ID TPS1_ACYSU Reviewed; 332 AA. AC A0A385AJM2; DT 14-DEC-2022, integrated into UniProtKB/Swiss-Prot. DT 05-DEC-2018, sequence version 1. DT 22-FEB-2023, entry version 8. DE RecName: Full=Terpene synthase 1 {ECO:0000303|PubMed:30254228}; DE EC=4.2.3.160 {ECO:0000269|PubMed:30254228}; GN Name=TPS1 {ECO:0000303|PubMed:30254228}; OS Acytostelium subglobosum (Slime mold). OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Acytosteliales; OC Acytosteliaceae; Acytostelium. OX NCBI_TaxID=361139; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY. RC STRAIN=LB1; RX PubMed=30254228; DOI=10.1038/s41598-018-32639-0; RA Chen X., Kollner T.G., Shaulsky G., Jia Q., Dickschat J.S., Gershenzon J., RA Chen F.; RT "Diversity and Functional Evolution of Terpene Synthases in Dictyostelid RT Social Amoebae."; RL Sci. Rep. 8:14361-14361(2018). CC -!- FUNCTION: Terpene synthase that converts its substrate farnesyl CC diphosphate (FPP) into the sesquiterpene protoillud-7-ene. CC {ECO:0000269|PubMed:30254228}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E,6E)-farnesyl diphosphate = (2S,3R,6S,9S)-(-)-protoillud-7- CC ene + diphosphate; Xref=Rhea:RHEA:53628, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:137530, ChEBI:CHEBI:175763; EC=4.2.3.160; CC Evidence={ECO:0000269|PubMed:30254228}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53629; CC Evidence={ECO:0000269|PubMed:30254228}; 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:0000250|UniProtKB:Q55E23}. 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; MG262459; AXN72967.1; -; mRNA. DR AlphaFoldDB; A0A385AJM2; -. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 1. DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf. DR PANTHER; PTHR35201; TERPENE SYNTHASE; 1. DR PANTHER; PTHR35201:SF3; TERPENE SYNTHASE; 1. DR Pfam; PF19086; Terpene_syn_C_2; 1. DR SUPFAM; SSF48576; Terpenoid synthases; 1. PE 1: Evidence at protein level; KW Lyase; Metal-binding. FT CHAIN 1..332 FT /note="Terpene synthase 1" FT /id="PRO_0000457030" FT MOTIF 81..86 FT /note="DDxx(x)D/E motif" FT /evidence="ECO:0000250|UniProtKB:Q54BE5" FT MOTIF 221..229 FT /note="NDxxSxxxD/E motif" FT /evidence="ECO:0000250|UniProtKB:Q54BE5" SQ SEQUENCE 332 AA; 39197 MW; BC6A1B42924C489F CRC64; MSLSLNDIKF PMHWNLDPNE FSYVEYVYRE GLELGVWRPD NKRDQMAHTN VVSLSRYFWP NVDFDRLVMG GELMLWFFTF DDGLDAGIYD DQKSLELVRR MDIVFMDGIL PEDPTGPEKV ALRLRNKCLA MCGRRKDTFN RFITSCVQWV DSIIPFNKVK VGGQSPHIEL YSFLRKINIG AYPCVTLTEV MLNHHLESYI WADPRWIKMN EDIAIVVTLI NDLVSYEKEV NDNAGDLNPL FFFQRQNNVD LCDSYKQMVT LIDYYVDHYV QLEQGFLRTL AKYHNPLQEQ EVNFMLDHLH YLITGSRMWS MQTPRYCSPT SPFIEMRKFR EA //