TPS1_METBS
ID TPS1_METBS Reviewed; 331 AA.
AC A0A0B4G504;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 1.
DT 25-MAY-2022, entry version 18.
DE RecName: Full=(E)-beta farnesene synthase MBR_03882 {ECO:0000303|PubMed:31239482};
DE EC=4.2.3.47 {ECO:0000269|PubMed:31239482};
DE AltName: Full=Typical fungal terpene synthase MBR_03882 {ECO:0000303|PubMed:31239482};
GN ORFNames=MBR_03882;
OS Metarhizium brunneum (strain ARSEF 3297).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=1276141;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 3297;
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=31239482; DOI=10.1038/s41598-019-45532-1;
RA Jia Q., Chen X., Koellner T.G., Rinkel J., Fu J., Labbe J., Xiong W.,
RA Dickschat J.S., Gershenzon J., Chen F.;
RT "Terpene synthase genes originated from bacteria through horizontal gene
RT transfer contribute to terpenoid diversity in fungi.";
RL Sci. Rep. 9:9223-9223(2019).
CC -!- FUNCTION: Terpene synthase that catalyzes the conversion of (2E,6E)-
CC farnesyl diphosphate (FPP) into the volatile sesquiterpene (E)-beta-
CC farnesene. {ECO:0000269|PubMed:31239482}.
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:31239482};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27426;
CC Evidence={ECO:0000269|PubMed:31239482};
CC -!- SIMILARITY: Belongs to the trichodiene 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; AZNG01000003; KID77563.1; -; Genomic_DNA.
DR RefSeq; XP_014546729.1; XM_014691243.1.
DR AlphaFoldDB; A0A0B4G504; -.
DR SMR; A0A0B4G504; -.
DR EnsemblFungi; KID77563; KID77563; MBR_03882.
DR GeneID; 26241152; -.
DR HOGENOM; CLU_052212_0_0_1; -.
DR GO; GO:0016838; F:carbon-oxygen lyase activity, acting on phosphates; IEA:InterPro.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR024652; Trichodiene_synth.
DR Pfam; PF06330; TRI5; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Lyase.
FT CHAIN 1..331
FT /note="(E)-beta farnesene synthase MBR_03882"
FT /id="PRO_0000451045"
SQ SEQUENCE 331 AA; 38026 MW; 788D6618F9C97EDC CRC64;
METDSFKRQY ADILRRYLCG ISYQKLSCEY DPSIEETVVQ HFRTLNFPND FLKRMMPIIH
ASAWIATSTY PFTPRHVQEA IAVYTSLAIA IEDTSKESTH DLKRFQQRLF NRQPQPNLLL
QAMVDCLVSL RGIYGPFICD MVAKSTAEYI SVCAFEAKYD GTLRPTPSSP DFPYYLRLKT
GVAEVYAFFA FPEVLYPEEA FLHEYILAVP DISRYFNLGN DLLSFYKESI VADERLNYIY
NCSRVSNSTP LESIWSTHLA LITCVENIRK TLSASPQMRR NIDQLINGYV MYHFGASRYK
LSDLGIQEVD ELRAKICCST TVDNGVGAYK H