ACSS_MAIZE
ID ACSS_MAIZE Reviewed; 590 AA.
AC Q84ZW8; A0A1D6DZW2; Q9XEI5;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-JUL-2019, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Acyclic sesquiterpene synthase;
DE AltName: Full=(3R,6E)-nerolidol synthase {ECO:0000303|PubMed:12481088};
DE EC=4.2.3.49 {ECO:0000269|PubMed:12481088, ECO:0000269|PubMed:26620527};
DE AltName: Full=(R)-linalool synthase {ECO:0000303|PubMed:12481088};
DE EC=4.2.3.26 {ECO:0000269|PubMed:12481088};
DE AltName: Full=Beta-farnesene synthase {ECO:0000303|PubMed:12481088};
DE EC=4.2.3.47 {ECO:0000269|PubMed:12481088};
DE AltName: Full=Ent-kaurene synthase 2.1 {ECO:0000303|PubMed:22683264};
DE Short=ZmKS2.1 {ECO:0000303|PubMed:22683264};
DE EC=4.2.3.19 {ECO:0000269|PubMed:26620527};
DE AltName: Full=Farnesyl diphosphatase {ECO:0000303|PubMed:12481088};
DE EC=3.1.7.6 {ECO:0000269|PubMed:12481088};
DE AltName: Full=Geraniol synthase {ECO:0000303|PubMed:12481088};
DE EC=3.1.7.11 {ECO:0000269|PubMed:12481088};
DE AltName: Full=Terpene synthase 1 {ECO:0000303|PubMed:12481088};
DE Short=ZmTPS1 {ECO:0000303|PubMed:26620527};
DE Flags: Precursor;
GN Name=TPS1 {ECO:0000303|PubMed:12481088};
GN Synonyms=csu186 {ECO:0000305}, eks1 {ECO:0000305},
GN KS2.1 {ECO:0000303|PubMed:22683264};
GN ORFNames=GRMZM2G049538 {ECO:0000305},
GN ZEAMMB73_Zm00001d002351 {ECO:0000312|EMBL:ONM14044.1};
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], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, COFACTOR, TISSUE SPECIFICITY, INDUCTION BY HERBIVORY; WOUNDING
RP AND ELICITORS, AND FUNCTION.
RC STRAIN=cv. B73, and cv. Delprim;
RX PubMed=12481088; DOI=10.1104/pp.008326;
RA Schnee C., Kollner T.G., Gershenzon J., Degenhardt J.;
RT "The maize gene terpene synthase 1 encodes a sesquiterpene synthase
RT catalyzing the formation of (E)-beta-farnesene, (E)-nerolidol, and (E,E)-
RT farnesol after herbivore damage.";
RL Plant Physiol. 130:2049-2060(2002).
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 NUCLEOTIDE SEQUENCE [MRNA] OF 133-590.
RC TISSUE=Leaf;
RA Richman A.S., Brandle J.E.;
RT "Partial kaurene synthase gene from Zea mays.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=22683264; DOI=10.1016/j.cub.2012.04.065;
RA Nelissen H., Rymen B., Jikumaru Y., Demuynck K., Van Lijsebettens M.,
RA Kamiya Y., Inze D., Beemster G.T.S.;
RT "A local maximum in gibberellin levels regulates maize leaf growth by
RT spatial control of cell division.";
RL Curr. Biol. 22:1183-1187(2012).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND INDUCTION BY
RP FUNGUS; ETHEPHON AND JASMONIC ACID.
RC STRAIN=cv. B73, and cv. Missouri 17;
RX PubMed=26620527; DOI=10.1104/pp.15.01727;
RA Fu J., Ren F., Lu X., Mao H., Xu M., Degenhardt J., Peters R.J., Wang Q.;
RT "A tandem array of ent-kaurene synthases in maize with roles in gibberellin
RT and more specialized metabolism.";
RL Plant Physiol. 170:742-751(2016).
RN [6]
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: Involved in the formation of (E)-beta-farnesene and (3E)-4,8-
CC dimethyl-1,3,7-nonatriene, key signal molecules in induced plant
CC defense mediated by the attraction of enemies of herbivores
CC (PubMed:12481088). In the presence of geranyl diphosphate, catalyzes
CC the formation of the acyclic monoterpens (3R)-linalool and geraniol
CC (PubMed:12481088). However, the in vitro rate of sesquiterpene
CC formation is about four times higher than the rate of monoterpene
CC formation (PubMed:12481088). Mediates the conversion of ent-copalyl
CC diphosphate into ent-kaurene, thus having probably a role in
CC gibberellin biosynthesis (PubMed:26620527).
CC {ECO:0000269|PubMed:12481088, ECO:0000269|PubMed:26620527}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (E)-beta-farnesene +
CC diphosphate; Xref=Rhea:RHEA:27425, ChEBI:CHEBI:10418,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.47;
CC Evidence={ECO:0000269|PubMed:12481088};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27426;
CC Evidence={ECO:0000269|PubMed:12481088};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = (3R,6E)-nerolidol +
CC diphosphate; Xref=Rhea:RHEA:27534, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:59959, ChEBI:CHEBI:175763;
CC EC=4.2.3.49; Evidence={ECO:0000269|PubMed:12481088,
CC ECO:0000269|PubMed:26620527};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27535;
CC Evidence={ECO:0000269|PubMed:12481088, ECO:0000269|PubMed:26620527};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = (2E,6E)-farnesol +
CC diphosphate; Xref=Rhea:RHEA:27526, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16619, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=3.1.7.6;
CC Evidence={ECO:0000269|PubMed:12481088};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27527;
CC Evidence={ECO:0000269|PubMed:12481088};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + H2O = (2E)-geraniol + diphosphate;
CC Xref=Rhea:RHEA:32679, ChEBI:CHEBI:15377, ChEBI:CHEBI:17447,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=3.1.7.11;
CC Evidence={ECO:0000269|PubMed:12481088};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32680;
CC Evidence={ECO:0000269|PubMed:12481088};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + H2O = (R)-linalool + diphosphate;
CC Xref=Rhea:RHEA:15809, ChEBI:CHEBI:28, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.26;
CC Evidence={ECO:0000269|PubMed:12481088};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15810;
CC Evidence={ECO:0000269|PubMed:12481088};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ent-copalyl diphosphate = diphosphate + ent-kaur-16-ene;
CC Xref=Rhea:RHEA:22220, ChEBI:CHEBI:15415, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58553; EC=4.2.3.19;
CC Evidence={ECO:0000269|PubMed:26620527};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22221;
CC Evidence={ECO:0000269|PubMed:26620527};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12481088};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:12481088};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:Q5GJ60};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.1 uM for geranyl diphosphate {ECO:0000269|PubMed:12481088};
CC KM=1.0 uM for farnesyl diphosphate {ECO:0000269|PubMed:12481088};
CC KM=470 uM for magnesium {ECO:0000269|PubMed:12481088};
CC KM=26 uM for manganese {ECO:0000269|PubMed:12481088};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:12481088};
CC Temperature dependence:
CC Optimum temperature is between 30 and 37 degrees Celsius.
CC {ECO:0000269|PubMed:12481088};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305|PubMed:30187155}.
CC -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
CC {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q6JD73}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6Q3H2}.
CC Plastid, chloroplast {ECO:0000269|PubMed:26620527}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves and sheath tissues. Not
CC detected in roots. {ECO:0000269|PubMed:12481088}.
CC -!- INDUCTION: By herbivory, wounding or elicitor treatments in young
CC leaves of cv. B73, but not of cv. Delprim (PubMed:12481088). Induced
CC transiently by F.graminearum and combination of jasmonic acid (JA) and
CC ethephon (EP), an ethylene precursor (PubMed:26620527).
CC {ECO:0000269|PubMed:12481088, ECO:0000269|PubMed:26620527}.
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}.
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DR EMBL; AF529266; AAO18435.1; -; mRNA.
DR EMBL; CM007648; ONM14044.1; -; Genomic_DNA.
DR EMBL; AF105149; AAD34319.1; -; mRNA.
DR RefSeq; NP_001105097.2; NM_001111627.2.
DR AlphaFoldDB; Q84ZW8; -.
DR SMR; Q84ZW8; -.
DR STRING; 4577.GRMZM2G049538_P01; -.
DR PaxDb; Q84ZW8; -.
DR EnsemblPlants; Zm00001eb071090_T001; Zm00001eb071090_P001; Zm00001eb071090.
DR GeneID; 541974; -.
DR Gramene; Zm00001eb071090_T001; Zm00001eb071090_P001; Zm00001eb071090.
DR KEGG; zma:541974; -.
DR MaizeGDB; 1219908; -.
DR eggNOG; ENOG502QVGX; Eukaryota.
DR OrthoDB; 318477at2759; -.
DR BioCyc; MetaCyc:MON-12827; -.
DR BRENDA; 4.2.3.49; 6752.
DR UniPathway; UPA00213; -.
DR UniPathway; UPA00390; -.
DR Proteomes; UP000007305; Chromosome 2.
DR ExpressionAtlas; Q84ZW8; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0102145; F:(3R)-(E)-nerolidol synthase activity; IDA:UniProtKB.
DR GO; GO:0009899; F:ent-kaurene synthase activity; IDA:UniProtKB.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0034008; F:R-linalool synthase activity; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0033332; P:ent-kaurene biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006715; P:farnesol biosynthetic process; IDA:UniProtKB.
DR GO; GO:1903448; P:geraniol biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009686; P:gibberellin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009723; P:response to ethylene; IEP:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR GO; GO:0016106; P:sesquiterpenoid 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; 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; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Cytoplasm; Hydrolase; Lyase; Magnesium; Manganese;
KW Metal-binding; Plant defense; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..53
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 54..590
FT /note="Acyclic sesquiterpene synthase"
FT /id="PRO_0000405117"
FT REGION 39..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 333..337
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT COMPBIAS 39..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 333
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 333
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 333
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 337
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 337
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 337
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 474
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 477
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 477
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 481
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 485
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT CONFLICT 434
FT /note="T -> I (in Ref. 1; AAO18435)"
FT CONFLICT 503
FT /note="S -> P (in Ref. 1; AAO18435)"
SQ SEQUENCE 590 AA; 67328 MW; B899F3E5804CDBBD CRC64;
MAMPVKLTPA SLSLKAVCCR FSSGGHALRF GSSLPCWRRT PTQRSTSSST TRPAAEVSSG
KSKQHDQEAS EATIRQQLQL VDVLENMGIS RHFAAEIKCI LDRTYRSWLQ RHEEIMLDTM
TCAMAFRILR LNGYNVSSDE LYHVVEASGL HNSLGGYLND TRTLLELHKA STVSISEDES
ILDSIGSRSR TLLREQLESG GALRKPSLFK EVEHALDGPF YTTLDRLHHR WNIENFNIIE
QHMLETPYLS NQHTSRDILA LSIRDFSSSQ FTYQQELQHL ESWVKECRLD QLQFARQKLA
YFYLSAAGTM FSPELSDART LWAKNGVLTT IVDDFFDVAG SKEELENLVM LVEMWDEHHK
VEFYSEQVEI IFSSIYDSVN QLGEKASLVQ DRSITKHLVE IWLDLLKSMM TEVEWRLSKY
VPTEKEYMIN ASLTFGLGPI VLPALYFVGP KISESIVKDP EYDELFKLMS TCGRLLNDVQ
TFEREYNEGK LNSVSLLVLH GGSMSISDAK RKLQKPIDTC RRDLLSLVLR EESVVPRPCK
ELFWKMCKVC YFFYSTTDGF SSQVERAKEV DAVINEPLKL QGSHTLVSDV
