TPS2_SORBI
ID TPS2_SORBI Reviewed; 545 AA.
AC C5YHI2;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 2.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Beta-sesquiphellandrene synthase;
DE Short=SbTPS2;
DE EC=4.2.3.123;
GN Name=TPS2; OrderedLocusNames=Sb07g004485;
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF TYR-373 AND VAL-405, FUNCTION,
RP CATALYTIC ACTIVITY, AND INDUCTION BY HERBIVORY.
RX PubMed=21880075; DOI=10.1111/j.1365-313x.2011.04771.x;
RA Zhuang X., Koellner T.G., Zhao N., Li G., Jiang Y., Zhu L., Ma J.,
RA Degenhardt J., Chen F.;
RT "Dynamic evolution of herbivore-induced sesquiterpene biosynthesis in
RT sorghum and related grass crops.";
RL Plant J. 69:70-80(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 22-544.
RC STRAIN=cv. BTx623;
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman M.,
RA Ware D., Westhoff P., Mayer K.F.X., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(2009).
CC -!- FUNCTION: Sesquiterpene synthase converting farnesyl diphosphate into
CC beta-sesquiphellandrene and six minor products, zingiberene, 7-epi-
CC sesquithujene, sesquisabinene A, (E)-alpha-bergamotene, (E)-beta-
CC farnesene and beta-bisabolene. Can also accept geranyl diphosphate as
CC substrate, producing nine monoterpenes, with myrcene and limonene as
CC the major products. {ECO:0000269|PubMed:21880075}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = beta-sesquiphellandrene +
CC diphosphate; Xref=Rhea:RHEA:32699, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:64361, ChEBI:CHEBI:175763; EC=4.2.3.123;
CC Evidence={ECO:0000269|PubMed:21880075};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Up-regulated by herbivory. {ECO:0000269|PubMed:21880075}.
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}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; CM000766; EES13422.1; -; Genomic_DNA.
DR AlphaFoldDB; C5YHI2; -.
DR SMR; C5YHI2; -.
DR EnsemblPlants; EES14619; EES14619; SORBI_3007G055700.
DR Gramene; EES14619; EES14619; SORBI_3007G055700.
DR eggNOG; ENOG502QUCN; Eukaryota.
DR HOGENOM; CLU_003125_7_2_1; -.
DR InParanoid; C5YHI2; -.
DR OMA; QCYMLEH; -.
DR OrthoDB; 360509at2759; -.
DR BRENDA; 4.2.3.123; 5768.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000000768; Chromosome 7.
DR ExpressionAtlas; C5YHI2; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0102887; F:beta-sesquiphellandrene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
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; Plant defense;
KW Reference proteome.
FT CHAIN 1..545
FT /note="Beta-sesquiphellandrene synthase"
FT /id="PRO_0000418830"
FT MOTIF 299..303
FT /note="DDXXD motif"
FT BINDING 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 443
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 447
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 451
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT MUTAGEN 373
FT /note="Y->S: Increased production of (E)-alpha-bergamotene
FT and (E)-beta-farnesene."
FT /evidence="ECO:0000269|PubMed:21880075"
FT MUTAGEN 405
FT /note="V->L: Changed product specificity and production of
FT mainly zingiberene."
FT /evidence="ECO:0000269|PubMed:21880075"
SQ SEQUENCE 545 AA; 63360 MW; DEC7711338AF5281 CRC64;
MALTPSVCSI SDVQGLQKDR TFHPSLWGDF FLTYQPPTAP KHAYMAERAE VLKEEVRKMV
KSANEIQNIL DLILTLQRLG LDNHYENEIN ELLSFVHDSD YDDKDLNLVS LRFYLLRKHG
YDVSSDVFKC FQDKEGNFVV KDTKSLLSLY NAAHLRIHGE EVLDEAIIFT RGKLESVLDS
LETTLADEVT LALQTPLFRR VRILETRNYI PIYEKEVARN EVILEFAKLN FNLLQLLYCE
ELKMITLWWK QLNVETNLSF IRDRIVEMHF WMTGACSEKK YSLTRTITTK MTAYITILDD
IMDTHSTTEE AMLLAEAIYR CEENAAELLP EYMKDFYLYL LKTFDSVKHE LGPNRSFRVF
YLKELLKILV RGYSQEIKWR DEHYVPETID EHLEVSKATV GAFQVACSSF VGMGDIITKE
ILDWLLSYPK LLKSMTTFVR LSNDIASTKR EQTGGHHAST VQCYMMQHGT TIHDACEKIK
ELTEDTWKDM MKLYLTPTEQ PKVIIQTVLD FARTAEFMYK KTDAFTFSHT IKDTIALLFV
EPTLV