Q9ZTK5 (DAT_CATRO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Deacetylvindoline O-acetyltransferase
EC=2.3.1.107

Alternative name(s):
Acetyl-coenzyme A:deacetylvindoline 4-O-acetyltransferase

Gene names

Name:

DAT

Organism

Catharanthus roseus (Madagascar periwinkle) (Vinca rosea)

Taxonomic identifier

4058 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Gentianales › Apocynaceae › Rauvolfioideae › Vinceae › Catharanthus

Protein attributes

Sequence length	439 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the biosynthesis of vindoline, a precursor of vinblastine and vincristine.
Catalytic activity	Acetyl-CoA + deacetylvindoline = CoA + vindoline.
Pathway	Alkaloid biosynthesis; vindoline biosynthesis; vindoline from tabersonine: step 6/6.
Tissue specificity	Predominantly expressed in young leaves of mature plants. Low expression in stems and flowers and not detected in roots. Expressed in the laticifer and idioblast cells of leaves, stems, and flower buds. Ref.1 Ref.3
Induction	Inhibited by tabersonine, coenzyme A, K+, Mg2+ and Mn2+. Induced by light with a maximum 48 hours after initiation of the light treatment. Ref.1
Sequence similarities	Belongs to the plant acyltransferase family.
Caution	Was originally (Ref.2) purified as a heterodimer of the N- and C-terminal end of the DAT gene product, but the cleavage of DAT protein appears to be a purification artifact.
Biophysicochemical properties	Kinetic parameters: KM=6.5 mM for acetyl-CoA Ref.2 KM=1.3 mM for deacetylvindoline Vmax=12.6 pmol/sec/µg enzyme toward acetyl-CoA Vmax=10.1 pmol/sec/µg enzyme toward deacetylvindoline pH dependence: Optimum pH is 7.5-9.0.

Ontologies

Keywords
Domain	Coiled coil
Molecular function	Acyltransferase Transferase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Molecular_function	17-O-deacetylvindoline O-acetyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 439	439	Deacetylvindoline O-acetyltransferase		PRO_0000310727
Regions
	Coiled coil	312 – 348	37	Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9ZTK5 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 1357C76550E0D04D	FASTA	439	49,873
	10 20 30 40 50 60 MESGKISVET ETLSKTLIKP SSPTPQSLSR YNLSYNDQNI YQTCVSVGFF YENPDGIEIS 70 80 90 100 110 120 TIREQLQNSL SKTLVSYYPF AGKVVKNDYI HCNDDGIEFV EVRIRCRMND ILKYELRSYA 130 140 150 160 170 180 RDLVLPKRVT VGSEDTTAIV QLSHFDCGGL AVAFGISHKV ADGGTIASFM KDWAASACYL 190 200 210 220 230 240 SSSHHVPTPL LVSDSIFPRQ DNIICEQFPT SKNCVEKTFI FPPEAIEKLK SKAVEFGIEK 250 260 270 280 290 300 PTRVEVLTAF LSRCATVAGK SAAKNNNCGQ SLPFPVLQAI NLRPILELPQ NSVGNLVSIY 310 320 330 340 350 360 FSRTIKENDY LNEKEYTKLV INELRKEKQK IKNLSREKLT YVAQMEEFVK SLKEFDISNF 370 380 390 400 410 420 LDIDAYLSDS WCRFPFYDVD FGWGKPIWVC LFQPYIKNCV VMMDYPFGDD YGIEAIVSFE 430 QEKMSAFEKN EQLLQFVSN

References

[1]	"The terminal O-acetyltransferase involved in vindoline biosynthesis defines a new class of proteins responsible for coenzyme A-dependent acyl transfer." St Pierre B., Laflamme P., Alarco A.-M., De Luca V. Plant J. 14:703-713(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 6-30; 73-83; 201-216; 232-250; 334-349; 353-373 AND 424-439, INDUCTION, TISSUE SPECIFICITY.
[2]	"Purification and characterization of acetylcoenzyme A: deacetylvindoline 4-O-acetyltransferase from Catharanthus roseus." Power R., Kurz W.G., De Luca V. Arch. Biochem. Biophys. 279:370-376(1990) [PubMed] [Europe PMC] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, INHIBITION.
[3]	"Multicellular compartmentation of Catharanthus roseus alkaloid biosynthesis predicts intercellular translocation of a pathway intermediate." St Pierre B., Vazquez-Flota F.A., De Luca V. Plant Cell 11:887-900(1999) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF053307 Genomic DNA. Translation: AAC99311.1.
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	Q9ZTK5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BRENDA	2.3.1.107. 1211.
SABIO-RK	Q9ZTK5.
UniPathway	UPA00365; UER00526.
Family and domain databases
Gene3D	3.30.559.10. 2 hits.
InterPro	IPR023213. CAT-like_dom. IPR003480. Transferase. [Graphical view]
Pfam	PF02458. Transferase. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DAT_CATRO

Accession

Primary (citable) accession number: Q9ZTK5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 13, 2007
Last sequence update:	May 1, 1999
Last modified:	April 3, 2013
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program