ID   TCEA2_TULGE             Reviewed;         382 AA.
AC   I4DST9; I4DSU0; I4DSU1; I4DSU3;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2012, sequence version 1.
DT   25-MAY-2022, entry version 21.
DE   RecName: Full=Tuliposide A-converting enzyme 2, chloroplastic;
DE            Short=TgTCEA2;
DE            EC=4.2.99.22;
DE   Flags: Precursor;
GN   Name=TCEA2; Synonyms=TCEA3, TCEA4, TCEA6;
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 75-84; 93-104 AND 315-325,
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP   REGULATION, TISSUE SPECIFICITY, AND 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=14 mM for 6-tuliposide A {ECO:0000269|PubMed:22474185};
CC         KM=72 mM for 6-tuliposide B {ECO:0000269|PubMed:22474185};
CC         Note=kcat is 2400 sec(-1) with 6-tuliposide A as substrate. kcat is
CC         480 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 {ECO:0000250}.
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; AB569209; BAM20979.1; -; mRNA.
DR   EMBL; AB569210; BAM20980.1; -; mRNA.
DR   EMBL; AB569211; BAM20981.1; -; mRNA.
DR   EMBL; AB569213; BAM20983.1; -; mRNA.
DR   AlphaFoldDB; I4DST9; -.
DR   SMR; I4DST9; -.
DR   KEGG; ag:BAM20979; -.
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..74
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:22474185"
FT   CHAIN           75..382
FT                   /note="Tuliposide A-converting enzyme 2, chloroplastic"
FT                   /id="PRO_0000423866"
FT   ACT_SITE        232
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        324
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        356
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        28
FT                   /note="S -> P (in Ref. 1; BAM20980)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        104..116
FT                   /note="Missing (in Ref. 1; BAM20983)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        307
FT                   /note="I -> S (in Ref. 1; BAM20981)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   382 AA;  41140 MW;  958999F8A9787E5C CRC64;
     MSVASFFSSL PARPFGYKDG RGRTGMVSTT DIGRRMVKPP VLACRPIESN TYHGSVFLTK
     SSRSPSPSLS PTPTALDDEI VLDLKPFLII YKSGRIERFL GTTVIPACPE VATKDVVIDP
     ATGVSVRLYL PNVVDLPSKK LPVLVYFHGG GFVIENTGSP NYHNYLTLLA AKAGVLIVSI
     NYRLAPEYPL PASYDDCMAG FNWVVSHSAG PALEPWLAQH GDFSQILLSG DSAGGNVTHY
     VAMRADAGVI EGVAIVHPYF LGSEPVGNEI NDPANIEFHD KLWRLAAPDT EGLDDPLINP
     VAPGAPILAG LKCKRAVVFV AGNDFLVERG RMYYEALVKS GWGGEAELVQ HEGVGHVFHL
     SDYSGDISVA MMTKLIAFLK GE