FSR2_GIBF5
ID FSR2_GIBF5 Reviewed; 387 AA.
AC S0DQQ0; G8C420;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=O-methyltransferase fsr2 {ECO:0000303|PubMed:22492438};
DE EC=2.1.1.- {ECO:0000255|PROSITE-ProRule:PRU01020};
DE AltName: Full=Fusarubin biosynthesis cluster protein 2 {ECO:0000303|PubMed:22492438};
GN Name=FSR2 {ECO:0000303|PubMed:22492438}; ORFNames=FFUJ_03985;
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 [GENOMIC DNA], FUNCTION, INDUCTION, DISRUPTION
RP PHENOTYPE, AND PATHWAY.
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831;
RX PubMed=22492438; DOI=10.1128/aem.00823-12;
RA Studt L., Wiemann P., Kleigrewe K., Humpf H.U., Tudzynski B.;
RT "Biosynthesis of fusarubins accounts for pigmentation of Fusarium fujikuroi
RT perithecia.";
RL Appl. Environ. Microbiol. 78:4468-4480(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND FUNCTION.
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).
CC -!- FUNCTION: O-methyltransferase; part of the gene cluster that mediates
CC the biosynthesis of fusarubins, highly pigmented naphthoquinones
CC responsible for the coloration of the fruiting bodies (PubMed:22492438,
CC PubMed:23825955). The non-reducing polyketide synthase FSR1 is
CC responsible for the condensation of seven acetyl-CoA units to yield a
CC haptaketide (PubMed:22492438). After rings A and B are formed by aldol-
CC type cyclization, the PKS-derived product is released as 6-O-
CC demethylfusarubinaldehyde (PubMed:22492438). Then, two hydroxyl groups
CC at C-5 and C-10 are incorporated by FSR3, and simultaneously hydroxyl
CC groups at C-6 and C-8 are methylated by FSR2 (PubMed:22492438). The
CC aldehyde is, on the one hand, reduced by FSR3 to 8-O-methylfusarubin
CC alcohol, which equilibrates mainly with 8-O-methylfusarubin and only
CC small amounts of 8-O-methylnectriafurone (PubMed:22492438). On the
CC other hand, the aldehyde can be oxidized to form 8-O-methylfusarubinic
CC acid, a reaction driven by FSR3 equilibrating with 8-O-
CC methylfusarubinlactone, finally resulting in 8-O-
CC methylanhydrofusarubinlactol after a further reduction step and loss of
CC water (PubMed:22492438). 8-O-Methylfusarubinic acid can also undergo
CC decarboxylation, resulting in 8-O-methyl-13-hydroxynorjavanicin after
CC another hydroxylation step at C-13 (PubMed:22492438). Both steps are
CC most likely also accomplished by FSR3 (PubMed:22492438). No enzymatic
CC function has been determined so far for either FSR4 and FSR5
CC (PubMed:22492438). Their deletion does not alter the product spectrum,
CC but the possibility that they catalyze specific enzymatic steps during
CC perithecium development cannot be ruled out (PubMed:22492438). FSR4
CC might possess a regulatory function in the biosynthesis of fusarubins
CC (PubMed:22492438). {ECO:0000269|PubMed:22492438,
CC ECO:0000269|PubMed:23825955}.
CC -!- PATHWAY: Polyketide biosynthesis. {ECO:0000269|PubMed:22492438}.
CC -!- INDUCTION: Expression is repressed under acidic conditions, while the
CC expression is induced under alkaline conditions (PubMed:22492438).
CC Expression is induced in presence of sodium nitrate, and repressed by
CC glutamine (PubMed:22492438). {ECO:0000269|PubMed:22492438}.
CC -!- DISRUPTION PHENOTYPE: Leads to an alteration in the product spectrum,
CC with an accumulation of 6-O-demethyl-10-deoxyfusarubin and 6-O-
CC demethylfusarubinaldehyde (PubMed:22492438).
CC {ECO:0000269|PubMed:22492438}.
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; HE613440; CCE67071.1; -; Genomic_DNA.
DR EMBL; HF679024; CCT64761.1; -; Genomic_DNA.
DR AlphaFoldDB; S0DQQ0; -.
DR SMR; S0DQQ0; -.
DR EnsemblFungi; CCT64761; CCT64761; FFUJ_03985.
DR EnsemblFungi; KLP16366; KLP16366; LW94_5849.
DR VEuPathDB; FungiDB:FFUJ_03985; -.
DR Proteomes; UP000016800; Chromosome 2.
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..387
FT /note="O-methyltransferase fsr2"
FT /id="PRO_0000442025"
FT ACT_SITE 280
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 231
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 387 AA; 43020 MW; BAA38EA9FACB0C34 CRC64;
MDKADRDAVI EHATQVKRLV HDPHSFLTEL VAQQQQYHCI AWLCHFNILS NIPQPPESIA
YSDVATKAQV PLSKLQSVAR MAMTTGLLSE TKDGKLSHNT LSAQFITNVH MKTQLLHIVN
QTVPLMTGLI QATWKWGETS ATNETAYNII HGTELSFFEH LKTRPDLNEG FQAYMKSRAV
SHTGSNVEHL LNAFDWKALG QAQVVDIGGS SGSTSIMLAT AFPLLNLVIE DLPEPIENAK
ARLSELPSDI KSRIEIMAYD FFTPQPVKNA DVYLLRTILH DWPDADAIKI IQGIVAAMGP
SSRLLIMDMV LPKPGSGSVT FEAALRQKDL TMIQCFNAQE REVEEWKALL TKADPRLKIQ
AIERPAGSEL SVIEAMLDES PEQAAWF
