ID   HL3_CATRO               Reviewed;         321 AA.
AC   A0A2P1GIY2;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   23-MAY-2018, sequence version 1.
DT   25-MAY-2022, entry version 10.
DE   RecName: Full=Hydrolase 3 {ECO:0000303|PubMed:29511102};
DE            Short=CrHL3 {ECO:0000303|PubMed:29511102};
DE            EC=4.-.-.- {ECO:0000269|PubMed:30256480};
GN   Name=HL3 {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].
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   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
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).
CC   -!- FUNCTION: Component of the seco-iridoid and derivatives monoterpenoid
CC       indole alkaloids (MIAs, e.g. vincadifformine) biosynthesis pathway.
CC       Catalyzes the conversion of O-acetylstemmadenine (OAS) to
CC       vincadifformine. May also trigger the formation of additional unknown
CC       MIAs. {ECO:0000269|PubMed:30256480}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dihydroprecondylocarpine acetate + NADPH = (+)-vincadifformine
CC         + acetate + NADP(+); Xref=Rhea:RHEA:58588, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:142770,
CC         ChEBI:CHEBI:142830; Evidence={ECO:0000269|PubMed:30256480};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58589;
CC         Evidence={ECO:0000269|PubMed:30256480};
CC   -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:30256480}.
CC   -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; MF770514; AVM85922.1; -; mRNA.
DR   AlphaFoldDB; A0A2P1GIY2; -.
DR   SMR; A0A2P1GIY2; -.
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   Alkaloid metabolism; Lyase.
FT   CHAIN           1..321
FT                   /note="Hydrolase 3"
FT                   /id="PRO_0000446424"
FT   MOTIF           80..82
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        172
FT                   /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT   ACT_SITE        267
FT                   /evidence="ECO:0000250|UniProtKB:Q5NUF3"
SQ   SEQUENCE   321 AA;  36436 MW;  06238125C5947531 CRC64;
     MASSDETIFD LPPYIRVFKD GRVERLHSSP YVPPSLNDPE TGVSWKDVPI SSKVSARIYL
     PKISDQQENE EKLPIFVYFH GAGFCLESAF RSFFHTFIKH FVSEAKAIGV SVEYRLAPEH
     PLPAAYEDCW EALQWVASHV RLDNSSLKRS MDKDPWIINY GDFDRLYLGG DSPGGNIVHN
     VLLRAGKEKL NGGVKILGAI QYYPYFLIRT SSKQSDYMEN DYRCYWKLAY PNAPGGTDNP
     MINPTVENAP DLAGYGCSRL LISMVADETR DITLLFIEAL KKSGWKGQLD VADFEAEFFD
     LFQTQTEVGK NMIRRLTSFI K