GIP1_GIBZE
ID GIP1_GIBZE Reviewed; 677 AA.
AC I1RF62; A0A098D823;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Multicopper oxidase GIP1 {ECO:0000303|PubMed:15811992};
DE EC=1.-.-.- {ECO:0000305};
DE AltName: Full=Aurofusarin biosynthesis cluster protein GIP1 {ECO:0000303|PubMed:16461721};
DE AltName: Full=Gibberella pigment protein 1 {ECO:0000303|PubMed:15811992};
DE AltName: Full=Laccase-1 {ECO:0000303|PubMed:15809006};
DE Flags: Precursor;
GN Name=GIP1 {ECO:0000303|PubMed:15811992};
GN Synonyms=lac1 {ECO:0000303|PubMed:15809006};
GN ORFNames=FG02328, FGRAMPH1_01T05601;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15811992; DOI=10.1128/aem.71.4.1701-1708.2005;
RA Kim J.E., Han K.H., Jin J., Kim H., Kim J.C., Yun S.H., Lee Y.W.;
RT "Putative polyketide synthase and laccase genes for biosynthesis of
RT aurofusarin in Gibberella zeae.";
RL Appl. Environ. Microbiol. 71:1701-1708(2005).
RN [5]
RP FUNCTION, AND PATHWAY.
RX PubMed=15809006; DOI=10.1016/j.fgb.2005.01.010;
RA Malz S., Grell M.N., Thrane C., Maier F.J., Rosager P., Felk A.,
RA Albertsen K.S., Salomon S., Bohn L., Schaefer W., Giese H.;
RT "Identification of a gene cluster responsible for the biosynthesis of
RT aurofusarin in the Fusarium graminearum species complex.";
RL Fungal Genet. Biol. 42:420-433(2005).
RN [6]
RP FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=16879655; DOI=10.1111/j.1365-2958.2006.05295.x;
RA Frandsen R.J., Nielsen N.J., Maolanon N., Soerensen J.C., Olsson S.,
RA Nielsen J., Giese H.;
RT "The biosynthetic pathway for aurofusarin in Fusarium graminearum reveals a
RT close link between the naphthoquinones and naphthopyrones.";
RL Mol. Microbiol. 61:1069-1080(2006).
RN [7]
RP INDUCTION.
RX PubMed=16461721; DOI=10.1128/aem.72.2.1645-1652.2006;
RA Kim J.E., Jin J., Kim H., Kim J.C., Yun S.H., Lee Y.W.;
RT "GIP2, a putative transcription factor that regulates the aurofusarin
RT biosynthetic gene cluster in Gibberella zeae.";
RL Appl. Environ. Microbiol. 72:1645-1652(2006).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND PATHWAY.
RX PubMed=21296881; DOI=10.1074/jbc.m110.179853;
RA Frandsen R.J., Schuett C., Lund B.W., Staerk D., Nielsen J., Olsson S.,
RA Giese H.;
RT "Two novel classes of enzymes are required for the biosynthesis of
RT aurofusarin in Fusarium graminearum.";
RL J. Biol. Chem. 286:10419-10428(2011).
RN [9]
RP FUNCTION.
RX PubMed=23557488; DOI=10.1186/1475-2859-12-31;
RA Rugbjerg P., Naesby M., Mortensen U.H., Frandsen R.J.;
RT "Reconstruction of the biosynthetic pathway for the core fungal polyketide
RT scaffold rubrofusarin in Saccharomyces cerevisiae.";
RL Microb. Cell Fact. 12:31-31(2013).
CC -!- FUNCTION: Multicopper oxidase; part of the gene cluster that mediates
CC the biosynthesis of aurofusarin, a red mycelium pigment which is acting
CC as a mycotoxin (PubMed:15811992, PubMed:15809006, PubMed:16879655). The
CC first step is performed by the polyketide synthase which condenses one
CC acetyl-CoA and 6 malonyl-CoA units to form the first intermediate, the
CC cyclic heptaketide and yellow pigment YWA1 (PubMed:21296881,
CC PubMed:23557488). The C2 hydroxyl group in the pyrone ring of YWA1 is
CC probably formed during ring closure by an aldol-type cyclization
CC reaction (PubMed:21296881). The dehydratase aurZ then acts as the first
CC tailoring enzyme in the aurofusarin biosynthetic pathway by converting
CC YWA1 to nor-rubrofusarin (PubMed:21296881, PubMed:23557488). Nor-
CC rubrofusarin is then methylated to rubrofusarin by the O-
CC methyltransferase aurJ (PubMed:21296881, PubMed:23557488). Rubrofusarin
CC is then transported across the plasma membrane by the rubrofusarin-
CC specific pump aurT for further enzymatic processing by the
CC extracellular complex composed of GIP1, aurF, aurO and aurS to yield
CC aurofusarin (PubMed:21296881). {ECO:0000269|PubMed:15809006,
CC ECO:0000269|PubMed:15811992, ECO:0000269|PubMed:16879655,
CC ECO:0000269|PubMed:21296881, ECO:0000269|PubMed:23557488}.
CC -!- PATHWAY: Pigment biosynthesis. {ECO:0000269|PubMed:15809006,
CC ECO:0000269|PubMed:16879655, ECO:0000269|PubMed:21296881}.
CC -!- SUBUNIT: Might be part of an extracellular enzyme complex composed of
CC GIP1, aurF, aurO and aurS (PubMed:21296881).
CC {ECO:0000305|PubMed:21296881}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:21296881}. Secreted,
CC extracellular space {ECO:0000305|PubMed:21296881}.
CC -!- INDUCTION: Expression is regulated by the aurofusarin biosynthesis
CC cluster-specific transcription factor aurR1/GIP2 (PubMed:16879655,
CC PubMed:16461721). {ECO:0000269|PubMed:16461721,
CC ECO:0000269|PubMed:16879655}.
CC -!- DISRUPTION PHENOTYPE: Impairs autofusarin biosynthesis and leads to a
CC yellow pigmentation via accumulation of the intermediate rubrofusarin
CC (PubMed:15811992, PubMed:16879655). {ECO:0000269|PubMed:15811992,
CC ECO:0000269|PubMed:16879655}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; HG970332; CEF74605.1; -; Genomic_DNA.
DR RefSeq; XP_011318237.1; XM_011319935.1.
DR AlphaFoldDB; I1RF62; -.
DR SMR; I1RF62; -.
DR STRING; 5518.FGSG_02328P0; -.
DR GeneID; 23549710; -.
DR KEGG; fgr:FGSG_02328; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G05601; -.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_006504_5_0_1; -.
DR InParanoid; I1RF62; -.
DR BioCyc; MetaCyc:MON-19450; -.
DR PHI-base; PHI:3991; -.
DR PHI-base; PHI:712; -.
DR Proteomes; UP000070720; Chromosome 1.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.420; -; 3.
DR InterPro; IPR001117; Cu-oxidase.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR PANTHER; PTHR11709; PTHR11709; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; SSF49503; 3.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 1: Evidence at protein level;
KW Copper; Glycoprotein; Metal-binding; Oxidoreductase; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..677
FT /note="Multicopper oxidase GIP1"
FT /id="PRO_5010124150"
FT DOMAIN 31..150
FT /note="Plastocyanin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 179..379
FT /note="Plastocyanin-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 469..588
FT /note="Plastocyanin-like 3"
FT /evidence="ECO:0000255"
FT REGION 629..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 80
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 82
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 130
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 132
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 503
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 677 AA; 75310 MW; 6DC1B77634B307F2 CRC64;
MLTSPRLILL LLAWVFSALV ASALVKKDWT ITWEPGAPNG QERNMIKINN QFPGPTILCD
EDDDIEVTVH NKMPFNTTVH WHGLERVNCV RMMGTPWSDG TPGMSQKPIE MGQSFIYRFK
ASPAGTHWYH SHSRATVLDG LYGPIFIRRK PDAPAPWHLI SKEQADIDAM SRAVIDPKLV
MVSDWTRFMS WEYMAAEESS GMAIFCSDSI LVNGKGSLYC PDVDVLINHT STYMKYGLYP
RQVNDKGCFP FMRSTQGPYL TTGKPETIPL HLQHGCTPAE GTNETIEVDP ADQWASLNFI
GGATFKTIVF SVDEHDMWVY EVDGHYIVPQ RVNTVHMYAG ERYAVMIKLD KTPKDYTIRV
ADSGLTQVIS AFATLRYKGG IQGSDSVGVI DYGGQNSTKD GSVITLDREH LPPYPPNPPA
RKADAMHVLS THRWKSAWQY TMSGHGMYEE DRSAYGPLLY DPHSADAMDE GLVIRTKNGS
WVDLVLQVGS LPGQPQEFPH MMHKHTGKTW QIGSGMGIWN YSSVEEAIAA EPHNFDLDTP
KWRDTFVTSF DGSAWIVLRY QVTNPGPWLF HCHIETHLAG GMAIAILDGI DVWPQIPAEY
GPDQRGFMPG TLPELESGGK QGTVDKQCPL LAVSPSGGPK KDSGETSASD SRWETLIRGL
IQVLQGWLSD EASSRSS
