BIK3_GIBF5
ID BIK3_GIBF5 Reviewed; 453 AA.
AC S0E608;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=O-methyltransferase bik3 {ECO:0000305};
DE EC=2.1.1.- {ECO:0000269|PubMed:26382642};
DE AltName: Full=Bikaverin biosynthesis protein 3 {ECO:0000303|PubMed:19400779};
GN Name=bik3 {ECO:0000303|PubMed:19400779}; ORFNames=FFUJ_06744;
OS Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS and foot rot disease fungus) (Fusarium fujikuroi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=1279085;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831;
RX PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA Wiemann P., Sieber C.M.K., von Bargen K.W., Studt L., Niehaus E.-M.,
RA Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA Proctor R.H., Muensterkoetter M., Freitag M., Humpf H.-U., Gueldener U.,
RA Tudzynski B.;
RT "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT novel metabolites.";
RL PLoS Pathog. 9:E1003475-E1003475(2013).
RN [2]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19400779; DOI=10.1111/j.1365-2958.2009.06695.x;
RA Wiemann P., Willmann A., Straeten M., Kleigrewe K., Beyer M., Humpf H.U.,
RA Tudzynski B.;
RT "Biosynthesis of the red pigment bikaverin in Fusarium fujikuroi: genes,
RT their function and regulation.";
RL Mol. Microbiol. 72:931-946(2009).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26382642; DOI=10.1016/j.fgb.2015.09.006;
RA Arndt B., Studt L., Wiemann P., Osmanov H., Kleigrewe K., Koehler J.,
RA Krug I., Tudzynski B., Humpf H.U.;
RT "Genetic engineering, high resolution mass spectrometry and nuclear
RT magnetic resonance spectroscopy elucidate the bikaverin biosynthetic
RT pathway in Fusarium fujikuroi.";
RL Fungal Genet. Biol. 84:26-36(2015).
CC -!- FUNCTION: O-methyltransferase; part of the gene cluster that mediates
CC the biosynthesis of bikaverin, a red pigment also considered as a
CC mycotoxin (PubMed:19400779). The first stage is catalyzed by the
CC polyketide synthase bik1, which catalyzes the formation of the
CC intermediate SMA76a also knowm as pre-bikaverin (PubMed:19400779). FAD-
CC dependent monooxygenase bik2 might then be responsible for the
CC oxidation of pre-bikaverin to oxo-pre-bikaverin which is in turn
CC methylated by the O-methyltransferase bik3 to me-oxo-pre-bikaverin
CC (PubMed:26382642). A further cycle of oxydation and methylation by bik2
CC and bik3 leads to the final product of bikaverin, via a nor-bikaverin
CC intermediate (PubMed:19400779, PubMed:26382642).
CC {ECO:0000269|PubMed:19400779, ECO:0000269|PubMed:26382642}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:19400779, ECO:0000269|PubMed:26382642}.
CC -!- INDUCTION: Expression is repressed by glutamine and at alkaline ambient
CC pH and highly induced under nitrogen starvation and acidic pH
CC conditions (PubMed:19400779). {ECO:0000269|PubMed:19400779}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of bikaverin
CC (PubMed:19400779). Leads to the accumulation of the intermediate oxo-
CC pre-bikaverin (PubMed:26382642). {ECO:0000269|PubMed:19400779,
CC ECO:0000269|PubMed:26382642}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family. COMT
CC subfamily. {ECO:0000305}.
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DR EMBL; HF679027; CCT67993.1; -; Genomic_DNA.
DR AlphaFoldDB; S0E608; -.
DR SMR; S0E608; -.
DR EnsemblFungi; CCT67993; CCT67993; FFUJ_06744.
DR VEuPathDB; FungiDB:FFUJ_06744; -.
DR HOGENOM; CLU_005533_1_4_1; -.
DR Proteomes; UP000016800; Chromosome 5.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR016461; COMT-like.
DR InterPro; IPR001077; O_MeTrfase_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00891; Methyltransf_2; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51683; SAM_OMT_II; 1.
PE 2: Evidence at transcript level;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..453
FT /note="O-methyltransferase bik3"
FT /id="PRO_0000436340"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 355
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 305
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 453 AA; 50033 MW; 8F5B239B69B9A578 CRC64;
MVSNGISNGT NGTNGTTTNG TNGVNGHAAL SPLEVLVQDL NKNTTTLNGY LRANKLPEPS
FERDAPIINL SPDAPEEAQV AKEKVLDSAL QIFQLVSGPG EYLQNVITGY HYMEILRWMS
HFKIFELVPL EGKISYTELA SKAGVAELRL KTLARMGMTN HLFAEPEPGF IAHSATSAAL
VTNNRFSDQR VWMTSIIAPV IASMVTAHER WPDSTAPNKA AFNAAFNTDL RMYEYISKQP
DVYKLFGRVM DAIATSPKSD LKHLVSGFDW AGLGKANVVD IGGNIGHSCV KLAEAFPDLN
FIIQDIPHVV EEGAKVIKEN NEASIANRIQ FQEYDFFQKQ PVVGADIYLL RQIFHNWDFE
NSVKILKNTV ESMGQNSHVL IMDFVVPEPG TVSSVNERVL RSRDVGMMQL FNSLERDLEG
WKAILEAVDS RLKINAVNTP YGSFMSVIDV VLG
