CS_CATRO
ID CS_CATRO Reviewed; 330 AA.
AC A0A2P1GIW2;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2018, sequence version 1.
DT 03-AUG-2022, entry version 17.
DE RecName: Full=Catharanthine synthase {ECO:0000303|PubMed:29724909};
DE EC=4.-.-.- {ECO:0000269|PubMed:29511102, ECO:0000269|PubMed:29724909};
DE AltName: Full=Hydrolase 1 {ECO:0000303|PubMed:29511102};
DE Short=CrHL1 {ECO:0000303|PubMed:29511102};
GN Name=CS {ECO:0000303|PubMed:29724909};
GN Synonyms=HL1 {ECO:0000303|PubMed:29511102};
GN ORFNames=Caros025416 {ECO:0000305};
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 catharanthine.
CC {ECO:0000269|PubMed:29511102, ECO:0000269|PubMed:29724909}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dihydroprecondylocarpine acetate = acetate + catharanthine +
CC H(+); Xref=Rhea:RHEA:58580, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:142675, ChEBI:CHEBI:142770;
CC Evidence={ECO:0000269|PubMed:29511102, ECO:0000269|PubMed:29724909};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58581;
CC Evidence={ECO:0000269|PubMed:29511102, ECO:0000269|PubMed:29724909};
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:29511102}.
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:29724909, ECO:0000269|PubMed:30256480}.
CC -!- DISRUPTION PHENOTYPE: Reduced accumulation of catharanthine, increased
CC biosynthesis of vindoline, but normal levels of ajmalicine.
CC {ECO:0000269|PubMed:29511102, ECO:0000269|PubMed:29724909}.
CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=ORCAE database;
CC URL="https://bioinformatics.psb.ugent.be/orcae/overview/Catro";
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DR EMBL; MF770512; AVM85920.1; -; mRNA.
DR PDB; 6RT8; X-ray; 2.19 A; A/B/C/D/E/F/G/H=7-330.
DR PDBsum; 6RT8; -.
DR AlphaFoldDB; A0A2P1GIW2; -.
DR SMR; A0A2P1GIW2; -.
DR ESTHER; castro-TS; Plant_carboxylesterase.
DR BioCyc; MetaCyc:MON-20642; -.
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..330
FT /note="Catharanthine synthase"
FT /id="PRO_0000446422"
FT MOTIF 81..83
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 173
FT /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT ACT_SITE 274
FT /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:6RT8"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:6RT8"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:6RT8"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:6RT8"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:6RT8"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:6RT8"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:6RT8"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:6RT8"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:6RT8"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:6RT8"
FT HELIX 93..106
FT /evidence="ECO:0007829|PDB:6RT8"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:6RT8"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:6RT8"
FT HELIX 125..138
FT /evidence="ECO:0007829|PDB:6RT8"
FT TURN 139..142
FT /evidence="ECO:0007829|PDB:6RT8"
FT HELIX 156..161
FT /evidence="ECO:0007829|PDB:6RT8"
FT STRAND 162..172
FT /evidence="ECO:0007829|PDB:6RT8"
FT HELIX 174..189
FT /evidence="ECO:0007829|PDB:6RT8"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:6RT8"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:6RT8"
FT HELIX 217..230
FT /evidence="ECO:0007829|PDB:6RT8"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:6RT8"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:6RT8"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:6RT8"
FT STRAND 259..265
FT /evidence="ECO:0007829|PDB:6RT8"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:6RT8"
FT HELIX 277..289
FT /evidence="ECO:0007829|PDB:6RT8"
FT STRAND 294..300
FT /evidence="ECO:0007829|PDB:6RT8"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:6RT8"
FT HELIX 307..310
FT /evidence="ECO:0007829|PDB:6RT8"
FT HELIX 314..326
FT /evidence="ECO:0007829|PDB:6RT8"
SQ SEQUENCE 330 AA; 37132 MW; 543E34CBDE24EB9C CRC64;
MNSSTDPTSD ETIWDLSPYI KIFKDGRVER LHNSPYVPPS LNDPETGVSW KDVPISSQVS
ARVYIPKISD HEKLPIFVYV HGAGFCLESA FRSFFHTFVK HFVAETKVIG VSIEYRLAPE
HLLPAAYEDC WEALQWVASH VGLDNSGLKT AIDKDPWIIN YGDFDRLYLA GDSPGANIVH
NTLIRAGKEK LKGGVKILGA ILYYPYFIIP TSTKLSDDFE YNYTCYWKLA YPNAPGGMNN
PMINPIAENA PDLAGYGCSR LLVTLVSMIS TTPDETKDIN AVYIEALEKS GWKGELEVAD
FDADYFELFT LETEMGKNMF RRLASFIKHE
