GLIP_TANCI
ID GLIP_TANCI Reviewed; 365 AA.
AC H6U1I8; H6U1I5; H6U1I7; H6U1J0;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 1.
DT 25-MAY-2022, entry version 32.
DE RecName: Full=GDSL lipase {ECO:0000303|PubMed:22385412, ECO:0000303|PubMed:23104830};
DE Short=TcGLIP {ECO:0000303|PubMed:22385412, ECO:0000303|PubMed:23104830};
DE EC=3.1.1.- {ECO:0000305};
DE AltName: Full=Pyrethrin type I synthase {ECO:0000305|PubMed:22385412};
DE Flags: Precursor;
GN Name=GLIP {ECO:0000303|PubMed:22385412, ECO:0000303|PubMed:23104830};
OS Tanacetum cinerariifolium (Dalmatian daisy) (Chrysanthemum
OS cinerariifolium).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC Anthemidinae; Tanacetum.
OX NCBI_TaxID=118510;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Ovary;
RX PubMed=23104830; DOI=10.1105/tpc.112.105031;
RA Ramirez A.M., Stoopen G., Menzel T.R., Gols R., Bouwmeester H.J., Dicke M.,
RA Jongsma M.A.;
RT "Bidirectional secretions from glandular trichomes of pyrethrum enable
RT immunization of seedlings.";
RL Plant Cell 24:4252-4265(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 28-60 AND
RP 145-151, FUNCTION, MUTAGENESIS OF SER-40, SUBCELLULAR LOCATION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND INDUCTION
RP BY WOUNDING.
RX PubMed=22385412; DOI=10.1111/j.1365-313x.2012.04980.x;
RA Kikuta Y., Ueda H., Takahashi M., Mitsumori T., Yamada G., Sakamori K.,
RA Takeda K., Furutani S., Nakayama K., Katsuda Y., Hatanaka A., Matsuda K.;
RT "Identification and characterization of a GDSL lipase-like protein that
RT catalyzes the ester-forming reaction for pyrethrin biosynthesis in
RT Tanacetum cinerariifolium- a new target for plant protection.";
RL Plant J. 71:183-193(2012).
RN [3]
RP REVIEW.
RX PubMed=15964038; DOI=10.1016/j.phytochem.2005.05.005;
RA Matsuda K., Kikuta Y., Haba A., Nakayama K., Katsuda Y., Hatanaka A.,
RA Komai K.;
RT "Biosynthesis of pyrethrin I in seedlings of Chrysanthemum
RT cinerariaefolium.";
RL Phytochemistry 66:1529-1535(2005).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=29122986; DOI=10.1104/pp.17.01330;
RA Xu H., Moghe G.D., Wiegert-Rininger K., Schilmiller A.L., Barry C.S.,
RA Last R.L., Pichersky E.;
RT "Coexpression analysis identifies two oxidoreductases involved in the
RT biosynthesis of the monoterpene acid moiety of natural pyrethrin
RT insecticides in Tanacetum cinerariifolium.";
RL Plant Physiol. 176:524-537(2018).
RN [5]
RP REVIEW.
RX PubMed=30468448; DOI=10.1039/c8np00077h;
RA Liu Y., Jing S.-X., Luo S.-H., Li S.-H.;
RT "Non-volatile natural products in plant glandular trichomes: chemistry,
RT biological activities and biosynthesis.";
RL Nat. Prod. Rep. 36:626-665(2019).
CC -!- FUNCTION: Component of the monoterpenoid pyrethrins biosynthesis;
CC pyrethrins are widely used plant-derived pesticide (PubMed:30468448).
CC Acyltransferase that catalyzes the esterification of terpene acids and
CC lipid alcohol substrates into pyrethrins; mediates the transfer of a
CC chrysanthemoyl moiety from the coenzyme A (CoA) thio-ester
CC chrysanthemoyl CoA to pyrethrolone, and, to a lower extent, to
CC jasmololone and cinerolone thus producing pyrethrins (e.g. pyrethrin
CC type I) (PubMed:22385412). Can also use pyrethroyl CoA as substrate
CC (PubMed:22385412). Has also esterase activity, being able to cleave the
CC ester bond of pyrethrin I, p-nitrophenyl butanoate and p-nitrophenyl
CC octanoate to produce pyrethrolone and p-nitrophenol, respectively
CC (PubMed:22385412). {ECO:0000269|PubMed:22385412,
CC ECO:0000303|PubMed:30468448}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1R,3R)-chrysanthemoyl-CoA + (Z,S)-pyrethrolone = CoA +
CC pyrethrin I; Xref=Rhea:RHEA:60744, ChEBI:CHEBI:27815,
CC ChEBI:CHEBI:39111, ChEBI:CHEBI:57287, ChEBI:CHEBI:143950;
CC Evidence={ECO:0000269|PubMed:22385412};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60745;
CC Evidence={ECO:0000269|PubMed:22385412};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1R,3R)-pyrethroyl-CoA + (Z,S)-pyrethrolone = CoA + pyrethrin
CC II; Xref=Rhea:RHEA:60748, ChEBI:CHEBI:27474, ChEBI:CHEBI:39111,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:143953;
CC Evidence={ECO:0000269|PubMed:22385412};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60749;
CC Evidence={ECO:0000269|PubMed:22385412};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1R,3R)-chrysanthemoyl-CoA + (Z,S)-jasmololone = CoA +
CC jasmolin I; Xref=Rhea:RHEA:60752, ChEBI:CHEBI:39113,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:143950, ChEBI:CHEBI:143951;
CC Evidence={ECO:0000269|PubMed:22385412};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60753;
CC Evidence={ECO:0000269|PubMed:22385412};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1R,3R)-chrysanthemoyl-CoA + (Z,S)-cinerolone = cinerin I +
CC CoA; Xref=Rhea:RHEA:60756, ChEBI:CHEBI:3706, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:143950, ChEBI:CHEBI:143952;
CC Evidence={ECO:0000269|PubMed:22385412};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60757;
CC Evidence={ECO:0000269|PubMed:22385412};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1R,3R)-pyrethroyl-CoA + (Z,S)-jasmololone = CoA + jasmolin
CC II; Xref=Rhea:RHEA:60760, ChEBI:CHEBI:39114, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:143951, ChEBI:CHEBI:143953;
CC Evidence={ECO:0000269|PubMed:22385412};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60761;
CC Evidence={ECO:0000269|PubMed:22385412};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1R,3R)-pyrethroyl-CoA + (Z,S)-cinerolone = cinerin II + CoA;
CC Xref=Rhea:RHEA:60764, ChEBI:CHEBI:3707, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:143952, ChEBI:CHEBI:143953;
CC Evidence={ECO:0000269|PubMed:22385412};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60765;
CC Evidence={ECO:0000269|PubMed:22385412};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=768 uM for (1R,3R)-chrysanthemoyl CoA (in the presence of (S)-
CC pyrethrolone, at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:22385412};
CC KM=30.7 uM for (S)-pyrethrolone (in the presence of (1R,3R)-
CC chrysanthemoyl CoA, at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:22385412};
CC KM=1050 uM for (1R,3R)-pyrethroyl CoA (in the presence of (S)-
CC pyrethrolone, at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:22385412};
CC KM=31.7 uM for (S)-pyrethrolone (in the presence of (1R,3R)-
CC pyrethroyl CoA, at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:22385412};
CC Vmax=1.52 nmol/sec/mg enzyme with (1R,3R)-chrysanthemoyl CoA as
CC substrate (in the presence of (S)-pyrethrolone, at pH 7.5 and 25
CC degrees Celsius) {ECO:0000269|PubMed:22385412};
CC Vmax=0.95 nmol/sec/mg enzyme with (1R,3R)-pyrethroyl CoA as substrate
CC (in the presence of (S)-pyrethrolone, at pH 7.5 and 25 degrees
CC Celsius) {ECO:0000269|PubMed:22385412};
CC Vmax=1.17 nmol/sec/mg enzyme with (S)-pyrethrolone as substrate (in
CC the presence of (1R,3R)-chrysanthemoyl CoA, at pH 7.5 and 25 degrees
CC Celsius) {ECO:0000269|PubMed:22385412};
CC Vmax=0.65 nmol/sec/mg enzyme with (S)-pyrethrolone as substrate (in
CC the presence of (1R,3R)-pyrethroyl CoA, at pH 7.5 and 25 degrees
CC Celsius) {ECO:0000269|PubMed:22385412};
CC Vmax=0.0105 nmol/sec/mg enzyme with pyrethrin I as substrate (in the
CC absence of CoA, at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:22385412};
CC Vmax=0.0305 nmol/sec/mg enzyme with pyrethrin I as substrate (in the
CC presence of CoA, at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:22385412};
CC Vmax=0.88 nmol/sec/mg enzyme with p-nitrophenyl butanoate as
CC substrate (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:22385412};
CC Vmax=0.309 nmol/sec/mg enzyme with p-nitrophenyl octanoate as
CC substrate (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:22385412};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:22385412};
CC Temperature dependence:
CC Optimum temperature is 25 degrees Celsius.
CC {ECO:0000269|PubMed:22385412};
CC -!- PATHWAY: Isoprenoid biosynthesis. {ECO:0000269|PubMed:22385412}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000269|PubMed:22385412}.
CC -!- TISSUE SPECIFICITY: Restricted to the pericarp during achene maturation
CC (PubMed:23104830). Expressed in the leaves of mature plants and
CC seedlings, as well as in buds and flowers (PubMed:22385412,
CC PubMed:29122986). Present in disk florets (PubMed:29122986).
CC {ECO:0000269|PubMed:22385412, ECO:0000269|PubMed:23104830,
CC ECO:0000269|PubMed:29122986}.
CC -!- DEVELOPMENTAL STAGE: Mostly expressed in ovaries of flowers at stages
CC S1 to S7 (bud to overblown), before the first disk florets opening, and
CC prior embryos formation. {ECO:0000269|PubMed:23104830}.
CC -!- INDUCTION: By wounding. {ECO:0000269|PubMed:22385412}.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC {ECO:0000305}.
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DR EMBL; JQ513384; AFJ04755.1; -; Genomic_DNA.
DR EMBL; JX913533; AGC03152.1; -; mRNA.
DR EMBL; JN418990; AEZ63353.1; -; mRNA.
DR EMBL; JN418992; AEZ63355.1; -; mRNA.
DR EMBL; JN418991; AEZ63354.1; -; mRNA.
DR EMBL; JN418993; AEZ63356.1; -; mRNA.
DR EMBL; JN418994; AEZ63357.1; -; mRNA.
DR EMBL; JN418995; AEZ63358.1; -; mRNA.
DR EMBL; JN418996; AEZ63359.1; -; mRNA.
DR AlphaFoldDB; H6U1I8; -.
DR SMR; H6U1I8; -.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0016746; F:acyltransferase activity; IMP:UniProtKB.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IMP:UniProtKB.
DR GO; GO:0016412; F:serine O-acyltransferase activity; IMP:CACAO.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
DR CDD; cd01837; SGNH_plant_lipase_like; 1.
DR Gene3D; 3.40.50.1110; -; 1.
DR InterPro; IPR001087; GDSL.
DR InterPro; IPR044552; GLIP1-5/GLL25.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR InterPro; IPR035669; SGNH_plant_lipase-like.
DR PANTHER; PTHR45966; PTHR45966; 1.
DR Pfam; PF00657; Lipase_GDSL; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:22385412"
FT CHAIN 28..365
FT /note="GDSL lipase"
FT /id="PRO_5007666575"
FT ACT_SITE 40
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q09LX1"
FT ACT_SITE 318
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q09LX1"
FT ACT_SITE 321
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q09LX1"
FT SITE 137
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q09LX1"
FT SITE 168
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q09LX1"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 40
FT /note="S->A: Reduced acyltransferase and esterase
FT activities."
FT /evidence="ECO:0000269|PubMed:22385412"
FT CONFLICT 103
FT /note="D -> Y (in Ref. 2; AEZ63359)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="T -> A (in Ref. 2; AEZ63353/AEZ63354/AEZ63355)"
FT /evidence="ECO:0000305"
FT CONFLICT 249..253
FT /note="QLEKQ -> HLEKE (in Ref. 2; AEZ63353/AEZ63354/
FT AEZ63355)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="Y -> F (in Ref. 2; AEZ63356/AEZ63353/AEZ63354/
FT AEZ63355)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 365 AA; 40378 MW; 7C7939D11F35B969 CRC64;
MAVASRKLGA LVLVAVLCLS LPTGCLSSQQ AAALFIFGDS VFDPGNNNHI NTHVNFKANF
WPYGQSYFSS PTGRFSDGRI IPDFIAEYAS LPIIPAYLEP NNDFTHGANF ASAGAGALIA
SHAGLAVGLQ TQLRYFGDLV DHYRQNLGDI KSRQLLSDAV YLFSCGGNDY QSPYYPYTQE
QYVDIVIGNM TNVIKGIYEK GGRKFGVVNV PLIGCWPGMR AKQPGNTCNT EVDELTRLHN
QAFAKRLEQL EKQLEGFVYA KFDLSTAILN RMKNPSKYGF KEGESACCGS GPFGGNYDCG
RIKEFGLCDN ATEYFFFDPF HPNELASRQF AEMFWDGDSM VTQPYNLKAL FEGKPSTKYL
PNDEL
