STS25_POSPM
ID STS25_POSPM Reviewed; 332 AA.
AC A0A348B793;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2018, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=Monoterpene synthase 25 {ECO:0000303|PubMed:30105900};
DE EC=4.2.3.- {ECO:0000269|PubMed:30105900};
DE AltName: Full=Terpene cyclase 25 {ECO:0000303|PubMed:30105900};
GN Name=STS-25 {ECO:0000303|PubMed:30105900};
OS Postia placenta (strain ATCC 44394 / Madison 698-R) (Brown rot fungus)
OS (Poria monticola).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Dacryobolaceae; Postia.
OX NCBI_TaxID=561896;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DOMAIN, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 44394 / Madison 698-R;
RX PubMed=30105900; DOI=10.1111/1751-7915.13304;
RA Ichinose H., Kitaoka T.;
RT "Insight into metabolic diversity of the brown-rot basidiomycete Postia
RT placenta responsible for sesquiterpene biosynthesis: semi-comprehensive
RT screening of cytochrome P450 monooxygenase involved in protoilludene
RT metabolism.";
RL Microb. Biotechnol. 11:952-965(2018).
CC -!- FUNCTION: Terpene cyclase that catalyzes the cyclization of geranyl
CC diphosphate (GPP) to myrcene and linalool.
CC {ECO:0000269|PubMed:30105900}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:I3ZNU9};
CC -!- DOMAIN: The conserved DDXXXXD and NSE/DTE motifs are important for the
CC catalytic activity, presumably through binding to Mg(2+).
CC {ECO:0000305|PubMed:30105900}.
CC -!- SIMILARITY: Belongs to the trichodiene synthase family. {ECO:0000305}.
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DR EMBL; LC378439; BBD74531.1; -; mRNA.
DR AlphaFoldDB; A0A348B793; -.
DR SMR; A0A348B793; -.
DR GO; GO:0016838; F:carbon-oxygen lyase activity, acting on phosphates; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 SFLD; SFLDG01021; Trichodiene_Synthase_Like; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding.
FT CHAIN 1..332
FT /note="Monoterpene synthase 25"
FT /id="PRO_0000451375"
FT MOTIF 115..121
FT /note="DDXXXXD motif"
FT /evidence="ECO:0000305|PubMed:30105900"
FT MOTIF 240..248
FT /note="NSE/DTE motif"
FT /evidence="ECO:0000305|PubMed:30105900"
FT BINDING 115
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13513"
FT BINDING 180
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13513"
FT BINDING 240
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13513"
FT BINDING 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13513"
FT BINDING 248
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13513"
SQ SEQUENCE 332 AA; 37340 MW; C0ED64BDA6307BB4 CRC64;
MSPTSDFVNT TSTAKGHEII AGLTAKPVEG STITLCKDII REFFDKVQVP SPNFTRDPEL
EARVADIVRT WGNEEHLRPY VVTSLILTVT AYSHIANFET RVQITLFTII IIAMDDPVVF
DSLATREFHQ RMCTGVIQDE AGMLGAFTKI LESMWDHYSG FSANTIYASA LRFVNASIIE
NETDVTTLRS HALPFVEYKR SMTATTEAYA CFIWDKARFP DVKVYMQAIP DAMLYVSYVN
DILSFYKEEL AGETANYIHE RAYVTGKSIP DTLRNLINET ASAVERVRDI LGEGEARAAF
ENFAAGYIRV HTGNPRYHLK DVIGGDYIID RV