TS_CATRO
ID TS_CATRO Reviewed; 320 AA.
AC A0A2P1GIW3;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2018, sequence version 1.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=Tabersonine synthase {ECO:0000303|PubMed:29724909};
DE EC=4.-.-.- {ECO:0000269|PubMed:29511102, ECO:0000269|PubMed:29724909};
DE AltName: Full=Hydrolase 2 {ECO:0000303|PubMed:29511102};
DE Short=CrHL2 {ECO:0000303|PubMed:29511102};
GN Name=TS {ECO:0000303|PubMed:29724909};
GN Synonyms=HL2 {ECO:0000303|PubMed:29511102};
OS Catharanthus roseus (Madagascar periwinkle) (Vinca rosea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae; Vinceae;
OC Catharanthinae; Catharanthus.
OX NCBI_TaxID=4058;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC
RP ACTIVITY, AND PATHWAY.
RX PubMed=29511102; DOI=10.1073/pnas.1719979115;
RA Qu Y., Easson M.E.A.M., Simionescu R., Hajicek J., Thamm A.M.K., Salim V.,
RA De Luca V.;
RT "Solution of the multistep pathway for assembly of corynanthean, strychnos,
RT iboga, and aspidosperma monoterpenoid indole alkaloids from 19E-
RT geissoschizine.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:3180-3185(2018).
RN [2]
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Little Delicata;
RX PubMed=30256480; DOI=10.1111/tpj.14111;
RA Qu Y., Safonova O., De Luca V.;
RT "Completion of the canonical pathway for assembly of anticancer drugs
RT vincristine/vinblastine in Catharanthus roseus.";
RL Plant J. 97:257-266(2019).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, INTERACTION WITH DPAS,
RP SUBCELLULAR LOCATION, AND PATHWAY.
RC STRAIN=cv. Little Bright Eyes;
RX PubMed=29724909; DOI=10.1126/science.aat4100;
RA Caputi L., Franke J., Farrow S.C., Chung K., Payne R.M.E., Nguyen T.-D.,
RA Dang T.-T.T., Soares Teto Carqueijeiro I., Koudounas K.,
RA Duge de Bernonville T., Ameyaw B., Jones D.M., Vieira I.J.C.,
RA Courdavault V., O'Connor S.E.;
RT "Missing enzymes in the biosynthesis of the anticancer drug vinblastine in
RT Madagascar periwinkle.";
RL Science 360:1235-1239(2018).
CC -!- FUNCTION: Component of iboga and aspidosperma monoterpenoid indole
CC alkaloids (MIAs, e.g. tabersonine and catharanthine) biosynthesis
CC pathway from 19E-geissoschizine. Catalyzes the conversion of O-
CC acetylstemmadenine (OAS) to tabersonine, a precursor of vindoline.
CC {ECO:0000269|PubMed:29511102, ECO:0000269|PubMed:29724909}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dihydroprecondylocarpine acetate = (-)-tabersonine + acetate +
CC H(+); Xref=Rhea:RHEA:58584, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:57893, ChEBI:CHEBI:142770;
CC Evidence={ECO:0000269|PubMed:29511102, ECO:0000269|PubMed:29724909};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58585;
CC Evidence={ECO:0000269|PubMed:29511102, ECO:0000269|PubMed:29724909};
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:29511102,
CC ECO:0000269|PubMed:29724909}.
CC -!- SUBUNIT: Interacts with dehydroprecondylocarpine acetate synthase
CC (DPAS). {ECO:0000269|PubMed:29724909}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:29724909}.
CC Nucleus {ECO:0000269|PubMed:29724909}.
CC -!- TISSUE SPECIFICITY: Expressed in leaf epidermis.
CC {ECO:0000269|PubMed:30256480}.
CC -!- DISRUPTION PHENOTYPE: Reduced accumulation of vindoline and
CC tabersonine, increased biosynthesis of catharanthine, but normal levels
CC of ajmalicine. {ECO:0000269|PubMed:29511102,
CC ECO:0000269|PubMed:29724909}.
CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC {ECO:0000305}.
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DR EMBL; MF770513; AVM85921.1; -; mRNA.
DR PDB; 6RS4; X-ray; 1.30 A; A/B=2-320.
DR PDBsum; 6RS4; -.
DR AlphaFoldDB; A0A2P1GIW3; -.
DR SMR; A0A2P1GIW3; -.
DR ESTHER; castro-CS; Plant_carboxylesterase.
DR BioCyc; MetaCyc:MON-20643; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0009820; P:alkaloid metabolic process; 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 3D-structure; Alkaloid metabolism; Cytoplasm; Lyase; Nucleus.
FT CHAIN 1..320
FT /note="Tabersonine synthase"
FT /id="PRO_0000446423"
FT MOTIF 78..80
FT /note="Involved in the stabilization of the negatively
FT charged intermediate by the formation of the oxyanion hole"
FT /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT ACT_SITE 170
FT /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT ACT_SITE 266
FT /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:6RS4"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:6RS4"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:6RS4"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:6RS4"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:6RS4"
FT TURN 39..42
FT /evidence="ECO:0007829|PDB:6RS4"
FT STRAND 45..54
FT /evidence="ECO:0007829|PDB:6RS4"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:6RS4"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:6RS4"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:6RS4"
FT HELIX 90..103
FT /evidence="ECO:0007829|PDB:6RS4"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:6RS4"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:6RS4"
FT HELIX 122..135
FT /evidence="ECO:0007829|PDB:6RS4"
FT TURN 136..139
FT /evidence="ECO:0007829|PDB:6RS4"
FT HELIX 142..146
FT /evidence="ECO:0007829|PDB:6RS4"
FT HELIX 153..158
FT /evidence="ECO:0007829|PDB:6RS4"
FT STRAND 159..169
FT /evidence="ECO:0007829|PDB:6RS4"
FT HELIX 170..183
FT /evidence="ECO:0007829|PDB:6RS4"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:6RS4"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:6RS4"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:6RS4"
FT HELIX 220..228
FT /evidence="ECO:0007829|PDB:6RS4"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:6RS4"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:6RS4"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:6RS4"
FT STRAND 257..263
FT /evidence="ECO:0007829|PDB:6RS4"
FT HELIX 268..282
FT /evidence="ECO:0007829|PDB:6RS4"
FT STRAND 286..292
FT /evidence="ECO:0007829|PDB:6RS4"
FT HELIX 297..301
FT /evidence="ECO:0007829|PDB:6RS4"
FT HELIX 306..316
FT /evidence="ECO:0007829|PDB:6RS4"
SQ SEQUENCE 320 AA; 36192 MW; 43DBC4548F045B04 CRC64;
MGSSDETIFD LPPYIKVFKD GRVERLHSSP YVPPSLNDPE TGGVSWKDVP ISSVVSARIY
LPKINNHDEK LPIIVYFHGA GFCLESAFKS FFHTYVKHFV AEAKAIAVSV EFRLAPENHL
PAAYEDCWEA LQWVASHVGL DISSLKTCID KDPWIINYAD FDRLYLWGDS TGANIVHNTL
IRSGKEKLNG GKVKILGAIL YYPYFLIRTS SKQSDYMENE YRSYWKLAYP DAPGGNDNPM
INPTAENAPD LAGYGCSRLL ISMVADEARD ITLLYIDALE KSGWKGELDV ADFDKQYFEL
FEMETEVAKN MLRRLASFIK
