I1RF62 · GIP1_GIBZE

Function

function

Multicopper oxidase; part of the gene cluster that mediates the biosynthesis of aurofusarin, a red mycelium pigment which is acting as a mycotoxin (PubMed:15809006, PubMed:15811992, PubMed:16879655).
The first step is performed by the polyketide synthase which condenses one acetyl-CoA and 6 malonyl-CoA units to form the first intermediate, the cyclic heptaketide and yellow pigment YWA1 (PubMed:21296881, PubMed:23557488).
The C2 hydroxyl group in the pyrone ring of YWA1 is probably formed during ring closure by an aldol-type cyclization reaction (PubMed:21296881).
The dehydratase aurZ then acts as the first tailoring enzyme in the aurofusarin biosynthetic pathway by converting YWA1 to nor-rubrofusarin (PubMed:21296881, PubMed:23557488).
Nor-rubrofusarin is then methylated to rubrofusarin by the O-methyltransferase aurJ (PubMed:21296881, PubMed:23557488).
Rubrofusarin is then transported across the plasma membrane by the rubrofusarin-specific pump aurT for further enzymatic processing by the extracellular complex composed of GIP1, aurF, aurO and aurS to yield aurofusarin (PubMed:21296881).

Pathway

Pigment biosynthesis.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site80Cu cation 1 (UniProtKB | ChEBI)
Binding site82Cu cation 2 (UniProtKB | ChEBI)
Binding site130Cu cation 2 (UniProtKB | ChEBI)
Binding site132Cu cation 3 (UniProtKB | ChEBI)
Binding site503Cu cation 4 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentextracellular region
Molecular Functioncopper ion binding
Molecular Functionoxidoreductase activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Multicopper oxidase GIP1
  • EC number
  • Alternative names
    • Aurofusarin biosynthesis cluster protein GIP1
    • Gibberella pigment protein 1
    • Laccase-1

Gene names

    • Name
      GIP1
    • Synonyms
      lac1
    • ORF names
      FG02328, FGRAMPH1_01T05601

Organism names

Accessions

  • Primary accession
    I1RF62
  • Secondary accessions
    • A0A098D823

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Impairs autofusarin biosynthesis and leads to a yellow pigmentation via accumulation of the intermediate rubrofusarin (PubMed:15811992, PubMed:16879655).

Miscellaneous

PTM/Processing

Features

Showing features for signal, chain, glycosylation.

TypeIDPosition(s)Description
Signal1-23
ChainPRO_501012415024-677Multicopper oxidase GIP1
Glycosylation76N-linked (GlcNAc...) asparagine
Glycosylation228N-linked (GlcNAc...) asparagine
Glycosylation283N-linked (GlcNAc...) asparagine
Glycosylation396N-linked (GlcNAc...) asparagine
Glycosylation478N-linked (GlcNAc...) asparagine
Glycosylation520N-linked (GlcNAc...) asparagine

Keywords

PTM databases

Expression

Induction

Expression is regulated by the aurofusarin biosynthesis cluster-specific transcription factor aurR1/GIP2 (PubMed:16461721, PubMed:16879655).

Interaction

Subunit

Might be part of an extracellular enzyme complex composed of GIP1, aurF, aurO and aurS (PubMed:21296881).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain31-150Plastocyanin-like 1
Domain179-379Plastocyanin-like 2
Domain469-588Plastocyanin-like 3
Region629-651Disordered

Sequence similarities

Belongs to the multicopper oxidase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    677
  • Mass (Da)
    75,310
  • Last updated
    2012-06-13 v1
  • Checksum
    6DC1B77634B307F2
MLTSPRLILLLLAWVFSALVASALVKKDWTITWEPGAPNGQERNMIKINNQFPGPTILCDEDDDIEVTVHNKMPFNTTVHWHGLERVNCVRMMGTPWSDGTPGMSQKPIEMGQSFIYRFKASPAGTHWYHSHSRATVLDGLYGPIFIRRKPDAPAPWHLISKEQADIDAMSRAVIDPKLVMVSDWTRFMSWEYMAAEESSGMAIFCSDSILVNGKGSLYCPDVDVLINHTSTYMKYGLYPRQVNDKGCFPFMRSTQGPYLTTGKPETIPLHLQHGCTPAEGTNETIEVDPADQWASLNFIGGATFKTIVFSVDEHDMWVYEVDGHYIVPQRVNTVHMYAGERYAVMIKLDKTPKDYTIRVADSGLTQVISAFATLRYKGGIQGSDSVGVIDYGGQNSTKDGSVITLDREHLPPYPPNPPARKADAMHVLSTHRWKSAWQYTMSGHGMYEEDRSAYGPLLYDPHSADAMDEGLVIRTKNGSWVDLVLQVGSLPGQPQEFPHMMHKHTGKTWQIGSGMGIWNYSSVEEAIAAEPHNFDLDTPKWRDTFVTSFDGSAWIVLRYQVTNPGPWLFHCHIETHLAGGMAIAILDGIDVWPQIPAEYGPDQRGFMPGTLPELESGGKQGTVDKQCPLLAVSPSGGPKKDSGETSASDSRWETLIRGLIQVLQGWLSDEASSRSS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
HG970332
EMBL· GenBank· DDBJ
CEF74605.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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