DAT_CATRO
ID DAT_CATRO Reviewed; 439 AA.
AC Q9ZTK5;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Deacetylvindoline O-acetyltransferase {ECO:0000303|PubMed:11154328, ECO:0000303|PubMed:2350183, ECO:0000303|PubMed:9681034};
DE EC=2.3.1.107 {ECO:0000269|PubMed:11154328, ECO:0000269|PubMed:2350183};
DE AltName: Full=Acetyl-coenzyme A:deacetylvindoline 4-O-acetyltransferase {ECO:0000303|PubMed:2350183};
GN Name=DAT {ECO:0000303|PubMed:11154328, ECO:0000303|PubMed:2350183,
GN ECO:0000303|PubMed:9681034};
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 [GENOMIC DNA], PROTEIN SEQUENCE OF 6-30; 73-83;
RP 201-216; 232-250; 334-349; 353-373 AND 424-439, INDUCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=9681034; DOI=10.1046/j.1365-313x.1998.00174.x;
RA St Pierre B., Laflamme P., Alarco A.-M., De Luca V.;
RT "The terminal O-acetyltransferase involved in vindoline biosynthesis
RT defines a new class of proteins responsible for coenzyme A-dependent acyl
RT transfer.";
RL Plant J. 14:703-713(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INHIBITION,
RP AND PATHWAY.
RX PubMed=2350183; DOI=10.1016/0003-9861(90)90504-r;
RA Power R., Kurz W.G.W., De Luca V.;
RT "Purification and characterization of acetylcoenzyme A: deacetylvindoline
RT 4-O-acetyltransferase from Catharanthus roseus.";
RL Arch. Biochem. Biophys. 279:370-376(1990).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=10330473; DOI=10.2307/3870822;
RA St Pierre B., Vazquez-Flota F.A., De Luca V.;
RT "Multicellular compartmentation of Catharanthus roseus alkaloid
RT biosynthesis predicts intercellular translocation of a pathway
RT intermediate.";
RL Plant Cell 11:887-900(1999).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND PATHWAY.
RX PubMed=11154328; DOI=10.1104/pp.125.1.189;
RA Laflamme P., St-Pierre B., De Luca V.;
RT "Molecular and biochemical analysis of a Madagascar periwinkle root-
RT specific minovincinine-19-hydroxy-O-acetyltransferase.";
RL Plant Physiol. 125:189-198(2001).
RN [5]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=21047699; DOI=10.1016/j.jplph.2010.08.018;
RA Guirimand G., Guihur A., Poutrain P., Hericourt F., Mahroug S.,
RA St-Pierre B., Burlat V., Courdavault V.;
RT "Spatial organization of the vindoline biosynthetic pathway in Catharanthus
RT roseus.";
RL J. Plant Physiol. 168:549-557(2011).
CC -!- FUNCTION: Involved in the biosynthesis of vindoline, a precursor of
CC vinblastine and vincristine. {ECO:0000269|PubMed:11154328,
CC ECO:0000269|PubMed:2350183}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-O-deacetylvindoline + acetyl-CoA = CoA + vindoline;
CC Xref=Rhea:RHEA:24496, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57753, ChEBI:CHEBI:58461; EC=2.3.1.107;
CC Evidence={ECO:0000269|PubMed:11154328, ECO:0000269|PubMed:2350183};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.5 uM for acetyl-CoA (at pH 7.6 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:11154328};
CC KM=30 uM for deactylvindoline (at pH 7.6 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:11154328};
CC KM=6.5 mM for acetyl-CoA {ECO:0000269|PubMed:2350183};
CC KM=1.3 mM for deacetylvindoline {ECO:0000269|PubMed:2350183};
CC Vmax=1.9 pmol/sec/mg enzyme toward acetyl-CoA (at pH 7.6 and 37
CC degrees Celsius) {ECO:0000269|PubMed:11154328};
CC Vmax=3.81 pmol/sec/mg enzyme toward deactylvindoline (at pH 7.6 and
CC 37 degrees Celsius) {ECO:0000269|PubMed:11154328};
CC Vmax=12.6 pmol/sec/ug enzyme toward acetyl-CoA
CC {ECO:0000269|PubMed:2350183};
CC Vmax=10.1 pmol/sec/ug enzyme toward deacetylvindoline
CC {ECO:0000269|PubMed:2350183};
CC pH dependence:
CC Optimum pH is 7.5-9.0. {ECO:0000269|PubMed:2350183};
CC -!- PATHWAY: Alkaloid biosynthesis; vindoline biosynthesis.
CC {ECO:0000269|PubMed:11154328, ECO:0000269|PubMed:2350183}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:21047699}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21047699}. Nucleus
CC {ECO:0000269|PubMed:21047699}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in young leaves of mature
CC plants. Low expression in stems and flowers and not detected in roots.
CC Confined to the laticifer and idioblast cells of leaves, stems, and
CC flower buds (PubMed:11154328). {ECO:0000269|PubMed:10330473,
CC ECO:0000269|PubMed:11154328, ECO:0000269|PubMed:21047699,
CC ECO:0000269|PubMed:9681034}.
CC -!- INDUCTION: Inhibited by tabersonine, coenzyme A, K(+), Mg(2+) and
CC Mn(2+). Induced by light with a maximum 48 hours after initiation of
CC the light treatment. {ECO:0000269|PubMed:9681034}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
CC -!- CAUTION: Was originally purified as a heterodimer of the N- and C-
CC terminal end of the DAT gene product, but the cleavage of DAT protein
CC appears to be a purification artifact. {ECO:0000305|PubMed:2350183}.
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DR EMBL; AF053307; AAC99311.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9ZTK5; -.
DR SMR; Q9ZTK5; -.
DR KEGG; ag:AAC99311; -.
DR BRENDA; 2.3.1.107; 1211.
DR SABIO-RK; Q9ZTK5; -.
DR UniPathway; UPA00365; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0047162; F:17-O-deacetylvindoline 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; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Nucleus; Transferase.
FT CHAIN 1..439
FT /note="Deacetylvindoline O-acetyltransferase"
FT /id="PRO_0000310727"
FT COILED 317..344
FT /evidence="ECO:0000255"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT ACT_SITE 380
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
SQ SEQUENCE 439 AA; 49873 MW; 1357C76550E0D04D CRC64;
MESGKISVET ETLSKTLIKP SSPTPQSLSR YNLSYNDQNI YQTCVSVGFF YENPDGIEIS
TIREQLQNSL SKTLVSYYPF AGKVVKNDYI HCNDDGIEFV EVRIRCRMND ILKYELRSYA
RDLVLPKRVT VGSEDTTAIV QLSHFDCGGL AVAFGISHKV ADGGTIASFM KDWAASACYL
SSSHHVPTPL LVSDSIFPRQ DNIICEQFPT SKNCVEKTFI FPPEAIEKLK SKAVEFGIEK
PTRVEVLTAF LSRCATVAGK SAAKNNNCGQ SLPFPVLQAI NLRPILELPQ NSVGNLVSIY
FSRTIKENDY LNEKEYTKLV INELRKEKQK IKNLSREKLT YVAQMEEFVK SLKEFDISNF
LDIDAYLSDS WCRFPFYDVD FGWGKPIWVC LFQPYIKNCV VMMDYPFGDD YGIEAIVSFE
QEKMSAFEKN EQLLQFVSN
