TPS21_MAIZE
ID TPS21_MAIZE Reviewed; 571 AA.
AC A0A291LSD6;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2017, sequence version 1.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=Beta-selinene synthase {ECO:0000303|PubMed:28931629};
DE EC=4.2.3.66 {ECO:0000269|PubMed:28931629};
DE AltName: Full=Terpene synthase 21 {ECO:0000303|PubMed:28931629};
DE Short=ZmTps21 {ECO:0000303|PubMed:28931629};
GN Name=TPS21 {ECO:0000303|PubMed:30187155};
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 [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP INDUCTION BY FUNGUS.
RC STRAIN=cv. HP301, cv. Missouri 17, and cv. Ohio 43;
RX PubMed=28931629; DOI=10.1104/pp.17.00879;
RA Ding Y., Huffaker A., Koellner T.G., Weckwerth P., Robert C.A.M.,
RA Spencer J.L., Lipka A.E., Schmelz E.A.;
RT "Selinene volatiles are essential precursors for maize defense promoting
RT fungal pathogen resistance.";
RL Plant Physiol. 175:1455-1468(2017).
RN [2]
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: Sesquiterpene cyclase that converts farnesyl diphosphate to
CC the volatile beta-selinene and the corresponding nonvolatile antibiotic
CC derivative beta-costic acid, especially in roots upon infection by
CC rootworm larvae (D.balteata) and fungal pathogens (e.g. Fusarium spp.).
CC {ECO:0000269|PubMed:28931629}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (+)-beta-selinene +
CC diphosphate; Xref=Rhea:RHEA:29483, ChEBI:CHEBI:10443,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.66;
CC Evidence={ECO:0000269|PubMed:28931629};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29484;
CC Evidence={ECO:0000269|PubMed:28931629};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q1EG72};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q1EG72};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:Q1EG72};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000250|UniProtKB:Q1EG72}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q6JD73}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6Q3H2}.
CC -!- INDUCTION: Accumulates strongly following fungal elicitation (e.g.
CC Fusarium spp., C.heterostrophus, F.verticillioides, R.microsporus and
CC A.parasiticus). {ECO:0000269|PubMed:28931629}.
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 -!- CAUTION: The allele found in cv. Missouri 17 (AC K7WDC8) encodes an
CC active enzyme while the allele found in cv. B73 contains a frame shift
CC mutation. {ECO:0000305|PubMed:28931629}.
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DR EMBL; MF614110; ATI25525.1; -; Genomic_DNA.
DR EMBL; MF614112; ATI25527.1; -; Genomic_DNA.
DR EMBL; MF614115; ATI25530.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A291LSD6; -.
DR SMR; A0A291LSD6; -.
DR MaizeGDB; 9022637; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; A0A291LSD6; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; IDA:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IEP:UniProtKB.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0080027; P:response to herbivore; IEP:UniProtKB.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IDA:UniProtKB.
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..571
FT /note="Beta-selinene synthase"
FT /id="PRO_0000447519"
FT MOTIF 325..329
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 325
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 325
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 325
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 329
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 329
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 329
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 464
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 467
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 467
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 471
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 571 AA; 64463 MW; 7609216EE3145035 CRC64;
MDGDIAAALP PVNQQSKADG TAVAAAAAAA ACHGDFEPSV WGDFFVTYTS PPSLSQEPEE
QMRERANFLK GEVRKKFEAA AAMSAINSAM LVDAVVHLGI DHCFREEIAT ALRSVHKEEG
EFGSCDDLHT VAVRFLVLRQ HGLWVSADVF DKFRDDTGSL SKSLLCSNPR GLLSLYNAAH
MVTPEEKVLD DAIAFARSHL EAMIGELRSP MVEQVSRSLD IPLPRFSRRL ESMHYIAEYG
QEEGHDAQIL ELARLEFELV RSLHLRELRE ICRWWRELYN DVKLPYARDR IVEIYFWACG
VIHEEEMSRA RMIFAKTFAF TSLIDDTCDV HATLEEVQKF NEAMQSWEED AVSIVPEYLR
TLYSRTIKGF QEFEDMLEPN EKYSMSYVKK AYKLLLQYYL KEATWANENH TPSFKEHVQV
SIISSGLPML VPVLLMGTGL ATREAFEWAD SAPDMVLASG EVGRFLNDMA SYKLGKNKKD
VANAHECYMK EYGATGEEAF AFIANMTENA WRKINQACME MDPAMLPAFK VAVVDLSRSM
EIIYLGGKRD AYTFGSNLKD LVTSLFLKPC A
