I1RF49 · NRPS4_GIBZE

Function

function

Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the fusahexin, a cyclic hydrophobic hexapeptide with the amino acid sequence cyclo-(D-Ala-L-Leu-D-allo-Thr-L-Pro-D-Leu-L-Leu) that plays an important role in cell surface hydrophobicity (PubMed:22862913, PubMed:34292732).
Fusahexin might also play a role in virulence, sensitivity to osmotic stress and oxidative stress (PubMed:34292732).
NRPS4 is the only enzyme within the cluster and its 5 catalytic modules are sufficient to produce fusahexin (PubMed:34292732).
The modules 1 to 4 incorporate respectively D-alanine, L-leucine, D-allo-threonine, and L-proline, which is supported by the presence of epimerase domains in modules 1 and 3, which incorporate D-amino acids (PubMed:34292732).
The terminal module is responsible for incorporation of the two adjacent leucine units, where the epimerase domain is only used to convert the first unit to D-leucine (PubMed:34292732).
The terminal condensation domain (Ct) is involved in cyclization with D-alanine and thereby releasing of fusahexin (PubMed:34292732).

Catalytic activity

Pathway

Secondary metabolite biosynthesis.

GO annotations

AspectTerm
Molecular Functionisomerase activity
Molecular Functionligase activity
Molecular Functionphosphopantetheine binding

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Nonribosomal peptide synthetase 4
  • EC number
  • Short names
    NRPS 4
  • Alternative names
    • Fusahexin biosynthesis cluster protein NPRS4

Gene names

    • Name
      NRPS4
    • ORF names
      FG02315, FGRAMPH1_01T05575

Organism names

Accessions

  • Primary accession
    I1RF49
  • Secondary accessions
    • A0A098D813

Proteomes

Organism-specific databases

Phenotypes & Variants

Disruption phenotype

Does not affect conidiation but results in reduction of cell surface hydrophobicity.

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00004556741-7639Nonribosomal peptide synthetase 4
Modified residue813O-(pantetheine 4'-phosphoryl)serine
Modified residue2350O-(pantetheine 4'-phosphoryl)serine
Modified residue3440O-(pantetheine 4'-phosphoryl)serine
Modified residue4981O-(pantetheine 4'-phosphoryl)serine
Modified residue6076O-(pantetheine 4'-phosphoryl)serine
Modified residue7125O-(pantetheine 4'-phosphoryl)serine

Keywords

Interaction

Protein-protein interaction databases

Structure

3D structure databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region244-636Adenylation 1
Domain776-852Carrier 1
Region865-1295Epimerization 1
Region1337-1767Condensation 1
Region1786-2181Adenylation 2
Domain2313-2389Carrier 2
Region2426-2852Condensation 2
Region2878-3269Adenylation 3
Domain3403-3479Carrier 3
Region3491-3928Epimerization 2
Region3961-4389Condensation 3
Region4407-4810Adenylation 4
Domain4944-5020Carrier 4
Region5058-5478Condensation 4
Region5498-5900Adenylation 5
Domain6039-6115Carrier 5
Region6133-6567Epimerization 3
Region6607-7032Condensation 5
Domain7088-7164Carrier 6
Region7254-7603Condensation 6

Domain

NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module. Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product. Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme. Occasionally, methyltransferase domains (responsible for amino acid methylation) are present within the NRP synthetase. NRPS4 has the following architecture: A-T-E-C-A-T-C-A-T-E-C-A-T-C-A-T-E-C-T-Ct.

Sequence similarities

Belongs to the NRP synthetase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    7,639
  • Mass (Da)
    843,997
  • Last updated
    2012-06-13 v1
  • Checksum
    F11CB81AFFCF07A1

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
HG970332
EMBL· GenBank· DDBJ
CEF74592.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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