ID   TCAB2_TULGE             Reviewed;         374 AA.
AC   R4X4V6; R4WVK6;
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 b2, amyloplastic;
DE            Short=TgTCEA-b2;
DE            EC=4.2.99.22;
DE   Flags: Precursor;
GN   Name=TCEA-B2; Synonyms=TCEA-B4, TCEA-B5;
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=14 mM for 6-tuliposide A {ECO:0000269|PubMed:23649245};
CC         KM=49 mM for 6-tuliposide B {ECO:0000269|PubMed:23649245};
CC         Note=kcat is 1700 sec(-1) with 6-tuliposide A as substrate. kcat is
CC         500 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; AB749807; BAN28566.1; -; mRNA.
DR   EMBL; AB749809; BAN28568.1; -; mRNA.
DR   EMBL; AB749810; BAN28569.1; -; mRNA.
DR   AlphaFoldDB; R4X4V6; -.
DR   SMR; R4X4V6; -.
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 b2, amyloplastic"
FT                   /id="PRO_0000423868"
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"
FT   CONFLICT        148
FT                   /note="I -> V (in Ref. 1; BAN28569)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   374 AA;  40499 MW;  56E68E9B9DF06593 CRC64;
     MSVALFCGPP PAVSFGCKDG RGRKGMVRSK DIVRQTVKPP AHACRLIGWN KYPGSVVPTN
     SSLSPSPTAL DDEIELDLSP 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