ID   TCAB4_TULGE             Reviewed;         374 AA.
AC   R4X247;
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=Probable tuliposide A-converting enzyme b6, amyloplastic;
DE            Short=TgTCEA-b6;
DE            EC=4.2.99.22;
DE   Flags: Precursor;
GN   Name=TCEA-B6;
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].
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 (By similarity).
CC       {ECO:0000250}.
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, amyloplast {ECO:0000250}.
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:0000250}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
CC   -!- CAUTION: No genomic clone corresponding to this cDNA could be found.
CC       {ECO:0000305}.
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DR   EMBL; AB749811; BAN28570.1; -; mRNA.
DR   AlphaFoldDB; R4X247; -.
DR   SMR; R4X247; -.
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   2: Evidence at transcript level;
KW   Amyloplast; Lyase; Plant defense; Plastid; Transit peptide.
FT   TRANSIT         1..68
FT                   /note="Amyloplast"
FT                   /evidence="ECO:0000250"
FT   CHAIN           69..374
FT                   /note="Probable tuliposide A-converting enzyme b6,
FT                   amyloplastic"
FT                   /id="PRO_0000423870"
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;  40482 MW;  3C21E32B8E6B082A CRC64;
     MSVALFCGPP PAVSFGCKDG RGRKGMVRSK DIVRQTVKPP AHACRLIGWN KYPGSVVPTN
     SSLSPSPTAL DDEIELDPSP FLIIYKDGRI ERLKGTTVIP ACPEVATKDV IIDPATGVSV
     RLYLPNVVDL PSKKLPVLVY FHGGGFVIEN TGSPNYHNYL TLLAAKSGLL IVSVNYRLAP
     EHPIPASFDD CMAGFNWVVS HSAGPAPEPW LARHGDLTQI LISGDSAGGT VTHYVLLRAD
     AGVIEGAALV HPYFLGSKRL ENQTEEDFEF HEKLWRLSTP DTEGLDDPLI NPLAPGAPSL
     AGLKCKRAVV FVAELDFLVE RGRMYYDALV KSGWGGEAEL VHQKGVGHVF HLSDYSGDVS
     VDMMAKMVAF LRGE