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 07-NOV-2018, entry version 47. 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 PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084) OS (Wheat head blight fungus) (Fusarium graminearum). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae; OC Fusarium. OX NCBI_TaxID=229533; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084; RX PubMed=17823352; DOI=10.1126/science.1143708; RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., RA Di Pietro A., Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., RA Antoniw J., Baldwin T., Calvo S.E., Chang Y.-L., DeCaprio D., RA Gale L.R., Gnerre S., Goswami R.S., Hammond-Kosack K., Harris L.J., RA Hilburn K., Kennell J.C., Kroken S., Magnuson J.K., Mannhaupt G., RA Mauceli E.W., Mewes H.-W., Mitterbauer R., Muehlbauer G., RA Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T., Qi W., RA 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=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084; RX PubMed=20237561; DOI=10.1038/nature08850; RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., RA Daboussi M.-J., Di Pietro A., Dufresne M., Freitag M., Grabherr M., RA Henrissat B., Houterman P.M., Kang S., Shim W.-B., Woloshuk C., RA Xie X., Xu J.-R., Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., RA Brown D.W., Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., RA Danchin E.G.J., Diener A., Gale L.R., Gardiner D.M., Goff S., RA Hammond-Kosack K.E., Hilburn K., Hua-Van A., Jonkers W., Kazan K., RA Kodira C.D., Koehrsen M., Kumar L., Lee Y.-H., Li L., Manners J.M., RA Miranda-Saavedra D., Mukherjee M., Park G., Park J., Park S.-Y., RA Proctor R.H., Regev A., Ruiz-Roldan M.C., Sain D., Sakthikumar S., RA Sykes S., Schwartz D.C., Turgeon B.G., Wapinski I., Yoder O., RA Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A., Kistler H.C., RA 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=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084; 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 RT Fusarium 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 RT reveals a 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., RA Olsson S., 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 RT polyketide scaffold rubrofusarin in Saccharomyces cerevisiae."; RL Microb. Cell Fact. 12:31-31(2013). CC -!- FUNCTION: Multicopper oxidase; part of the gene cluster that CC mediates the biosynthesis of aurofusarin, a red mycelium pigment CC which is acting as a mycotoxin (PubMed:15811992, PubMed:15809006, CC PubMed:16879655). The first step is performed by the polyketide CC synthase which condenses one acetyl-CoA and 6 malonyl-CoA units to CC form the first intermediate, the cyclic heptaketide and yellow CC pigment YWA1 (PubMed:21296881, PubMed:23557488). The C2 hydroxyl CC group in the pyrone ring of YWA1 is probably formed during ring CC closure by an aldol-type cyclization reaction (PubMed:21296881). CC The dehydratase aurZ then acts as the first tailoring enzyme in CC the aurofusarin biosynthetic pathway by converting YWA1 to nor- CC rubrofusarin (PubMed:21296881, PubMed:23557488). Nor-rubrofusarin CC is then methylated to rubrofusarin by the O-methyltransferase aurJ CC (PubMed:21296881, PubMed:23557488). Rubrofusarin is then CC 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 CC yield 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 CC of GIP1, aurF, aurO and aurS (PubMed:21296881). CC {ECO:0000305|PubMed:21296881}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:21296881}. CC Secreted, 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 CC to a yellow pigmentation via accumulation of the intermediate CC rubrofusarin (PubMed:15811992, PubMed:16879655). CC {ECO:0000269|PubMed:15811992, ECO:0000269|PubMed:16879655}. CC -!- SIMILARITY: Belongs to the multicopper oxidase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; HG970332; CEF74605.1; -; Genomic_DNA. DR RefSeq; XP_011318237.1; XM_011319935.1. DR STRING; 229533.XP_382504.1; -. DR GeneID; 23549710; -. DR KEGG; fgr:FGSG_02328; -. DR EuPathDB; FungiDB:FGRAMPH1_01G05601; -. DR eggNOG; KOG1263; Eukaryota. DR eggNOG; COG2132; LUCA. DR InParanoid; I1RF62; -. DR OrthoDB; EOG092C0ZMK; -. DR BioCyc; MetaCyc:MONOMER-19450; -. 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; -; 2. DR InterPro; IPR001117; Cu-oxidase. DR InterPro; IPR011706; Cu-oxidase_2. DR InterPro; IPR011707; Cu-oxidase_3. DR InterPro; IPR033138; Cu_oxidase_CS. DR InterPro; IPR002355; Cu_oxidase_Cu_BS. DR InterPro; IPR008972; Cupredoxin. 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 Complete proteome; Copper; Glycoprotein; Metal-binding; KW Oxidoreductase; Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1 23 {ECO:0000255}. FT CHAIN 24 677 Multicopper oxidase GIP1. FT /FTId=PRO_5010124150. FT DOMAIN 31 150 Plastocyanin-like 1. {ECO:0000255}. FT DOMAIN 179 379 Plastocyanin-like 2. {ECO:0000255}. FT DOMAIN 469 588 Plastocyanin-like 3. {ECO:0000255}. FT METAL 80 80 Copper 1. {ECO:0000250|UniProtKB:Q70KY3}. FT METAL 82 82 Copper 2. {ECO:0000250|UniProtKB:Q70KY3}. FT METAL 130 130 Copper 2. {ECO:0000250|UniProtKB:Q70KY3}. FT METAL 132 132 Copper 3. {ECO:0000250|UniProtKB:Q70KY3}. FT METAL 503 503 Copper 4. {ECO:0000250|UniProtKB:Q70KY3}. FT CARBOHYD 76 76 N-linked (GlcNAc...) asparagine. FT {ECO:0000255|PROSITE-ProRule:PRU00498}. FT CARBOHYD 228 228 N-linked (GlcNAc...) asparagine. FT {ECO:0000255|PROSITE-ProRule:PRU00498}. FT CARBOHYD 283 283 N-linked (GlcNAc...) asparagine. FT {ECO:0000255|PROSITE-ProRule:PRU00498}. FT CARBOHYD 396 396 N-linked (GlcNAc...) asparagine. FT {ECO:0000255|PROSITE-ProRule:PRU00498}. FT CARBOHYD 478 478 N-linked (GlcNAc...) asparagine. FT {ECO:0000255|PROSITE-ProRule:PRU00498}. FT CARBOHYD 520 520 N-linked (GlcNAc...) asparagine. FT {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 //