TPS8_DICDI
ID TPS8_DICDI Reviewed; 312 AA.
AC Q54BE5;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Terpene synthase 8 {ECO:0000303|PubMed:27790999};
DE EC=4.2.3.- {ECO:0000269|PubMed:31063135};
DE AltName: Full=Discodiene biosynthesis cluster protein tps8 {ECO:0000303|PubMed:31063135};
GN Name=tps8 {ECO:0000303|PubMed:27790999}; ORFNames=DDB0192081;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, FUNCTION, AND DOMAIN.
RC STRAIN=AX4;
RX PubMed=27790999; DOI=10.1073/pnas.1610379113;
RA Chen X., Koellner T.G., Jia Q., Norris A., Santhanam B., Rabe P.,
RA Dickschat J.S., Shaulsky G., Gershenzon J., Chen F.;
RT "Terpene synthase genes in eukaryotes beyond plants and fungi: Occurrence
RT in social amoebae.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:12132-12137(2016).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=31063135; DOI=10.7554/elife.44352;
RA Chen X., Luck K., Rabe P., Dinh C.Q., Shaulsky G., Nelson D.R.,
RA Gershenzon J., Dickschat J.S., Koellner T.G., Chen F.;
RT "A terpene synthase-cytochrome P450 cluster in Dictyostelium discoideum
RT produces a novel trisnorsesquiterpene.";
RL Elife 8:0-0(2019).
CC -!- FUNCTION: Terpene synthase; part of the gene cluster that mediates the
CC biosynthesis of the trisnorsesquiterpene discodiene which has a
CC function during later stages of multicellular development, during the
CC transition from fingers to Mexican hats (PubMed:27790999,
CC PubMed:31063135). The terpene synthase tps8 converts its substrate
CC farnesyl diphosphate (FDP) into the bicyclic sesquiterpene alcohol
CC discoidol (PubMed:31063135). The cytochrome P450 monooxygenase cyp521A1
CC then catalyzes the oxidative degradation of discoidol to form the
CC trisnorsesquiterpene discodiene (PubMed:31063135).
CC {ECO:0000269|PubMed:27790999, ECO:0000269|PubMed:31063135}.
CC -!- PATHWAY: Sesquiterpene biosynthesis. {ECO:0000269|PubMed:31063135}.
CC -!- INDUCTION: Expression is almost undetectable in vegetatively growing
CC cells (PubMed:27790999, PubMed:31063135). Small amounts of transcripts
CC accumulate between 4-8 hrs of development, continue to accumulate until
CC they peak at 16 hrs, and decline thereafter (PubMed:27790999,
CC PubMed:31063135). {ECO:0000269|PubMed:27790999,
CC ECO:0000269|PubMed:31063135}.
CC -!- DOMAIN: Contains several highly conserved motifs that are important for
CC catalytic activity including the aspartate-rich 'DDxx(x)D/E' motif and
CC the 'NDxxSxxxD/E' motif, both of which are involved in complexing metal
CC ions to coordinate the binding of the isoprenyl diphosphate substrate
CC in the active site. {ECO:0000305|PubMed:31063135}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of discoidol and
CC discodiene, and leads to delayed multicellular development.
CC {ECO:0000269|PubMed:31063135}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; KX364381; APC23392.1; -; mRNA.
DR EMBL; AAFI01000293; EAL60645.1; -; Genomic_DNA.
DR RefSeq; XP_629084.1; XM_629082.1.
DR AlphaFoldDB; Q54BE5; -.
DR SMR; Q54BE5; -.
DR STRING; 44689.DDB0304480; -.
DR PaxDb; Q54BE5; -.
DR GeneID; 8629377; -.
DR KEGG; ddi:DDB_G0293666; -.
DR dictyBase; DDB_G0293666; tps8.
DR eggNOG; ENOG502RHRK; Eukaryota.
DR HOGENOM; CLU_892617_0_0_1; -.
DR InParanoid; Q54BE5; -.
DR OMA; SECKGIN; -.
DR PRO; PR:Q54BE5; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0010334; F:sesquiterpene synthase activity; TAS:dictyBase.
DR GO; GO:0051762; P:sesquiterpene biosynthetic process; TAS:dictyBase.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Lyase; Metal-binding.
FT CHAIN 1..312
FT /note="Terpene synthase 8"
FT /id="PRO_0000448097"
FT MOTIF 96..101
FT /note="DDxx(x)D/E motif"
FT /evidence="ECO:0000305|PubMed:31063135"
FT MOTIF 224..232
FT /note="NDxxSxxxD/E motif"
FT /evidence="ECO:0000305|PubMed:31063135"
SQ SEQUENCE 312 AA; 37305 MW; 2B59D0CF07DD42CA CRC64;
MDYDIKFTWD KNQFLDQEIR IPKYTLPWDF KSSPFDKDFE NQEMEYVKQF FQNYENAVNY
VKKNEIGKIA ALNFPLGEKD EYMVNSKLLD FLFILDDYIY ESRNYEEDYV DNLMDRSSKS
HDPFGREIWR LFDEYYRVGV KESVDLLIRD FEYWSRSAIK TNKYKSLNSS LSIEDYFNSR
HGDFGMTITA SSCTSTLYVE NEIRESKNFK KFFKYFELCN LMINDCGSFK MEINEILLTN
FVKVRAIQLG SIDLALKYCV GLLNKYIIKV DKYSTKLEQQ YPNHSHLKKY IYTLKTFTAG
HNKGYGHANR YN