KSL4_MAIZE
ID KSL4_MAIZE Reviewed; 848 AA.
AC A0A1D6KUI6; C0PHK0;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2016, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Dolabradiene synthase KSL4, chloroplastic {ECO:0000305};
DE EC=4.2.3.196 {ECO:0000269|PubMed:29475898};
DE AltName: Full=Ent-kaurene synthase-like 4 {ECO:0000303|PubMed:29475898};
DE Short=ZmKSL4 {ECO:0000303|PubMed:29475898};
DE Flags: Precursor;
GN Name=KSL4 {ECO:0000303|PubMed:29475898};
GN ORFNames=ZEAMMB73_Zm00001d032858 {ECO:0000312|EMBL:ONM06227.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=19965430; DOI=10.1126/science.1178534;
RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT "The B73 maize genome: complexity, diversity, and dynamics.";
RL Science 326:1112-1115(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. B73;
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=29475898; DOI=10.1104/pp.17.01351;
RA Mafu S., Ding Y., Murphy K.M., Yaacoobi O., Addison J.B., Wang Q., Shen Z.,
RA Briggs S.P., Bohlmann J., Castro-Falcon G., Hughes C.C., Betsiashvili M.,
RA Huffaker A., Schmelz E.A., Zerbe P.;
RT "Discovery, biosynthesis and stress-related accumulation of dolabradiene-
RT derived defenses in maize.";
RL Plant Physiol. 176:2677-2690(2018).
CC -!- FUNCTION: Involved in the production of antifungal dolabralexin
CC phytoalexins in response to biotic and abiotic stresses
CC (PubMed:29475898). In response to fungal infection and in associtation
CC with AN2, is involved in the production dolabradiene, a type of
CC antifungal phytoalexin (PubMed:29475898). Converts ent-copalyl
CC disphosphate (ent-CPP) to dolabradiene (PubMed:29475898).
CC {ECO:0000269|PubMed:29475898}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ent-copalyl diphosphate = diphosphate + dolabradiene;
CC Xref=Rhea:RHEA:58160, ChEBI:CHEBI:33019, ChEBI:CHEBI:58553,
CC ChEBI:CHEBI:141822; EC=4.2.3.196;
CC Evidence={ECO:0000269|PubMed:29475898};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58161;
CC Evidence={ECO:0000269|PubMed:29475898};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q40577};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q40577};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for
CC the catalytic activity, presumably through binding to Mg(2+).
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; CM007647; ONM06227.1; -; Genomic_DNA.
DR EMBL; BT067769; ACN34666.1; -; mRNA.
DR RefSeq; NP_001169726.1; NM_001176255.1.
DR AlphaFoldDB; A0A1D6KUI6; -.
DR SMR; A0A1D6KUI6; -.
DR STRING; 4577.GRMZM2G016922_P01; -.
DR EnsemblPlants; Zm00001eb047160_T001; Zm00001eb047160_P001; Zm00001eb047160.
DR GeneID; 100383607; -.
DR Gramene; Zm00001eb047160_T001; Zm00001eb047160_P001; Zm00001eb047160.
DR KEGG; zma:100383607; -.
DR eggNOG; ENOG502QVGX; Eukaryota.
DR OMA; RSKEYIH; -.
DR OrthoDB; 318477at2759; -.
DR BioCyc; MetaCyc:MON-20516; -.
DR Proteomes; UP000007305; Chromosome 1.
DR ExpressionAtlas; A0A1D6KUI6; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0010333; F:terpene synthase activity; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0051502; P:diterpene phytoalexin biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IBA:GO_Central.
DR CDD; cd00684; Terpene_cyclase_plant_C1; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR Gene3D; 1.50.10.130; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR044814; Terpene_cyclase_plant_C1.
DR InterPro; IPR001906; Terpene_synth_N.
DR InterPro; IPR036965; Terpene_synth_N_sf.
DR InterPro; IPR005630; Terpene_synthase_metal-bd.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR Pfam; PF01397; Terpene_synth; 1.
DR Pfam; PF03936; Terpene_synth_C; 1.
DR SUPFAM; SSF48239; SSF48239; 2.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Lyase; Magnesium; Metal-binding; Plant defense; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..64
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 65..848
FT /note="Dolabradiene synthase KSL4, chloroplastic"
FT /id="PRO_0000447768"
FT REGION 148..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 597..601
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 597
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 597
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 601
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 601
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 742
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 746
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 750
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT CONFLICT 751
FT /note="A -> G (in Ref. 2; ACN34666)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 848 AA; 95121 MW; 8FC5A8B3DEE934CC CRC64;
MASLSFASSH ASLFCCQQSS SAIILRPAGA LLRLSRRQPS SHTISTTDQL FPRRSRMPRN
VDTHAAAERN SPSTMSSLEA VDELETNGDS AVVVVREQQQ QQHLLMGATD DGLPPSPYDT
AWVAMVPAPG NPLVPRFPQC VDWILQNQRS DGSWGPDGGS GDHPSSPLGK DALMSTLACV
LALKTWDAGE EHVRKGLSFV GNNSPSCVMT GDERDAPVGF SVIFPGMLAR AIDMGLDIPM
MTQANVDAFI RLRDTELNRM AATTGSKAFM SYVAEGLGDV LDWDEAAMVY QRQNGSFFNS
PATTAAAAIH GNNDRALRYL DSLVNMFGSS VPTVYPRSTY SRLHMVDTLQ KMGLSRSFVS
EINEMLDMTY RSWLANDDEE MMLDMSTCAM AFRLLRMHGY DVSSDGLAQF SSESSFRDSV
HGQANDTEAL LELYKASQIQ ITEDELVLVD IRSWSAKLLK EQLGSDKVSR SVDAQEVQQV
LKFPFYTTLD RLEHRRHIEQ FKAGGFHMLK SAYRFCKEDE ELVSLAVQGF HSSQALYQQE
LQFLTRWAKE ARLHDLEFAR IMPMNTFFPN AALMYAPELS EARILCTKNC MLATAVDDLF
DVGGSREEME NLVRLIDMWD EHEEVGFCSE RVEILFRAIY DTSKELAAKA MAVQNRSVIN
HVAELWADLV RAMMTEAEWS MRGHVPSSME EYMQVAETSF ALGPIVLMPL YLIGPELPEA
VVRCPEYKQL FHHMNVCGRL LNDLQSYERE AKQGKINSVL LVAPRHGGSI EAAKSEVRRA
IEASRRELLR MLVAEADATV PRPFRQEFWN MCKMVHLFYM EDDCYSSPKE LVHAANMVVF
DPLRVREL
