ID   TCEB1_TULGE             Reviewed;         440 AA.
AC   A0A0H5BMX5;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2015, sequence version 1.
DT   25-MAY-2022, entry version 17.
DE   RecName: Full=Tuliposide B-converting enzyme 1, amyloplastic {ECO:0000303|PubMed:25997073};
DE            Short=TgTCEB1 {ECO:0000303|PubMed:25997073};
DE            EC=4.2.99.23 {ECO:0000269|PubMed:25997073};
DE   Flags: Precursor;
GN   Name=TCEB1 {ECO:0000303|PubMed:25997073};
OS   Tulipa gesneriana (Garden tulip).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Liliales; Liliaceae; Tulipa.
OX   NCBI_TaxID=13306 {ECO:0000312|EMBL:BAR97239.1};
RN   [1] {ECO:0000312|EMBL:BAR97239.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 59-71; 87-96; 220-231 AND
RP   344-353, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP   SUBCELLULAR LOCATION, LACK OF GLYCOSYLATION, ACTIVITY REGULATION, AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=Pollen {ECO:0000312|EMBL:BAR97239.1};
RX   PubMed=25997073; DOI=10.1111/tpj.12883;
RA   Nomura T., Murase T., Ogita S., Kato Y.;
RT   "Molecular identification of tuliposide B-converting enzyme: a lactone-
RT   forming carboxylesterase from the pollen of tulip.";
RL   Plant J. 83:252-262(2015).
CC   -!- FUNCTION: Lactone-forming carboxylesterase, 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 B > 6-tuliposide A.
CC       {ECO:0000269|PubMed:25997073}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-tuliposide B = D-glucose + tulipalin B;
CC         Xref=Rhea:RHEA:38655, ChEBI:CHEBI:4167, ChEBI:CHEBI:87123,
CC         ChEBI:CHEBI:87124; EC=4.2.99.23;
CC         Evidence={ECO:0000269|PubMed:25997073};
CC   -!- ACTIVITY REGULATION: Inhibited by Ag(+), Cu(2+), Fe(2+), Hg(2+), V(3+)
CC       and phenylmethylsulfonyl fluoride (PMSF).
CC       {ECO:0000269|PubMed:25997073}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3.0 mM for 6-tuliposide A {ECO:0000269|PubMed:25997073};
CC         KM=6.8 mM for 6-tuliposide B {ECO:0000269|PubMed:25997073};
CC         Note=kcat is 8.7 sec(-1) with 6-tuliposide A as substrate. kcat is
CC         2000 sec(-1) with 6-tuliposide B as substrate.
CC         {ECO:0000269|PubMed:25997073};
CC       pH dependence:
CC         Optimum pH is 7.0-7.5. {ECO:0000269|PubMed:25997073};
CC       Temperature dependence:
CC         Optimum temperature is 30-40 degrees Celsius.
CC         {ECO:0000269|PubMed:25997073};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:25997073}.
CC   -!- SUBCELLULAR LOCATION: Plastid {ECO:0000269|PubMed:25997073}. Plastid,
CC       amyloplast {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in the pollen grains.
CC       {ECO:0000269|PubMed:25997073}.
CC   -!- PTM: Not glycosylated. {ECO:0000269|PubMed:25997073}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR   EMBL; AB828597; BAR97239.1; -; mRNA.
DR   EMBL; AB829723; BAR97240.1; -; mRNA.
DR   AlphaFoldDB; A0A0H5BMX5; -.
DR   SMR; A0A0H5BMX5; -.
DR   ESTHER; tulge-a0a0h5bmx5; Plant_carboxylesterase.
DR   KEGG; ag:BAR97239; -.
DR   GO; GO:0009501; C:amyloplast; 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   InterPro; IPR033140; Lipase_GDXG_put_SER_AS.
DR   Pfam; PF07859; Abhydrolase_3; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS01174; LIPASE_GDXG_SER; 1.
PE   1: Evidence at protein level;
KW   Amyloplast; Direct protein sequencing; Lyase; Plant defense; Plastid;
KW   Transit peptide.
FT   TRANSIT         1..58
FT                   /note="Amyloplast"
FT                   /evidence="ECO:0000269|PubMed:25997073"
FT   CHAIN           59..440
FT                   /note="Tuliposide B-converting enzyme 1, amyloplastic"
FT                   /id="PRO_0000440619"
FT   ACT_SITE        232
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:I4DST8"
FT   ACT_SITE        325
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:I4DST8"
FT   ACT_SITE        357
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:I4DST8"
SQ   SEQUENCE   440 AA;  49023 MW;  A29DAFA3C0E567B7 CRC64;
     MSIVSFCSSL PAGPHGFKHG RGTRDMVHMP CIVRRTARSP AQACRLLRWN KYHCAAVPTN
     SSLSPSPTPL DVEIELDLEP FLIKYKSGRI ERLGRFGDRT DYVEASLDPA TEVTSRDAIT
     DTGVPVRIYL PKVDDSPPNS LRVLVYFHGG AFLVEDSASP PYHNYLNNLA SKANILIVSV
     NYRLAPEYPL PVAYDDCMEA LNWVNKHSDG TGQEDWINKH GDFDHLFISG DSAGGNITHN
     IAMSTDAPKN IEGIALVHPY FFGKVALETE LQDPTNLLLH RKLWSFITPE SEGLDDPRVN
     PLGPTAPSLE KIKCKRAVVF VAGEDFHSER GRKYSEKLKS EFKGEVPLLC NHDGVGHVYH
     LSVDATEEEI ESAAAWKMMT DLLKFYKDND VVLEGSIVES LKAKTTEGIK KMKEIEKGMS
     ERMMEQLVAF YNGKPVPYSS