I1RF62 · GIP1_GIBZE
- ProteinMulticopper oxidase GIP1
- GeneGIP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids677 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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).
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 80 | Cu cation 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 82 | Cu cation 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 130 | Cu cation 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 132 | Cu cation 3 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 503 | Cu cation 4 (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | copper ion binding | |
Molecular Function | oxidoreductase activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMulticopper oxidase GIP1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Nectriaceae > Fusarium
Accessions
- Primary accessionI1RF62
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-23 | |||||
Sequence: MLTSPRLILLLLAWVFSALVASA | ||||||
Chain | PRO_5010124150 | 24-677 | Multicopper oxidase GIP1 | |||
Sequence: LVKKDWTITWEPGAPNGQERNMIKINNQFPGPTILCDEDDDIEVTVHNKMPFNTTVHWHGLERVNCVRMMGTPWSDGTPGMSQKPIEMGQSFIYRFKASPAGTHWYHSHSRATVLDGLYGPIFIRRKPDAPAPWHLISKEQADIDAMSRAVIDPKLVMVSDWTRFMSWEYMAAEESSGMAIFCSDSILVNGKGSLYCPDVDVLINHTSTYMKYGLYPRQVNDKGCFPFMRSTQGPYLTTGKPETIPLHLQHGCTPAEGTNETIEVDPADQWASLNFIGGATFKTIVFSVDEHDMWVYEVDGHYIVPQRVNTVHMYAGERYAVMIKLDKTPKDYTIRVADSGLTQVISAFATLRYKGGIQGSDSVGVIDYGGQNSTKDGSVITLDREHLPPYPPNPPARKADAMHVLSTHRWKSAWQYTMSGHGMYEEDRSAYGPLLYDPHSADAMDEGLVIRTKNGSWVDLVLQVGSLPGQPQEFPHMMHKHTGKTWQIGSGMGIWNYSSVEEAIAAEPHNFDLDTPKWRDTFVTSFDGSAWIVLRYQVTNPGPWLFHCHIETHLAGGMAIAILDGIDVWPQIPAEYGPDQRGFMPGTLPELESGGKQGTVDKQCPLLAVSPSGGPKKDSGETSASDSRWETLIRGLIQVLQGWLSDEASSRSS | ||||||
Glycosylation | 76 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 228 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 283 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 396 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 478 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 520 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
PTM databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 31-150 | Plastocyanin-like 1 | ||||
Sequence: ITWEPGAPNGQERNMIKINNQFPGPTILCDEDDDIEVTVHNKMPFNTTVHWHGLERVNCVRMMGTPWSDGTPGMSQKPIEMGQSFIYRFKASPAGTHWYHSHSRATVLDGLYGPIFIRRK | ||||||
Domain | 179-379 | Plastocyanin-like 2 | ||||
Sequence: LVMVSDWTRFMSWEYMAAEESSGMAIFCSDSILVNGKGSLYCPDVDVLINHTSTYMKYGLYPRQVNDKGCFPFMRSTQGPYLTTGKPETIPLHLQHGCTPAEGTNETIEVDPADQWASLNFIGGATFKTIVFSVDEHDMWVYEVDGHYIVPQRVNTVHMYAGERYAVMIKLDKTPKDYTIRVADSGLTQVISAFATLRYKG | ||||||
Domain | 469-588 | Plastocyanin-like 3 | ||||
Sequence: DEGLVIRTKNGSWVDLVLQVGSLPGQPQEFPHMMHKHTGKTWQIGSGMGIWNYSSVEEAIAAEPHNFDLDTPKWRDTFVTSFDGSAWIVLRYQVTNPGPWLFHCHIETHLAGGMAIAILD | ||||||
Region | 629-651 | Disordered | ||||
Sequence: PLLAVSPSGGPKKDSGETSASDS |
Sequence similarities
Belongs to the multicopper oxidase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length677
- Mass (Da)75,310
- Last updated2012-06-13 v1
- Checksum6DC1B77634B307F2
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
HG970332 EMBL· GenBank· DDBJ | CEF74605.1 EMBL· GenBank· DDBJ | Genomic DNA |