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Q9ZTK5 (DAT_CATRO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Deacetylvindoline O-acetyltransferase

EC=2.3.1.107
Alternative name(s):
Acetyl-coenzyme A:deacetylvindoline 4-O-acetyltransferase
Gene names
Name:DAT
OrganismCatharanthus roseus (Madagascar periwinkle) (Vinca rosea)
Taxonomic identifier4058 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsGentianalesApocynaceaeRauvolfioideaeVinceaeCatharanthinaeCatharanthus

Protein attributes

Sequence length439 AA.
Sequence statusComplete.
Protein existenceEvidence 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
   DomainCoiled coil
   Molecular functionAcyltransferase
Transferase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Molecular_function17-O-deacetylvindoline O-acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 439439Deacetylvindoline O-acetyltransferase
PRO_0000310727

Regions

Coiled coil312 – 34837 Potential

Sites

Active site1581Proton acceptor Potential
Active site3801Proton acceptor Potential

Sequences

Sequence LengthMass (Da)Tools
Q9ZTK5 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 1357C76550E0D04D

FASTA43949,873
        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 

« Hide

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

ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ9ZTK5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA2.3.1.107. 1211.
SABIO-RKQ9ZTK5.
UniPathwayUPA00365; UER00526.

Family and domain databases

Gene3D3.30.559.10. 2 hits.
InterProIPR023213. CAT-like_dom.
IPR003480. Transferase.
[Graphical view]
PfamPF02458. Transferase. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDAT_CATRO
AccessionPrimary (citable) accession number: Q9ZTK5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways