the cluster. Another nonproteinogenic amino acid, beta-Ala, could be produced by an aspartic acid decarboxylase also localized outside of the cluster. Two candidates are VFPBJ_01400 and VFPBJ_10476 (Probable). The final peptide scaffold may be released by the NAD(P)H-dependent thioester reductase (TE) at the C-terminal region of lcsA (Probable). Transamination of the lcsA product by the transaminase lcsP may produce DPD at the C-terminus (Probable). Further hydroxylation steps performed alternatively by the cytochrome P450 monooxygenases lcsI, lcsK and lcsN then yield the non-methylated leucinostatins precursor. It is also possible that leucines can be hydroxylated prior to their incorporation into the peptide (Probable). Varying extents of methylation then lead to the formation of leucinostatins A and B (Probable).

1 Publication1 Publication

<p>This subsection of the <a href="">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: Secondary metabolite biosynthesis

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


Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="">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 sitei137SubstrateBy similarity1
Binding sitei216ATPBy similarity1
Binding sitei235ATPBy similarity1
Binding sitei331ATPBy similarity1


Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="">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 bindingi107 – 115ATPBy similarity9

<p>The <a href="">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

<p>UniProtKB Keywords constitute a <a href="">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 functionLigase
LigandATP-binding, Nucleotide-binding

<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="">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:
Acyl-CoA ligase lcsD1 Publication (EC:6.2.1.-1 Publication)
Alternative name(s):
Leucinostatins biosynthesis cluster protein D1 Publication
<p>This subsection of the <a href="">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:lcsD1 Publication
ORF Names:VFPBJ_02533, VFPFJ_04705
<p>This subsection of the <a href="">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>OrganismiPurpureocillium lilacinum (Paecilomyces lilacinus)
<p>This subsection of the <a href="">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 identifieri33203 [NCBI]
<p>This subsection of the <a href="">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 lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesOphiocordycipitaceaePurpureocillium
<p>This subsection of the <a href="">Names and taxonomy</a> section is present for entries that are part of a <a href="">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
  • UP000078340 <p>A UniProt <a href="">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
  • UP000078240 Componenti: Unassembled WGS sequence

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Abolishes the production of leucinostatins A and B.1 Publication

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004466021 – 386Acyl-CoA ligase lcsDAdd BLAST386

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Expression is positively regulated by the leucinostatins biosynthesis cluster-specific transcription regulator lcsF.1 Publication

<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


Database of comparative protein structure models


<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


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>Regioni62 – 132SBD1By similarityAdd BLAST71
Regioni133 – 195SBD2By similarityAdd BLAST63
Regioni243 – 245Coenzyme A bindingBy similarity3
Regioni313 – 316Coenzyme A bindingBy similarity4
Regioni352 – 386DisorderedSequence analysisAdd BLAST35

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 biasi352 – 376Basic and acidic residuesSequence analysisAdd BLAST25

<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

Both substrate-binding domains (SBD1 and SBD2) are involved in the substrate recognition, and are sufficient to confer the substrate specificity.By similarity

<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

Database of Orthologous Groups


Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

Gene3Di, 1 hit

Integrated resource of protein families, domains and functional sites

View protein in InterPro
IPR025110, AMP-bd_C
IPR000873, AMP-dep_Synth/Lig
IPR042099, AMP-dep_Synthh-like_sf

Pfam protein domain database

View protein in Pfam
PF00501, AMP-binding, 1 hit
PF13193, AMP-binding_C, 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="">length</a> and <a href="">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="">Sequence</a> section indicates if the <a href="">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.

A0A179HJB8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
60 70 80 90 100
110 120 130 140 150
160 170 180 190 200
210 220 230 240 250
260 270 280 290 300
310 320 330 340 350
360 370 380
Mass (Da):42,272
Last modified:September 7, 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="">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i916BD897A6ACC2B2

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database


GenBank nucleotide sequence database


DNA Data Bank of Japan; a nucleotide sequence database

Links Updated
LSBH01000002 Genomic DNA Translation: OAQ83766.1
LSBI01000004 Genomic DNA Translation: OAQ90546.1

NCBI Reference Sequences

XP_018179265.1, XM_018321785.1

Genome annotation databases

Ensembl fungal genome annotation project

OAQ83766; OAQ83766; VFPBJ_02533
OAQ90546; OAQ90546; VFPFJ_04705

Database of genes from NCBI RefSeq genomes


KEGG: Kyoto Encyclopedia of Genes and Genomes


<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="">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:
Links Updated
LSBH01000002 Genomic DNA Translation: OAQ83766.1
LSBI01000004 Genomic DNA Translation: OAQ90546.1
RefSeqiXP_018179265.1, XM_018321785.1

3D structure databases


Genome annotation databases

EnsemblFungiiOAQ83766; OAQ83766; VFPBJ_02533
OAQ90546; OAQ90546; VFPFJ_04705

Phylogenomic databases


Family and domain databases

Gene3Di3.40.50.12780, 1 hit
InterProiView protein in InterPro
IPR025110, AMP-bd_C
IPR000873, AMP-dep_Synth/Lig
IPR042099, AMP-dep_Synthh-like_sf
PfamiView protein in Pfam
PF00501, AMP-binding, 1 hit
PF13193, AMP-binding_C, 1 hit

MobiDB: a database of protein disorder and mobility annotations


<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 nameiLCSD_PURLI
<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: A0A179HJB8
<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="">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 10, 2019
Last sequence update: September 7, 2016
Last modified: June 2, 2021
This is version 18 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


  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again