TCEA1_TULGE
ID TCEA1_TULGE Reviewed; 385 AA.
AC I4DST8; I4DSU2;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 1.
DT 25-MAY-2022, entry version 23.
DE RecName: Full=Tuliposide A-converting enzyme 1, chloroplastic;
DE Short=TgTCEA1;
DE EC=4.2.99.22;
DE Flags: Precursor;
GN Name=TCEA1; Synonyms=TCEA5;
OS Tulipa gesneriana (Garden tulip).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Liliales; Liliaceae; Tulipa.
OX NCBI_TaxID=13306;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 78-87; 96-107 AND 318-328,
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITES, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVITY REGULATION, MUTAGENESIS OF GLY-152; GLY-153; GLY-154; SER-235;
RP ASP-327; HIS-359 AND HIS-362, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP SUBUNIT.
RC TISSUE=Petal;
RX PubMed=22474185; DOI=10.1104/pp.112.195388;
RA Nomura T., Ogita S., Kato Y.;
RT "A novel lactone-forming carboxylesterase: molecular identification of a
RT tuliposide a-converting enzyme in tulip.";
RL Plant Physiol. 159:565-578(2012).
CC -!- FUNCTION: Lactone-forming carboxylesterases, specifically catalyzing
CC intramolecular transesterification, but not hydrolysis. Involved in the
CC biosynthesis of tulipalins, defensive chemicals that show antimicrobial
CC activities against a broad range of strains of bacteria and fungi.
CC Substrates are 6-tuliposide A > 6-tuliposide B.
CC {ECO:0000269|PubMed:22474185}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-tuliposide A = D-glucose + tulipalin A;
CC Xref=Rhea:RHEA:36071, ChEBI:CHEBI:4167, ChEBI:CHEBI:72781,
CC ChEBI:CHEBI:104120; EC=4.2.99.22;
CC Evidence={ECO:0000269|PubMed:22474185};
CC -!- ACTIVITY REGULATION: Inhibited by NaF, AgNO(3), HgCl(2), CuSO(4) and
CC phenylmethylsulfonyl fluoride (PMSF). {ECO:0000269|PubMed:22474185}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18 mM for 6-tuliposide A {ECO:0000269|PubMed:22474185};
CC KM=71 mM for 6-tuliposide B {ECO:0000269|PubMed:22474185};
CC Note=kcat is 2800 sec(-1) with 6-tuliposide A as substrate. kcat is
CC 510 sec(-1) with 6-tuliposide B as substrate.;
CC pH dependence:
CC Optimum pH is 6.5-7.5. {ECO:0000269|PubMed:22474185};
CC Temperature dependence:
CC Optimum temperature is 35-45 degrees Celsius.
CC {ECO:0000269|PubMed:22474185};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22474185}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:22474185}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, petals, stamens
CC and pistils, but not in bulb scales. {ECO:0000269|PubMed:22474185}.
CC -!- MISCELLANEOUS: 6-tuliposide A and tuliposide A-converting enzyme, which
CC are compartmentalized in the vacuoles and plastids respectively, come
CC into contact with each other for the enzyme reaction releasing toxic
CC tulipalin A upon cell disruption by pathogen infection or herbivore
CC predation. {ECO:0000305|PubMed:22474185}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR EMBL; AB569208; BAM20978.1; -; mRNA.
DR EMBL; AB569212; BAM20982.1; -; mRNA.
DR AlphaFoldDB; I4DST8; -.
DR SMR; I4DST8; -.
DR KEGG; ag:BAM20978; -.
DR BRENDA; 4.2.99.22; 6538.
DR BRENDA; 4.2.99.23; 6538.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Direct protein sequencing; Lyase; Plant defense; Plastid;
KW Transit peptide.
FT TRANSIT 1..77
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:22474185"
FT CHAIN 78..385
FT /note="Tuliposide A-converting enzyme 1, chloroplastic"
FT /id="PRO_0000423865"
FT ACT_SITE 235
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000305|PubMed:22474185"
FT ACT_SITE 327
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:22474185"
FT ACT_SITE 359
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:22474185"
FT MUTAGEN 152
FT /note="G->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:22474185"
FT MUTAGEN 153
FT /note="G->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:22474185"
FT MUTAGEN 154
FT /note="G->A: 12% reduction of activity."
FT /evidence="ECO:0000269|PubMed:22474185"
FT MUTAGEN 235
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:22474185"
FT MUTAGEN 327
FT /note="D->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:22474185"
FT MUTAGEN 359
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:22474185"
FT MUTAGEN 362
FT /note="H->A: 94% reduction of activity."
FT /evidence="ECO:0000269|PubMed:22474185"
FT CONFLICT 324
FT /note="A -> S (in Ref. 1; BAM20982)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 385 AA; 41511 MW; 1C01A8CF7D41E35F CRC64;
MSVASFFSSL PARPFGYKDG RGRTGMVPTT DIGRRMVKPP VLACRPIESN TYHGSVTSVF
LTKSSRSPSP SLSPTPTALD DEIVLDLKPF LIIYKSGRIE RFLGTTVIPA CPEVATKDVV
IDPATGVSVR LYLPNVVDLP SKKLPVLVYF HGGGFVIENT GSPNYHNYLT LLAAKAGVLI
VSINYRLAPE YPLPASYDDC MAGFNWVVSH SAGPALEPWL AQHGDFSQIL LSGDSAGGNV
THYVAMRADA GVIEGVAIVH PYFLGSEPVG NEINDPANIE FHDKLWRLAA PDTEGLDDPL
INPVAPGAPS LAGLKCKRAV VFVAGNDFLV ERGRMYYEAL VKSGWRGEAE LVQHEGVGHV
FHLSDYSGDI SVAMMTKLIA FLKGE
