AT1_PAPSO
ID AT1_PAPSO Reviewed; 471 AA.
AC I3PLR4;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=(13S,14R)-1,13-dihydroxy-N-methylcanadine 13-O-acetyltransferase AT1 {ECO:0000305};
DE EC=2.3.1.285 {ECO:0000269|PubMed:25485687, ECO:0000269|PubMed:27378283};
DE AltName: Full=Acetyltransferase 1 {ECO:0000303|PubMed:22653730};
DE Short=PsAT1 {ECO:0000303|PubMed:27378283};
GN Name=AT1 {ECO:0000303|PubMed:22653730};
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 [GENOMIC DNA].
RX PubMed=22653730; DOI=10.1126/science.1220757;
RA Winzer T., Gazda V., He Z., Kaminski F., Kern M., Larson T.R., Li Y.,
RA Meade F., Teodor R., Vaistij F.E., Walker C., Bowser T.A., Graham I.A.;
RT "A Papaver somniferum 10-gene cluster for synthesis of the anticancer
RT alkaloid noscapine.";
RL Science 336:1704-1708(2012).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=25485687; DOI=10.1038/nchembio.1717;
RA Dang T.T., Chen X., Facchini P.J.;
RT "Acetylation serves as a protective group in noscapine biosynthesis in
RT opium poppy.";
RL Nat. Chem. Biol. 11:104-106(2015).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=27378283; DOI=10.1038/ncomms12137;
RA Li Y., Smolke C.D.;
RT "Engineering biosynthesis of the anticancer alkaloid noscapine in yeast.";
RL Nat. Commun. 7:12137-12137(2016).
RN [4]
RP FUNCTION.
RX PubMed=29610307; DOI=10.1073/pnas.1721469115;
RA Li Y., Li S., Thodey K., Trenchard I., Cravens A., Smolke C.D.;
RT "Complete biosynthesis of noscapine and halogenated alkaloids in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E3922-E3931(2018).
CC -!- FUNCTION: Acetyltransferase involved in the biosynthesis of the
CC benzylisoquinoline alkaloid noscapine (PubMed:25485687,
CC PubMed:27378283, PubMed:29610307). Converts (13S,14R)-1,13-dihydroxy-N-
CC methylcanadine to (13S,14R)-13-O-acetyl-1-hydroxy-N-methylcanadine
CC (PubMed:25485687, PubMed:27378283). {ECO:0000269|PubMed:25485687,
CC ECO:0000269|PubMed:27378283, ECO:0000269|PubMed:29610307}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(13S,14R)-1,13-dihydroxy-N-methylcanadine + acetyl-CoA =
CC (13S,14R)-13-O-acetyl-1-hydroxy-N-methylcanadine + CoA;
CC Xref=Rhea:RHEA:57384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:141639, ChEBI:CHEBI:141640; EC=2.3.1.285;
CC Evidence={ECO:0000269|PubMed:25485687, ECO:0000269|PubMed:27378283};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57385;
CC Evidence={ECO:0000305|PubMed:25485687};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=16.5 uM for (13S,14R)-1,13-dihydroxy-N-methylcanadine
CC {ECO:0000269|PubMed:25485687};
CC KM=35.3 uM for acetyl-CoA {ECO:0000269|PubMed:25485687};
CC Vmax=152 nmol/min/mg enzyme with (13S,14R)-1,13-dihydroxy-N-
CC methylcanadine as substrate {ECO:0000269|PubMed:25485687};
CC Vmax=324 nmol/min/mg enzyme with acetyl-CoA as substrate
CC {ECO:0000269|PubMed:25485687};
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JQ659008; AFB74620.1; -; Genomic_DNA.
DR AlphaFoldDB; I3PLR4; -.
DR SMR; I3PLR4; -.
DR EnsemblPlants; RZC84731; RZC84731; C5167_047517.
DR Gramene; RZC84731; RZC84731; C5167_047517.
DR KEGG; ag:AFB74620; -.
DR BioCyc; MetaCyc:MON-20624; -.
DR BRENDA; 2.3.1.285; 4515.
DR GO; GO:0016746; F:acyltransferase 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; Transferase.
FT CHAIN 1..471
FT /note="(13S,14R)-1,13-dihydroxy-N-methylcanadine 13-O-
FT acetyltransferase AT1"
FT /id="PRO_0000447600"
SQ SEQUENCE 471 AA; 52494 MW; 24FD2F411E5EECFC CRC64;
MATMSSAAVE VISKETIKPR NPTPYQLRNY NMSLLDQYSS LVYVPIILFY PAASDANSTG
SKHHDDLHLL KRSLSETLVH FYPMAGRMKD NMTVDCNDEG IDFFEVRIKG RMCDFMMKSD
AHLSLLLPSE VASTNFVKEA QVIVQVNMFD CGGTAICFCI SNKIADACTM ITFIRSLAGT
TNIARRGSSI AAPTTNQNLV PSFDSTSLFP PSEQLASQVS YPTQDSTSVD KLVSKRFVFD
AAKITSAREK LQSLMHDKYK CHRPTRVEVV SALIWKSAVK SAPPGSISTV THAMNFRKKM
DPPLQDASFG NLCVVVTAVL PATTATTTNP ATKKVSSTSN EEQVALDELS DFVALLRREI
DKVKGDKGCM EKIIQKFIYG HDASVAKDSD VEDKVTALFM TSWCKFGFYE ADFGWGTPVW
VTTVPLIEPK YKNMVFMNDM KCGEGIEVWV NFLEDDMTKF EHHLREILQL F