TAT_CATRO
ID TAT_CATRO Reviewed; 436 AA.
AC A0A2K8FQU5;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 25-APR-2018, sequence version 1.
DT 03-AUG-2022, entry version 9.
DE RecName: Full=Tabersonine-19-hydroxy-O-acetyltransferase {ECO:0000303|PubMed:31009114};
DE EC=2.3.1.- {ECO:0000269|PubMed:31009114};
GN Name=TAT {ECO:0000303|PubMed:31009114};
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, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, INDUCTION BY JASMONIC ACID, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP TISSUE SPECIFICITY.
RX PubMed=29438577; DOI=10.1111/tpj.13868;
RA Carqueijeiro I., Duge de Bernonville T., Lanoue A., Dang T.-T.,
RA Teijaro C.N., Paetz C., Billet K., Mosquera A., Oudin A., Besseau S.,
RA Papon N., Glevarec G., Atehortua L., Clastre M., Giglioli-Guivarc'h N.,
RA Schneider B., St-Pierre B., Andrade R.B., O'Connor S.E., Courdavault V.;
RT "A BAHD acyltransferase catalyzing 19-O-acetylation of tabersonine
RT derivatives in roots of Catharanthus roseus enables combinatorial synthesis
RT of monoterpene indole alkaloids.";
RL Plant J. 94:469-484(2018).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=31009114; DOI=10.1111/tpj.14346;
RA Williams D., Qu Y., Simionescu R., De Luca V.;
RT "The assembly of (+)-vincadifformine- and (-)-tabersonine-derived
RT monoterpenoid indole alkaloids in Catharanthus roseus involves separate
RT branch pathways.";
RL Plant J. 99:626-636(2019).
CC -!- FUNCTION: Component of the monoterpenoid indole alkaloids (MIAs, e.g.
CC echitovenine, tabersonine, lochnericine, 19-hydroxytabersonine and
CC horhammericine) biosynthetic pathway; MIAs are used in cancer treatment
CC and other medical applications (PubMed:31009114). Acyltransferase
CC catalyzing the conversion of horhammericine to 19-O-
CC acetylhorhammericine, of 19-hydroxytabersonine to 19-O-
CC acetyltabersonine and of minovincinine to echitovenine
CC (PubMed:29438577, PubMed:31009114). {ECO:0000269|PubMed:29438577,
CC ECO:0000269|PubMed:31009114}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + horhammericine = 19-O-acetylhorhammericine + CoA;
CC Xref=Rhea:RHEA:61068, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:144375, ChEBI:CHEBI:144376;
CC Evidence={ECO:0000269|PubMed:29438577, ECO:0000269|PubMed:31009114};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(-)-(R)-19-hydroxytabersonine + acetyl-CoA = (-)-(R)-19-O-
CC acetyltabersonine + CoA; Xref=Rhea:RHEA:61072, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:144372, ChEBI:CHEBI:144377;
CC Evidence={ECO:0000269|PubMed:29438577, ECO:0000269|PubMed:31009114};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(-)-minovincinine + acetyl-CoA = (-)-echitovenine + CoA;
CC Xref=Rhea:RHEA:61076, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:144373, ChEBI:CHEBI:144384;
CC Evidence={ECO:0000269|PubMed:29438577, ECO:0000269|PubMed:31009114};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5 uM for acetyl-CoA (at pH 7.6 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:29438577};
CC KM=9 uM for (-)-minovincinine (at pH 7.6 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:29438577};
CC KM=58 uM for horhammericine (at pH 7.6 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:29438577};
CC KM=78 uM for 19-hydroxytabersonine (at pH 7.6 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:29438577};
CC Vmax=0.14 umol/sec/ug enzyme toward acetyl-CoA (at pH 7.6 and 30
CC degrees Celsius) {ECO:0000269|PubMed:29438577};
CC Vmax=0.13 umol/sec/ug enzyme with (-)-minovincinine as substrate (at
CC pH 7.6 and 30 degrees Celsius) {ECO:0000269|PubMed:29438577};
CC Vmax=0.02 umol/sec/ug enzyme with horhammericine as substrate (at pH
CC 7.6 and 30 degrees Celsius) {ECO:0000269|PubMed:29438577};
CC Vmax=1.32 umol/sec/ug enzyme with 19-hydroxytabersonine as substrate
CC (at pH 7.6 and 30 degrees Celsius) {ECO:0000269|PubMed:29438577};
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:31009114}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9ZTK5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29438577}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:29438577}.
CC -!- TISSUE SPECIFICITY: Confined to roots. {ECO:0000269|PubMed:29438577}.
CC -!- INDUCTION: Induced by jasmonic acid (MeJA).
CC {ECO:0000269|PubMed:29438577}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
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DR EMBL; KU821123; AQP25667.1; -; mRNA.
DR AlphaFoldDB; A0A2K8FQU5; -.
DR SMR; A0A2K8FQU5; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016407; F:acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0035835; P:indole alkaloid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR023213; CAT-like_dom_sf.
PE 1: Evidence at protein level;
KW Acyltransferase; Alkaloid metabolism; Cytoplasm; Nucleus; Transferase.
FT CHAIN 1..436
FT /note="Tabersonine-19-hydroxy-O-acetyltransferase"
FT /id="PRO_0000448560"
FT MOTIF 211..218
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT ACT_SITE 153
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT ACT_SITE 361
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
SQ SEQUENCE 436 AA; 49141 MW; A0A33E56ABA90DB0 CRC64;
MASKMVEIVS KMFIKPSSPT PQSLRRYNLS SIDQTIDSEV TSLAFFYTYN PSHESSKIGD
LLKNSLSKTL VSYYQFAGRL IENDYIDCND EGVEFVEVRI HGRMNDILKR GKSFATDLVL
PTRIIALHED SLLIVQLSHF DCGGIAIGFG ASHKVSDGVS NVMFMKDWAS STSLSTFHKP
TPLLTADSIF PPEDNKLLSN KSIVSFQQCL GKRFVFSTEA IEKLKSKAIE YGIQKPSRVE
VVTAFLCQCA ANCDLPRKKP YAIISAVNLR PYLALPQNSI GNIFSFYFCI NDEGMDNQFS
ALISKLRNGK QKLLENIISK EKLTYESQMQ ELTKCLDQLN ISSLDTYFCS SWCRFPVYDI
DFGWGKPILV SPFQPHVKDL ILLMDSPEGD GIEALITMEE KKMAAFEKNE ELRSFAYLDS
PEPEALIIPE EDKSFE
