CICC_EMENI
ID CICC_EMENI Reviewed; 611 AA.
AC A0A1U8QYA8; C8V0D9; Q5AZ35;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=Oxidoreductase cicC {ECO:0000303|PubMed:24244835};
DE EC=1.1.-.- {ECO:0000305|PubMed:24244835};
DE AltName: Full=Cichorine biosynthesis cluster protein C {ECO:0000303|PubMed:24244835};
DE Flags: Precursor;
GN Name=cicC {ECO:0000303|PubMed:24244835}; ORFNames=AN6445, ANIA_06445;
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: Oxidoreductase; part of the gene cluster that mediates the
CC biosynthesis of cichorine, a phytotoxin active against knapweed, corn,
CC 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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:E4QP00};
CC -!- PATHWAY: Phytotoxin biosynthesis. {ECO:0000269|PubMed:24244835}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of cichorine and
CC accumulates nidulol. {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 GMC oxidoreductase family. {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; BN001301; CBF69458.1; -; Genomic_DNA.
DR EMBL; AACD01000108; EAA58467.1; -; Genomic_DNA.
DR RefSeq; XP_664049.1; XM_658957.1.
DR AlphaFoldDB; A0A1U8QYA8; -.
DR SMR; A0A1U8QYA8; -.
DR STRING; 162425.CADANIAP00006530; -.
DR CAZy; AA3; Auxiliary Activities 3.
DR EnsemblFungi; CBF69458; CBF69458; ANIA_06445.
DR EnsemblFungi; EAA58467; EAA58467; AN6445.2.
DR GeneID; 2871342; -.
DR KEGG; ani:AN6445.2; -.
DR VEuPathDB; FungiDB:AN6445; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_6_3_1; -.
DR OMA; GPESYAM; -.
DR OrthoDB; 798314at2759; -.
DR Proteomes; UP000000560; Chromosome I.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR GO; GO:0062032; P:cichorine biosynthetic process; IMP:GO_Central.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552; PTHR11552; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Reference proteome;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..611
FT /note="Oxidoreductase cicC"
FT /evidence="ECO:0000255"
FT /id="PRO_5010519013"
FT ACT_SITE 547
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT ACT_SITE 547
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT ACT_SITE 591
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 45..46
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 65..66
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 123
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 131..134
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 581
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 592..593
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 611 AA; 65973 MW; 8F12EF96D3266557 CRC64;
MALRYLNKFS LLSLAVPTLA APIGSSFGVP GTDALYDYVV VGAGNAGAPV AYRLAETGHT
VALVEAGSLY EYGNGNLSQI PANSLFFIGK DPEWTNNLVD WNFVTSPQAE WNNASVHYAS
GKVLGGSTGR NLMTYHLPTK GSLDRWAEDV SDESWNFDNM LPYIMKSQRF TPPNNNLRFR
NATPTYDPAV LGRRGRLDVT YPNYANGLAS WLVRGFRDIG LAAIRGLNGG QLIGSAYTLS
TIQPGNQHRA SSKTAYLDPL IGRNLNLIIY QSTHAKRILF SNDTVATGVR VSSEGQEYTL
SARNEVIVSA GAFKTPQLLM VSGIGPAANL ERYGIPLVAD RPGVGQNLQD HTLAGPSYRV
NAITGSSNSI PEFITEAQRQ YNSNPPRGVL TNTGVDILGW EKVPEQLRGN FSTETEDALA
SLPEDWPELE YLPVYGYFGD QNNYMVTPND GFNYLTIAAA VVSPLSRGTV DIASNDTEVN
PIIDPRWFAH PGDIQVAVAG FRRSRALMAS PAMAGITLGG ESYPGTDVQT DDEIVEWLRE
ASNTVHHACC TAGMGPRDNP DSVVDTQGRV IGVSGLRIVD ASIMPFLPPG HPISIIYGLA
ERIAESILAD A
