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Q9ZTK5

- DAT_CATRO

UniProt

Q9ZTK5 - DAT_CATRO

Protein

Deacetylvindoline O-acetyltransferase

Gene

DAT

Organism
Catharanthus roseus (Madagascar periwinkle) (Vinca rosea)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 42 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Involved in the biosynthesis of vindoline, a precursor of vinblastine and vincristine.

    Catalytic activityi

    Acetyl-CoA + deacetylvindoline = CoA + vindoline.

    Kineticsi

    1. KM=6.5 mM for acetyl-CoA1 Publication
    2. KM=1.3 mM for deacetylvindoline1 Publication

    Vmax=12.6 pmol/sec/µg enzyme toward acetyl-CoA1 Publication

    Vmax=10.1 pmol/sec/µg enzyme toward deacetylvindoline1 Publication

    pH dependencei

    Optimum pH is 7.5-9.0.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei158 – 1581Proton acceptorSequence Analysis
    Active sitei380 – 3801Proton acceptorSequence Analysis

    GO - Molecular functioni

    1. 17-O-deacetylvindoline O-acetyltransferase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Enzyme and pathway databases

    BRENDAi2.3.1.107. 1211.
    SABIO-RKQ9ZTK5.
    UniPathwayiUPA00365; UER00526.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Deacetylvindoline O-acetyltransferase (EC:2.3.1.107)
    Alternative name(s):
    Acetyl-coenzyme A:deacetylvindoline 4-O-acetyltransferase
    Gene namesi
    Name:DAT
    OrganismiCatharanthus roseus (Madagascar periwinkle) (Vinca rosea)
    Taxonomic identifieri4058 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsGentianalesApocynaceaeRauvolfioideaeVinceaeCatharanthinaeCatharanthus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 439439Deacetylvindoline O-acetyltransferasePRO_0000310727Add
    BLAST

    Proteomic databases

    PRIDEiQ9ZTK5.

    Expressioni

    Tissue specificityi

    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.2 Publications

    Inductioni

    Inhibited by tabersonine, coenzyme A, K+, Mg2+ and Mn2+. Induced by light with a maximum 48 hours after initiation of the light treatment.1 Publication

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili312 – 34837Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the plant acyltransferase family.Curated

    Keywords - Domaini

    Coiled coil

    Family and domain databases

    Gene3Di3.30.559.10. 2 hits.
    InterProiIPR023213. CAT-like_dom.
    IPR003480. Transferase.
    [Graphical view]
    PfamiPF02458. Transferase. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9ZTK5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MESGKISVET ETLSKTLIKP SSPTPQSLSR YNLSYNDQNI YQTCVSVGFF    50
    YENPDGIEIS TIREQLQNSL SKTLVSYYPF AGKVVKNDYI HCNDDGIEFV 100
    EVRIRCRMND ILKYELRSYA RDLVLPKRVT VGSEDTTAIV QLSHFDCGGL 150
    AVAFGISHKV ADGGTIASFM KDWAASACYL SSSHHVPTPL LVSDSIFPRQ 200
    DNIICEQFPT SKNCVEKTFI FPPEAIEKLK SKAVEFGIEK PTRVEVLTAF 250
    LSRCATVAGK SAAKNNNCGQ SLPFPVLQAI NLRPILELPQ NSVGNLVSIY 300
    FSRTIKENDY LNEKEYTKLV INELRKEKQK IKNLSREKLT YVAQMEEFVK 350
    SLKEFDISNF LDIDAYLSDS WCRFPFYDVD FGWGKPIWVC LFQPYIKNCV 400
    VMMDYPFGDD YGIEAIVSFE QEKMSAFEKN EQLLQFVSN 439
    Length:439
    Mass (Da):49,873
    Last modified:May 1, 1999 - v1
    Checksum:i1357C76550E0D04D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF053307 Genomic DNA. Translation: AAC99311.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF053307 Genomic DNA. Translation: AAC99311.1 .

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q9ZTK5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00365 ; UER00526 .
    BRENDAi 2.3.1.107. 1211.
    SABIO-RK Q9ZTK5.

    Family and domain databases

    Gene3Di 3.30.559.10. 2 hits.
    InterProi IPR023213. CAT-like_dom.
    IPR003480. Transferase.
    [Graphical view ]
    Pfami PF02458. Transferase. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiDAT_CATRO
    AccessioniPrimary (citable) accession number: Q9ZTK5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2007
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 42 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Caution

    Was originally 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.1 Publication

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3