CLM1_GIBZE
ID CLM1_GIBZE Reviewed; 339 AA.
AC I1S104;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Longiborneol synthase CLM1 {ECO:0000303|PubMed:19880637};
DE EC=4.2.3.- {ECO:0000269|PubMed:19880637};
DE AltName: Full=Culmorin biosynthesis protein 1 {ECO:0000303|PubMed:19880637};
DE AltName: Full=Terpene cyclase CLM1 {ECO:0000303|PubMed:19880637};
GN Name=CLM1 {ECO:0000303|PubMed:19880637};
GN ORFNames=FG10397, FGRAMPH1_01T07999;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., 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=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., 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=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
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 Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [4]
RP FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=19880637; DOI=10.1128/aem.02017-09;
RA McCormick S.P., Alexander N.J., Harris L.J.;
RT "CLM1 of Fusarium graminearum encodes a longiborneol synthase required for
RT culmorin production.";
RL Appl. Environ. Microbiol. 76:136-141(2010).
RN [5]
RP 3D-STRUCTURE MODELING, DOMAIN, FUNCTION, AND BIOTECHNOLOGY.
RX PubMed=27324634; DOI=10.1007/s00894-016-3021-1;
RA Bresso E., Leroux V., Urban M., Hammond-Kosack K.E., Maigret B.,
RA Martins N.F.;
RT "Structure-based virtual screening of hypothetical inhibitors of the enzyme
RT longiborneol synthase-a potential target to reduce Fusarium head blight
RT disease.";
RL J. Mol. Model. 22:163-163(2016).
RN [6]
RP FUNCTION.
RX PubMed=26673640; DOI=10.1021/acs.jnatprod.5b00676;
RA Bahadoor A., Schneiderman D., Gemmill L., Bosnich W., Blackwell B.,
RA Melanson J.E., McRae G., Harris L.J.;
RT "Hydroxylation of Longiborneol by a Clm2-Encoded CYP450 Monooxygenase to
RT Produce Culmorin in Fusarium graminearum.";
RL J. Nat. Prod. 79:81-88(2016).
CC -!- FUNCTION: Terpene cyclase involved in the biosynthesis of culmorin, a
CC tricyclic sesquiterpene diol reported to have antifungal activity and
CC some phytotoxicity to wheat coleoptile tissue, contributing to Fusarium
CC head blight disease (PubMed:19880637) (Probable). The terpene cyclase
CC CLM1 is responsible for the cyclization of farnesyl diphosphate into
CC the intermediate longiborneol (PubMed:19880637). Longiborneol is then
CC hydroxylated in a regio- and endo-stereoselective manner at position C-
CC 11 by the cytochrome P450 monooxygenase CLM2 to produce culmorin
CC (PubMed:26673640). Additional non-specific oxygenases are also able to
CC hydroxylate longiborneol at other sites than C-11 leading to 3-
CC hydroxylongiborneol, 5-hydroxylongiborneol, 12-hydroxylongiborneol and
CC 15-hydroxylongiborneol (PubMed:26673640). Moreover, another oxygenase
CC capable of installing a C-11 exo-hydroxy group in longiborneol can also
CC yield 11-epi-acetylculmorin (PubMed:26673640). The production of these
CC longiborneol derivatives is dwarfed by the high abundance of culmorin,
CC suggesting that CLM2 displays superior enzymatic activity to the
CC unidentified, possibly promiscuous, additional oxygenases
CC (PubMed:26673640). {ECO:0000269|PubMed:19880637,
CC ECO:0000269|PubMed:26673640, ECO:0000305|PubMed:27324634}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P13513};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P13513};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:19880637}.
CC -!- INDUCTION: Expressed under trichothecene-inducing conditions.
CC {ECO:0000269|PubMed:19880637}.
CC -!- DISRUPTION PHENOTYPE: Leads to complete loss of culmorin production
CC (PubMed:19880637). Does not affect the trichothecene biosynthetic
CC pathway since 15-acetyldeoxynivalenol (15ADON) is still produced
CC (PubMed:19880637). Keeps the ability to convert exogenously added
CC longiborneol to culmorin (PubMed:19880637).
CC {ECO:0000269|PubMed:19880637}.
CC -!- BIOTECHNOLOGY: Longiborneol synthase CLM1 is a potential target to
CC reduce Fusarium head blight disease. 3D-structure modeling based on
CC known 3D-structure of losely related enzymes has been used for
CC screening of hypothetical inhibitors of CLM1 catalytic activity.
CC {ECO:0000269|PubMed:27324634}.
CC -!- SIMILARITY: Belongs to the trichodiene synthase family. {ECO:0000305}.
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DR EMBL; HG970332; CEF75803.1; -; Genomic_DNA.
DR RefSeq; XP_011319367.1; XM_011321065.1.
DR AlphaFoldDB; I1S104; -.
DR SMR; I1S104; -.
DR GeneID; 23557306; -.
DR KEGG; fgr:FGSG_10397; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G07999; -.
DR eggNOG; ENOG502SQ3X; Eukaryota.
DR HOGENOM; CLU_052212_0_2_1; -.
DR InParanoid; I1S104; -.
DR PHI-base; PHI:2394; -.
DR Proteomes; UP000070720; Chromosome 1.
DR GO; GO:0016838; F:carbon-oxygen lyase activity, acting on phosphates; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR024652; Trichodiene_synth.
DR Pfam; PF06330; TRI5; 1.
DR SFLD; SFLDG01021; Trichodiene_Synthase_Like; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding; Reference proteome; Virulence.
FT CHAIN 1..339
FT /note="Longiborneol synthase CLM1"
FT /id="PRO_0000444957"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 241..249
FT /note="NDXXSXXXE magnesium-binding motif"
FT /evidence="ECO:0000305|PubMed:27324634"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13513"
FT BINDING 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13513"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13513"
FT BINDING 249
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13513"
SQ SEQUENCE 339 AA; 38419 MW; 001EB840AFBE411B CRC64;
MLATPTLSNF DKPSLPSSEG GDPALAARLQ PLYSRFLTDL DLQPEYRRHE SEKLMEEVLK
FAKSTGVPHD LNSHSYQSLM VGYTYADNCL PYHDIEVKVY VAIYTWLATI CDDAEALGII
DDVQLFEQRF ILGEEQPTVL LRAFADQLKL TYKLYHPLVA NLILCSSLNL LTSTSLVARK
GIKEKGDHPS KGGNYFAWYI RERDGVGEAY SWFTFPKRQF PNLDIPIEAI EDMTRFIAYL
NDVLSFYKES LAGETHNYIN HTAAYEGVDS DAALHKTAQD TIDCARRIES VLAGKGEYEK
AWRLHASGYL QMHVQRGRYR LIEVGVGDAP DVHEVIKKI
