CICE_EMENI
ID CICE_EMENI Reviewed; 520 AA.
AC A0A1U8QH20; C8V0D6; Q5AZ33;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=O-methyltransferase cicE {ECO:0000303|PubMed:24244835};
DE EC=2.1.1.- {ECO:0000255|PROSITE-ProRule:PRU01020};
DE AltName: Full=Cichorine biosynthesis cluster protein E {ECO:0000303|PubMed:24244835};
GN Name=cicE {ECO:0000303|PubMed:24244835}; ORFNames=AN6447, ANIA_06447;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP FUNCTION.
RX PubMed=22510154; DOI=10.1021/ja3016395;
RA Ahuja M., Chiang Y.M., Chang S.L., Praseuth M.B., Entwistle R.,
RA Sanchez J.F., Lo H.C., Yeh H.H., Oakley B.R., Wang C.C.;
RT "Illuminating the diversity of aromatic polyketide synthases in Aspergillus
RT nidulans.";
RL J. Am. Chem. Soc. 134:8212-8221(2012).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=24244835; DOI=10.1039/c2md20055d;
RA Sanchez J.F., Entwistle R., Corcoran D., Oakley B.R., Wang C.C.;
RT "Identification and molecular genetic analysis of the cichorine gene
RT cluster in Aspergillus nidulans.";
RL Med. Chem. Commun. 3:0-0(2012).
RN [5]
RP BIOTECHNOLOGY.
RX PubMed=30708999; DOI=10.3390/molecules24030515;
RA Liao L., Zhang X., Lou Y., Zhou C., Yuan Q., Gao J.;
RT "Discovery of three new phytotoxins from the fungus Aspergillus nidulans by
RT pathway inactivation.";
RL Molecules 24:0-0(2019).
CC -!- FUNCTION: O-methyltransferase; part of the gene cluster that mediates
CC the biosynthesis of cichorine, a phytotoxin active against knapweed,
CC corn, and soybeans (PubMed:24244835). The first step in the pathway is
CC performed by the non-reducing polyketide synthase pkbA that condenses
CC one acetyl-CoA starter unit with 3 malonyl-CoA units (PubMed:22510154).
CC PkbA also catalyzes one methylation step to produce 3-methylorsellinate
CC (PubMed:22510154). The nonribosomal peptide synthase-like protein cicB,
CC the cytochrome P450 monooxygenase cicH and the O-methyltransferase cicE
CC are involved in the conversion of 3-methylorsellinate into nidulol
CC (PubMed:24244835). CicB converts 3-methylorsellinate to a yet
CC unidentified intermediate, cicH may play a ring-closing role for
CC cichorine and cicE is plausibly responsible for the methylation of one
CC of the phenol groups (Probable). The oxidoreductase cicC acts
CC downstream with still unidentified enzymes to further convert nidulol
CC into cichorine (PubMed:24244835). {ECO:0000269|PubMed:22510154,
CC ECO:0000269|PubMed:24244835, ECO:0000305|PubMed:24244835}.
CC -!- PATHWAY: Phytotoxin biosynthesis. {ECO:0000269|PubMed:24244835}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of cichorine.
CC {ECO:0000269|PubMed:24244835}.
CC -!- BIOTECHNOLOGY: Cichorine and its derivatives are promising in the
CC course of developing novel herbicides. {ECO:0000269|PubMed:30708999}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; BN001301; CBF69453.1; -; Genomic_DNA.
DR EMBL; AACD01000108; EAA58469.1; -; Genomic_DNA.
DR RefSeq; XP_664051.1; XM_658959.1.
DR AlphaFoldDB; A0A1U8QH20; -.
DR SMR; A0A1U8QH20; -.
DR EnsemblFungi; CBF69453; CBF69453; ANIA_06447.
DR EnsemblFungi; EAA58469; EAA58469; AN6447.2.
DR GeneID; 2871346; -.
DR KEGG; ani:AN6447.2; -.
DR eggNOG; ENOG502S7DY; Eukaryota.
DR HOGENOM; CLU_005533_0_1_1; -.
DR OMA; AMMSIIN; -.
DR OrthoDB; 817726at2759; -.
DR Proteomes; UP000000560; Chromosome I.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0062032; P:cichorine biosynthetic process; IMP:GO_Central.
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 1: Evidence at protein level;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..520
FT /note="O-methyltransferase cicE"
FT /id="PRO_0000450886"
FT BINDING 300..301
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 323
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 355..356
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 371
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
SQ SEQUENCE 520 AA; 57889 MW; BF4ABF1977954004 CRC64;
MERFPRSAAD AQQLLQLAEL FKQSAEIIAE EWNKEDFSRI KAETNSIKSN LGSLDTARIL
PSPRLHEATR TVLAITGAAT ELVAEPYSRI QEVACQYFES RALFVAAERR IPDLLAGAGE
YGLSVGEIAE ATGIEERKLS RILRCLCSIH IFRQIGTDRF ANNRISAALK NNEPLRAYVQ
LFNLDIYTAS DQLPKYLLSS QGASYKVHET AWQKAVGTTK ARWDWLAERV SLDEVRPKEA
PYPGLPDVRH LQPGPDGKYA RPELDNFGLA MVGGGKVSGA AHAYDFPWAS LGDALVVDVG
GGVGGFVLQL LPAYPQLRYI VQDRAEVLQQ AQEEIWPVEA PEAVADGRVQ FMEHNFFQPN
PVKGADVYWL RGIFYCVQIL SALRTSMAPT SRILVCDQVM NTTAGCDEIP PAPSPLPANY
GYYMRYPHHR DLAMMSIING IERTPAQFTE LVKQAGLKVN KIWNCRSMVG IVEIGLKNEK
DRHHRRLSYM GFGNYTQLGI GFFSSAKGPV RDELQADEQA
