MTS1_HUMLU
ID MTS1_HUMLU Reviewed; 585 AA.
AC B6SCF3;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Probable monoterpene synthase MTS1, chloroplastic {ECO:0000305};
DE Short=HlMTS1 {ECO:0000303|PubMed:18775972};
DE EC=4.2.3.- {ECO:0000305};
DE Flags: Precursor;
OS Humulus lupulus (European hop).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Humulus.
OX NCBI_TaxID=3486 {ECO:0000312|EMBL:ACI32637.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Lupulin gland;
RX PubMed=18775972; DOI=10.1104/pp.108.125187;
RA Wang G., Tian L., Aziz N., Broun P., Dai X., He J., King A., Zhao P.X.,
RA Dixon R.A.;
RT "Terpene biosynthesis in glandular trichomes of hop.";
RL Plant Physiol. 148:1254-1266(2008).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q40577};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in trichomes. Detected in flowers, but
CC not in leaves. {ECO:0000269|PubMed:18775972}.
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:Q40577}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: No monoterpene, sesquiterpene or diterpene synthase activity
CC detected in the heterologous expression system tested.
CC {ECO:0000305|PubMed:18775972}.
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DR EMBL; EU760348; ACI32637.1; -; mRNA.
DR AlphaFoldDB; B6SCF3; -.
DR SMR; B6SCF3; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
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; IPR034741; Terpene_cyclase-like_1_C.
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 SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Lyase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT TRANSIT 1..31
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 32..585
FT /note="Probable monoterpene synthase MTS1, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000439240"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 335..339
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT COMPBIAS 14..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 335
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 335
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 339
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 339
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 479
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 483
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 487
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 585 AA; 67511 MW; 7191F0BA8A3FC545 CRC64;
MSLSGVPLSA GLAPSPSNKP TNGKGQNIVR RSGNYKPALW DYDYLQSLPT LYAGEAHVEK
LNKLKGEVRI MLEKTVTENP LAQLEQIDTL YRLGISYHFQ DEIKALLNTI HNNNNNNNNN
DDVYATALEF KLLRLYGYTV HSEVFNVFKD EIDKGFKAIS LCGDYVKGML SLYEASFYSF
KGETILDEAR DFSTKHLQKY VMMRHNNNSK DQSVDDDDDL VILVEYALEL PMHWRMIRLE
AKWFIDVYSK RRDDMNPTFL ELAQIDFNLL QSTYQEDLKH VSRWWSTCKL GERLPFCRDR
LVEVFLLAVA LKYEAEFGYA RRLLTKIGVL VTLMDDIYDV YGTLDELKLL EDAIERWNIN
ELDQLPEYMN IFFVAMYNVV NGIAYDVLKE NEILIVKYLK RAWMDACKSY MVEAKWYYSG
YTPSLEEYLE NGLISITIPL DLIFLYCLTT SPITEDSMEY LLQYPTILGL SGTLFRLVDD
LATSSDELKR GDNPKSIQCY MHESGVCEND SREYIKNLIS ETWKQMNEVR VAKSPLFSQA
FIESAVDFVR GAMLLYQKGD GFGTKHDGDA KDKLVSLFFN PIPTP
