ID   TCAB3_TULGE             Reviewed;         374 AA.
AC   R4X5P0;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2013, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=Tuliposide A-converting enzyme b3, amyloplastic;
DE            Short=TgTCEA-b3;
DE            EC=4.2.99.22;
DE   Flags: Precursor;
GN   Name=TCEA-B3;
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 [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF N-TERMINUS,
RP   SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC   TISSUE=Bulb;
RX   PubMed=23649245; DOI=10.1271/bbb.130021;
RA   Nomura T., Tsuchigami A., Ogita S., Kato Y.;
RT   "Molecular diversity of tuliposide A-converting enzyme in the tulip.";
RL   Biosci. Biotechnol. Biochem. 77:1042-1048(2013).
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   -!- 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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=21 mM for 6-tuliposide A {ECO:0000269|PubMed:23649245};
CC         KM=51 mM for 6-tuliposide B {ECO:0000269|PubMed:23649245};
CC         Note=kcat is 3200sec(-1) with 6-tuliposide A as substrate. kcat is
CC         720 sec(-1) with 6-tuliposide B as substrate.;
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:23649245}.
CC   -!- SUBCELLULAR LOCATION: Plastid, amyloplast {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in pistil and bulb scales. Lower
CC       expression in stem, and barely detected in root, leaf, petal and
CC       stamen. {ECO:0000269|PubMed:23649245}.
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:23649245}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR   EMBL; AB749808; BAN28567.1; -; mRNA.
DR   AlphaFoldDB; R4X5P0; -.
DR   SMR; R4X5P0; -.
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   Pfam; PF07859; Abhydrolase_3; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Amyloplast; Direct protein sequencing; Lyase; Plant defense; Plastid;
KW   Transit peptide.
FT   TRANSIT         1..68
FT                   /note="Amyloplast"
FT                   /evidence="ECO:0000269|PubMed:23649245"
FT   CHAIN           69..374
FT                   /note="Tuliposide A-converting enzyme b3, amyloplastic"
FT                   /id="PRO_0000423869"
FT   ACT_SITE        226
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        316
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        348
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   374 AA;  40456 MW;  A4EA8C43AF17FC8C CRC64;
     MSAALFCGPP PAVSFGCKDG RGRKGMVRSK DIVRQTVKPP AHACRLIGWN KYPGSVVPTN
     SSLSPSPTAL DDDIELDLSP FLIIYKDGRI ERLKGTTVIP ACPEVATKDV IIDPATGVSV
     RLYLPNVVDL PSKKLPVLVY FHGGGFVIEN TGSPNYHNYL TLLAAKSGLL IVSVNYRLAP
     EHPIPASFDD CMAGFNWVVS HSAGPAPEPW LARHGDLTQI LISGDSAGGT VTHYVLLRAD
     AGVIEGAALV HPYFLGSKRL ENQTEEDFEF HEKLWRLSTP NTEGLDDPLI NPLAPGAPSL
     AGLKCKRAVV FVAELDFLVE RGRMYYDALV KSGWGGEAEL VHQEGVGHVF HLSDYSGDVS
     VDMMAKMVAF LRGE