ID   A0A2I0XHX2_9ASPA        Unreviewed;       352 AA.
AC   A0A2I0XHX2;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=tuliposide A-converting enzyme {ECO:0000256|ARBA:ARBA00039093};
DE            EC=4.2.99.22 {ECO:0000256|ARBA:ARBA00039093};
GN   Name=CXE2 {ECO:0000313|EMBL:PKU87505.1};
GN   ORFNames=MA16_Dca016692 {ECO:0000313|EMBL:PKU87505.1};
OS   Dendrobium catenatum.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC   Epidendroideae; Malaxideae; Dendrobiinae; Dendrobium.
OX   NCBI_TaxID=906689 {ECO:0000313|EMBL:PKU87505.1, ECO:0000313|Proteomes:UP000233837};
RN   [1] {ECO:0000313|EMBL:PKU87505.1, ECO:0000313|Proteomes:UP000233837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=The whole plant {ECO:0000313|EMBL:PKU87505.1};
RX   PubMed=26754549; DOI=10.1038/srep19029;
RA   Zhang G.Q., Xu Q., Bian C., Tsai W.C., Yeh C.M., Liu K.W., Yoshida K.,
RA   Zhang L.S., Chang S.B., Chen F., Shi Y., Su Y.Y., Zhang Y.Q., Chen L.J.,
RA   Yin Y., Lin M., Huang H., Deng H., Wang Z.W., Zhu S.L., Zhao X., Deng C.,
RA   Niu S.C., Huang J., Wang M., Liu G.H., Yang H.J., Xiao X.J., Hsiao Y.Y.,
RA   Wu W.L., Chen Y.Y., Mitsuda N., Ohme-Takagi M., Luo Y.B., Van de Peer Y.,
RA   Liu Z.J.;
RT   "The Dendrobium catenatum Lindl. genome sequence provides insights into
RT   polysaccharide synthase, floral development and adaptive evolution.";
RL   Sci. Rep. 6:19029-19029(2016).
RN   [2] {ECO:0000313|EMBL:PKU87505.1, ECO:0000313|Proteomes:UP000233837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=The whole plant {ECO:0000313|EMBL:PKU87505.1};
RX   PubMed=28902843; DOI=10.1038/nature23897;
RA   Zhang G.Q., Liu K.W., Li Z., Lohaus R., Hsiao Y.Y., Niu S.C., Wang J.Y.,
RA   Lin Y.C., Xu Q., Chen L.J., Yoshida K., Fujiwara S., Wang Z.W., Zhang Y.Q.,
RA   Mitsuda N., Wang M., Liu G.H., Pecoraro L., Huang H.X., Xiao X.J., Lin M.,
RA   Wu X.Y., Wu W.L., Chen Y.Y., Chang S.B., Sakamoto S., Ohme-Takagi M.,
RA   Yagi M., Zeng S.J., Shen C.Y., Yeh C.M., Luo Y.B., Tsai W.C.,
RA   Van de Peer Y., Liu Z.J.;
RT   "The Apostasia genome and the evolution of orchids.";
RL   Nature 549:379-383(2017).
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:0000256|ARBA:ARBA00037719}.
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:0000256|ARBA:ARBA00035823};
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DR   EMBL; KZ501874; PKU87505.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I0XHX2; -.
DR   STRING; 906689.A0A2I0XHX2; -.
DR   Proteomes; UP000233837; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013094; AB_hydrolase_3.
DR   PANTHER; PTHR23024; ARYLACETAMIDE DEACETYLASE; 1.
DR   PANTHER; PTHR23024:SF435; OS06G0214300 PROTEIN; 1.
DR   Pfam; PF07859; Abhydrolase_3; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000233837}.
FT   DOMAIN          113..329
FT                   /note="Alpha/beta hydrolase fold-3"
FT                   /evidence="ECO:0000259|Pfam:PF07859"
SQ   SEQUENCE   352 AA;  38816 MW;  0FD4B9F32B793DC7 CRC64;
     MPLASTSYPH LIGAQYSQFL ASSKFQPSSE TMNSSAASFD SDDVVFQLPG SIRLYRSGRV
     ERIYRDELVP PSLDPTTGVQ SKDVTINPTT NLSARLYLPP SATSIPKKLP VFLTIHGGGF
     CLFRSSSSIY HSYVNSLTAK AGILSVSVDY RLAPENPLPA AYDDCWEALE WVFAAEDPWL
     SNFGDLERVF IGGESAGGNI VHNLGIRLGG EGKKVEGLVM IHSFFWGKDR IGNEGVESGK
     KESLKAEDID ALWLTVCPET TGLDDPRINP VVEGAPSLAT LGCRRVLVCV AELDILRERG
     RVYFEKLKES GWEGEAEFLE SEGEDHCFFF MKPGSLKAEE FMERMVSFFN KS
//