MTSL4_MARPO
ID MTSL4_MARPO Reviewed; 431 AA.
AC A0A1L5YKS7;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=Alpha-gurjunene synthase {ECO:0000303|PubMed:27650333};
DE EC=4.2.3.184 {ECO:0000269|PubMed:27650333};
DE EC=4.2.3.72 {ECO:0000269|PubMed:27650333};
DE AltName: Full=5-hydroxy-alpha-gurjunene synthase {ECO:0000303|PubMed:27650333};
DE AltName: Full=Microbial terpene synthase-like 4 {ECO:0000303|PubMed:27650333};
DE Short=MpMTPSL4 {ECO:0000303|PubMed:27650333};
DE AltName: Full=Sesquiterpene synthase {ECO:0000305};
GN Name=MTPSL4 {ECO:0000303|PubMed:27650333};
OS Marchantia polymorpha (Liverwort) (Marchantia aquatica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=3197;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=27650333; DOI=10.1105/tpc.16.00062;
RA Kumar S., Kempinski C., Zhuang X., Norris A., Mafu S., Zi J., Bell S.A.,
RA Nybo S.E., Kinison S.E., Jiang Z., Goklany S., Linscott K.B., Chen X.,
RA Jia Q., Brown S.D., Bowman J.L., Babbitt P.C., Peters R.J., Chen F.,
RA Chappell J.;
RT "Molecular diversity of terpene synthases in the liverwort Marchantia
RT polymorpha.";
RL Plant Cell 28:2632-2650(2016).
CC -!- FUNCTION: Catalyzes the conversion of (2E,6E)-farnesyl diphosphate
CC (FPP) into the sesquiterpene alcohols (-)-alpha-gurjunene and 5-
CC hydroxy-alpha-gurjunene (PubMed:27650333). Other unidentified
CC sesquiterpene alcohols found to be catalyzed by MTPSL4 may arise from
CC carbocation reaction intermediates along the catalytic cascade to
CC gurjunene being quenched by a water molecule, yielding formation of the
CC alcohols (Probable). {ECO:0000269|PubMed:27650333,
CC ECO:0000305|PubMed:27650333}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (-)-alpha-gurjunene +
CC diphosphate; Xref=Rhea:RHEA:29507, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:61699, ChEBI:CHEBI:175763; EC=4.2.3.72;
CC Evidence={ECO:0000269|PubMed:27650333};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29509;
CC Evidence={ECO:0000269|PubMed:27650333};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = 5-hydroxy-alpha-gurjunene
CC + diphosphate; Xref=Rhea:RHEA:54380, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:138167, ChEBI:CHEBI:175763;
CC EC=4.2.3.184; Evidence={ECO:0000269|PubMed:27650333};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54381;
CC Evidence={ECO:0000269|PubMed:27650333};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:B5HDJ6};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:B5HDJ6};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=17.98 uM for (2E,6E)-farnesyl diphosphate
CC {ECO:0000269|PubMed:27650333};
CC Vmax=1.146 pmol/sec/ug enzyme {ECO:0000269|PubMed:27650333};
CC Note=kcat is 0.058 sec (-1) with (2E,6E)-farnesyl diphosphate as
CC substrate. {ECO:0000269|PubMed:27650333};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; KU664191; APP91789.1; -; mRNA.
DR AlphaFoldDB; A0A1L5YKS7; -.
DR SMR; A0A1L5YKS7; -.
DR KEGG; ag:APP91789; -.
DR BRENDA; 4.2.3.184; 3182.
DR UniPathway; UPA00213; -.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
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; Magnesium; Metal-binding.
FT CHAIN 1..431
FT /note="Alpha-gurjunene synthase"
FT /id="PRO_0000449918"
FT BINDING 126
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 130
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 130
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 267
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 321
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 325
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 328
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 329
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 412..413
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
SQ SEQUENCE 431 AA; 50271 MW; 8B5EEB57F6378D43 CRC64;
MAPTLDSDST VLSIRSDFRQ GRVQRQLKSE LYRNDNRMSV ENDFRAPYIQ LPYPQARLNP
KTTECMNITF DWLSSMGIDK QVDPSVWQAF VASRLSDIVG YSCNEDIEPE DFLWLCKFTT
WLFIFDSMMD DGHWAENICM SSHAILEMNL ILMWNDPENE RLLECSKSIL DLVMAIDASG
SRLQLDKFHA DMVDARKKSK SLLDVKMGVF TSAFRDCWME YVEDVPAEYT TRIAQTFQRY
ISSCLWEEKN RKEQAECMNV ADYVTLRRFS GCVEPYFVYV DRIIEHKRRK SPISHIPNTL
FYGEHMQNML AAATDVICWH NDIFSFPKET IREGDKHNLV YTVFQQYNCH SCTQAGELIV
ELLHDRIAEM EFAYEKLRSA AAPEFHPAID VYIKNCRDWI SGSHEFHMNS SRYNVRSFSG
PPENVKHINS V
