ID   SALAT_PAPSO             Reviewed;         474 AA.
AC   Q94FT4;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Salutaridinol 7-O-acetyltransferase {ECO:0000303|PubMed:11404355};
DE            Short=salAT {ECO:0000303|PubMed:11404355};
DE            EC=2.3.1.150 {ECO:0000269|PubMed:11404355, ECO:0000269|PubMed:8537369};
GN   Name=SALAT {ECO:0000303|PubMed:11404355};
OS   Papaver somniferum (Opium poppy).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC   Papaver.
OX   NCBI_TaxID=3469;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 14-30; 241-244; 257-272;
RP   287-313; 340-362 AND 378-394, FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX   PubMed=11404355; DOI=10.1074/jbc.m102688200;
RA   Grothe T., Lenz R., Kutchan T.M.;
RT   "Molecular characterization of the salutaridinol 7-O-acetyltransferase
RT   involved in morphine biosynthesis in Opium poppy Papaver somniferum.";
RL   J. Biol. Chem. 276:30717-30723(2001).
RN   [2]
RP   CATALYTIC ACTIVITY.
RX   PubMed=8537369; DOI=10.1074/jbc.270.52.31091;
RA   Lenz R., Zenk M.H.;
RT   "Acetyl coenzyme A:salutaridinol-7-O-acetyltransferase from Papaver
RT   somniferum plant cell cultures. The enzyme catalyzing the formation of
RT   thebaine in morphine biosynthesis.";
RL   J. Biol. Chem. 270:31091-31096(1995).
RN   [3]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=cv. Marianne;
RX   PubMed=16813579; DOI=10.1111/j.1365-313x.2006.02801.x;
RA   Samanani N., Alcantara J., Bourgault R., Zulak K.G., Facchini P.J.;
RT   "The role of phloem sieve elements and laticifers in the biosynthesis and
RT   accumulation of alkaloids in opium poppy.";
RL   Plant J. 47:547-563(2006).
CC   -!- FUNCTION: Involved in biosynthesis of morphinan-type benzylisoquinoline
CC       alkaloids. Catalyzes the conversion of the phenanthrene alkaloid
CC       salutaridinol to salutaridinol-7-O-acetate, the immediate precursor of
CC       thebaine along the morphine biosynthetic pathway. Conversion of 7-O-
CC       acetylsalutaridinol into thebaine is spontaneous.
CC       {ECO:0000269|PubMed:11404355}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(7S)-salutaridinol + acetyl-CoA = (7S)-O-acetylsalutaridinol +
CC         CoA; Xref=Rhea:RHEA:22856, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:57672, ChEBI:CHEBI:58463; EC=2.3.1.150;
CC         Evidence={ECO:0000269|PubMed:11404355, ECO:0000269|PubMed:8537369};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=9 uM for salutaridinol {ECO:0000269|PubMed:11404355};
CC         KM=54 uM for acetyl-CoA {ECO:0000269|PubMed:11404355};
CC         Vmax=25 pmol/sec/mg enzyme {ECO:0000269|PubMed:11404355};
CC       pH dependence:
CC         Optimum pH is 7-9. {ECO:0000269|PubMed:11404355};
CC       Temperature dependence:
CC         Optimum temperature is 47 degrees Celsius.
CC         {ECO:0000269|PubMed:11404355};
CC   -!- PATHWAY: Alkaloid biosynthesis; morphine biosynthesis.
CC   -!- TISSUE SPECIFICITY: Expressed in root, stem, leaf and capsule of the
CC       mature plant (PubMed:11404355, PubMed:16813579). Restricted to sieve
CC       elements of the phloem adjacent or proximal to laticifers
CC       (PubMed:16813579). {ECO:0000269|PubMed:11404355,
CC       ECO:0000269|PubMed:16813579}.
CC   -!- DEVELOPMENTAL STAGE: Increases rapidly between 1 and 3 days after seed
CC       germination. {ECO:0000269|PubMed:16813579}.
CC   -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
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DR   EMBL; AF339913; AAK73661.1; -; mRNA.
DR   AlphaFoldDB; Q94FT4; -.
DR   SMR; Q94FT4; -.
DR   KEGG; ag:AAK73661; -.
DR   BioCyc; MetaCyc:MON-12301; -.
DR   BRENDA; 2.3.1.150; 4515.
DR   UniPathway; UPA00852; -.
DR   PRO; PR:Q94FT4; -.
DR   GO; GO:0047180; F:salutaridinol 7-O-acetyltransferase activity; IEA:UniProtKB-EC.
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; Direct protein sequencing;
KW   Transferase.
FT   CHAIN           1..474
FT                   /note="Salutaridinol 7-O-acetyltransferase"
FT                   /id="PRO_0000147366"
FT   REGION          213..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..228
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        163
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        416
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   474 AA;  52632 MW;  3A467FEE8B6A155E CRC64;
     MATMYSAAVE VISKETIKPT TPTPSQLKNF NLSLLDQCFP LYYYVPIILF YPATAANSTG
     SSNHHDDLDL LKSSLSKTLV HFYPMAGRMI DNILVDCHDQ GINFYKVKIR GKMCEFMSQP
     DVPLSQLLPS EVVSASVPKE ALVIVQVNMF DCGGTAICSS VSHKIADAAT MSTFIRSWAS
     TTKTSRSGGS TAAVTDQKLI PSFDSASLFP PSERLTSPSG MSEIPFSSTP EDTEDDKTVS
     KRFVFDFAKI TSVREKLQVL MHDNYKSRRQ TRVEVVTSLI WKSVMKSTPA GFLPVVHHAV
     NLRKKMDPPL QDVSFGNLSV TVSAFLPATT TTTTNAVNKT INSTSSESQV VLHELHDFIA
     QMRSEIDKVK GDKGSLEKVI QNFASGHDAS IKKINDVEVI NFWISSWCRM GLYEIDFGWG
     KPIWVTVDPN IKPNKNCFFM NDTKCGEGIE VWASFLEDDM AKFELHLSEI LELI