ID   SAT_CATRO               Reviewed;         421 AA.
AC   A0A2P1GIW7;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   23-MAY-2018, sequence version 1.
DT   03-AUG-2022, entry version 14.
DE   RecName: Full=Stemmadenine O-acetyltransferase {ECO:0000303|PubMed:29511102};
DE            Short=CrSAT {ECO:0000303|PubMed:29511102};
DE            EC=1.7.1.- {ECO:0000269|PubMed:29511102};
GN   Name=SAT {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).
CC   -!- FUNCTION: Component of iboga and aspidosperma monoterpenoid indole
CC       alkaloids (MIAs, e.g. tabersonine and catharanthine) biosynthesis
CC       pathway from 19E-geissoschizine. Acetyltransferase that catalyzes the
CC       formation of O-acetylstemmadenine from stemmadenine.
CC       {ECO:0000269|PubMed:29511102}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=15alpha-stemmadenine + acetyl-CoA = CoA + O-acetyl-15alpha-
CC         stemmadenine; Xref=Rhea:RHEA:58568, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:142673, ChEBI:CHEBI:142674;
CC         Evidence={ECO:0000269|PubMed:29511102};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58569;
CC         Evidence={ECO:0000269|PubMed:29511102};
CC   -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:29511102}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q70PR7}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaf epidermis.
CC       {ECO:0000269|PubMed:30256480}.
CC   -!- DISRUPTION PHENOTYPE: Abnormal presence of stemmadenine, but normal
CC       accumulation of catharanthine and vindoline.
CC       {ECO:0000269|PubMed:29511102}.
CC   -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
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DR   EMBL; MF770511; AVM85919.1; -; mRNA.
DR   AlphaFoldDB; A0A2P1GIW7; -.
DR   SMR; A0A2P1GIW7; -.
DR   BioCyc; MetaCyc:MON-20644; -.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; -; 2.
DR   InterPro; IPR023213; CAT-like_dom_sf.
PE   1: Evidence at protein level;
KW   Acyltransferase; Alkaloid metabolism; Oxidoreductase; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q70PR7"
FT   CHAIN           2..421
FT                   /note="Stemmadenine O-acetyltransferase"
FT                   /id="PRO_0000446427"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        160
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q70PR7"
FT   ACT_SITE        362
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q70PR7"
SQ   SEQUENCE   421 AA;  47005 MW;  1F507D8503378534 CRC64;
     MAPQMQILSE ELIQPSSPTP QTLKTHKLSH LDQVLLTCHI PIILFYPNQL DSNLDRAQRS
     ENLKRSLSTV LTQFYPLAGR ININSSVDCN DSGVPFLEAR VHSQLSEAIK NVAIDELNQY
     LPFQPYPGGE ESGLKKDIPL AVKISCFECG GTAIGVCISH KIADALSLAT FLNSWTATCQ
     EETDIVQPNF DLGSHHFPPM ESIPAPEFLP DENIVMKRFV FDKEKLEALK AQLASSATEV
     KNSSRVQIVI AVIWKQFIDV TRAKFDTKNK LVAAQAVNLR SRMNPPFPQS AMGNIATMAY
     AVAEEDKDFS DLVGPLKTSL AKIDDEHVKE LQKGVTYLDY EAEPQELFSF SSWCRLGFYD
     LDFGWGKPVS VCTTTVPMKN LVYLMDTRNE DGMEAWISMA EDEMSMLSSD FLSLLDTDFS
     N