TPS8_MAIZE
ID TPS8_MAIZE Reviewed; 539 AA.
AC Q29VN3;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Alpha-copaene synthase {ECO:0000303|PubMed:21607717};
DE EC=4.2.3.133 {ECO:0000269|PubMed:21607717};
DE AltName: Full=(+)-germacrene D synthase {ECO:0000303|PubMed:21607717};
DE EC=4.2.3.77 {ECO:0000269|PubMed:21607717};
DE AltName: Full=Beta-caryophyllene synthase {ECO:0000303|PubMed:21607717};
DE EC=4.2.3.57 {ECO:0000269|PubMed:21607717};
DE AltName: Full=Delta-cadinene synthase {ECO:0000303|PubMed:21607717};
DE EC=4.2.3.- {ECO:0000269|PubMed:21607717};
DE AltName: Full=Terpene synthase 8 {ECO:0000303|Ref.1};
GN Name=TPS8 {ECO:0000303|Ref.1};
GN ORFNames=ZEAMMB73_Zm00001d029195 {ECO:0000312|EMBL:ONL98158.1};
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 [MRNA].
RC STRAIN=cv. B73;
RA Schnee C., Koellner T.G., Kubisch S., Gershenzon J., Degenhardt J.;
RT "The sesquiterpene synthase family of Zea mays.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73; TISSUE=Seedling;
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 [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=21607717; DOI=10.1007/s10886-011-9967-7;
RA Fontana A., Held M., Fantaye C.A., Turlings T.C., Degenhardt J.,
RA Gershenzon J.;
RT "Attractiveness of constitutive and herbivore-induced sesquiterpene blends
RT of maize to the parasitic wasp Cotesia marginiventris (Cresson).";
RL J. Chem. Ecol. 37:582-591(2011).
RN [4]
RP REVIEW.
RX PubMed=30187155; DOI=10.1007/s00425-018-2999-2;
RA Block A.K., Vaughan M.M., Schmelz E.A., Christensen S.A.;
RT "Biosynthesis and function of terpenoid defense compounds in maize (Zea
RT mays).";
RL Planta 249:21-30(2019).
CC -!- FUNCTION: Converts farnesyl diphosphate to the bicyclic olefins alpha-
CC copaene, (E)-beta-caryophyllene, and to the macrocyclic sesquiterpene
CC germacrene D (PubMed:21607717). Mediates also the biosynthesis of minor
CC sesquiterpene hydrocarbons including delta-cadinene (PubMed:21607717).
CC Involved in indirect defense by producing volatile signals attracting
CC natural enemies of herbivores (PubMed:21607717).
CC {ECO:0000269|PubMed:21607717}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = alpha-copaene + diphosphate;
CC Xref=Rhea:RHEA:33991, ChEBI:CHEBI:10221, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:175763; EC=4.2.3.133;
CC Evidence={ECO:0000269|PubMed:21607717};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33992;
CC Evidence={ECO:0000269|PubMed:21607717};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (+)-germacrene D + diphosphate;
CC Xref=Rhea:RHEA:30427, ChEBI:CHEBI:33019, ChEBI:CHEBI:49046,
CC ChEBI:CHEBI:175763; EC=4.2.3.77;
CC Evidence={ECO:0000269|PubMed:21607717};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30428;
CC Evidence={ECO:0000269|PubMed:21607717};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (-)-(E)-beta-caryophyllene +
CC diphosphate; Xref=Rhea:RHEA:28294, ChEBI:CHEBI:10357,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.57;
CC Evidence={ECO:0000269|PubMed:21607717};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28295;
CC Evidence={ECO:0000269|PubMed:21607717};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = delta-cadinene + diphosphate;
CC Xref=Rhea:RHEA:56556, ChEBI:CHEBI:33019, ChEBI:CHEBI:140564,
CC ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:21607717};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56557;
CC Evidence={ECO:0000269|PubMed:21607717};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q5GJ59};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q6JD73};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:21607717, ECO:0000305|PubMed:30187155}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q6JD73}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6Q3H2}.
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:0000250|UniProtKB:A0A1C9J6A7}.
CC -!- SIMILARITY: Belongs to the terpene synthase 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; AY928080; AAX99148.1; -; mRNA.
DR EMBL; CM007647; ONL98158.1; -; Genomic_DNA.
DR RefSeq; NP_001105912.1; NM_001112442.1.
DR AlphaFoldDB; Q29VN3; -.
DR SMR; Q29VN3; -.
DR STRING; 4577.GRMZM2G038153_P01; -.
DR PaxDb; Q29VN3; -.
DR PRIDE; Q29VN3; -.
DR GeneID; 732834; -.
DR KEGG; zma:732834; -.
DR eggNOG; ENOG502QUCN; Eukaryota.
DR HOGENOM; CLU_003125_7_0_1; -.
DR OrthoDB; 360509at2759; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000007305; Chromosome 1.
DR ExpressionAtlas; Q29VN3; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0080016; F:(-)-E-beta-caryophyllene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0102877; F:alpha-copaene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
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; IPR034741; Terpene_cyclase-like_1_C.
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 SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Lyase; Magnesium; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..539
FT /note="Alpha-copaene synthase"
FT /id="PRO_0000447516"
FT MOTIF 290..294
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 290
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 290
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 290
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 294
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 294
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 294
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 432
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
SQ SEQUENCE 539 AA; 62026 MW; 9F2F2FF494BF9482 CRC64;
MAPKTVWGYF FIDYIPEPLQ VSDKQRVVEL KGEVARLFED CNCKDVVERM NLVDVVQRLG
IDHHFKEQID TALKNIQGAE FNSSDLHEVS LRFRLLRQHG LWVPADQFDK FRRQEDGSFS
SDIADDPKGL LGLYNAASLL IHGEEVLEEA LLFARRHLES IRRGGGLHDS PYLSEQVGRS
LKIPLPRTLK RLEAVSYIPE YSSADDTTYI HPEILELARL DFNLLQHVHQ NELRTVTQWW
KGLCDVIGPD YGRDRIVECY FWAFSMYYEE EHARARMILA RLIMLASLLD DTFDDRATLQ
ECRELNKAIE RWDESDDISL LPECIQKFFL EVIRNFAEFE DELEAHEKYR VAYARKAYQL
LSKSYLQEVE WCHQGYTPSF DDHVSVSTAS AGIQVLCVGM LVGMGDAATK EVFEWMIGSN
NRVVRACAEV TRFMDDMADF KRGKNKTDVA TTVECYMKEQ NVTGEVAFDK IGSFVEDAWK
TLNQAALVGD RALLPVVQRV AGLAMSMMVF FHGKIDRYTD SEHLKETLED LFVNHVPLC
