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Protein

Vinorine synthase

Gene

ACT

Organism
Rauvolfia serpentina (Serpentine wood) (Ophioxylon serpentinum)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Acetyltransferase that catalyzes the formation of vinorine, a precursor of the antiarrhythmic monoterpenoid indole alkaloid ajmaline. Acts on gardneral, but not on polyneuridine aldehyde or N-methylgardneral.1 Publication

Catalytic activityi

Acetyl-CoA + 16-epivellosimine = CoA + vinorine.

Activity regulationi

Complete inhibition by 4-(2-aminoethyl)-benzenesulfonyl fluoride (AEBSF), N-tosyl-L-phenylalanine chloromethylketone (TPCK), Hg2+ and diethyl-pyrocarbonate (DEPC). 50% inhibition by N-(N-(L-3-trans-carboxirane-2-carbonyl)-L-leucyl)-agmanitine (E-64), N-alpha-p-tosyl-L-lysine chloromethylketone (TLCK) and phenylmethylsulfonyl fluoride (PMSF).

Kineticsi

Except vinorine, no other acetylated alkaloids are deacetylated by the reverse reaction.
  1. KM=57 µM for Acetyl-CoA1 Publication
  2. KM=7.5 µM for gardneral1 Publication
  3. KM=63 µM for CoA1 Publication
  4. KM=10 µM for vinorine1 Publication
  1. Vmax=3.9 µmol/min/mg enzyme for the forward reaction1 Publication
  2. Vmax=44.1 µmol/min/mg enzyme for the reverse reaction1 Publication

pH dependencei

Optimum pH is 7.8.1 Publication

Temperature dependencei

Optimum temperature is 35 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei160Proton acceptor2 Publications1
Active sitei362Proton acceptor2 Publications1

GO - Molecular functioni

  • vinorine synthase activity Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processAlkaloid metabolism

Enzyme and pathway databases

BRENDAi2.3.1.160 5309

Names & Taxonomyi

Protein namesi
Recommended name:
Vinorine synthase (EC:2.3.1.160)
Gene namesi
Name:ACT
OrganismiRauvolfia serpentina (Serpentine wood) (Ophioxylon serpentinum)
Taxonomic identifieri4060 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsGentianalesApocynaceaeRauvolfioideaeVinceaeRauvolfiinaeRauvolfia

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi16S → A: 29% reduction of activity. 1 Publication1
Mutagenesisi29S → A: 75% reduction of activity. 1 Publication1
Mutagenesisi32D → A: 86% reduction of activity. 1 Publication1
Mutagenesisi68S → A: No effect. 1 Publication1
Mutagenesisi89C → A: No effect. 1 Publication1
Mutagenesisi149C → A: 90% reduction of activity. 1 Publication1
Mutagenesisi160H → A: Total loss of activity. 1 Publication1
Mutagenesisi164D → A: Total loss of activity. 1 Publication1
Mutagenesisi243S → A: 83% reduction of activity. 1 Publication1
Mutagenesisi293N → A: 32% reduction of activity. 1 Publication1
Mutagenesisi360D → A: No effect. 1 Publication1
Mutagenesisi362D → A: 65% reduction of activity. 1 Publication1
Mutagenesisi413S → A: No effect. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002958622 – 421Vinorine synthaseAdd BLAST420

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1421
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ70PR7
SMRiQ70PR7
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ70PR7

Family & Domainsi

Sequence similaritiesi

Belongs to the plant acyltransferase family.Curated

Phylogenomic databases

KOiK12694

Family and domain databases

Gene3Di3.30.559.10, 2 hits
InterProiView protein in InterPro
IPR023213 CAT-like_dom_sf
IPR003480 Transferase
PfamiView protein in Pfam
PF02458 Transferase, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q70PR7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAPQMEKVSE ELILPSSPTP QSLKCYKISH LDQLLLTCHI PFILFYPNPL
60 70 80 90 100
DSNLDPAQTS QHLKQSLSKV LTHFYPLAGR INVNSSVDCN DSGVPFVEAR
110 120 130 140 150
VQAQLSQAIQ NVVELEKLDQ YLPSAAYPGG KIEVNEDVPL AVKISFFECG
160 170 180 190 200
GTAIGVNLSH KIADVLSLAT FLNAWTATCR GETEIVLPNF DLAARHFPPV
210 220 230 240 250
DNTPSPELVP DENVVMKRFV FDKEKIGALR AQASSASEEK NFSRVQLVVA
260 270 280 290 300
YIWKHVIDVT RAKYGAKNKF VVVQAVNLRS RMNPPLPHYA MGNIATLLFA
310 320 330 340 350
AVDAEWDKDF PDLIGPLRTS LEKTEDDHNH ELLKGMTCLY ELEPQELLSF
360 370 380 390 400
TSWCRLGFYD LDFGWGKPLS ACTTTFPKRN AALLMDTRSG DGVEAWLPMA
410 420
EDEMAMLPVE LLSLVDSDFS K
Length:421
Mass (Da):46,828
Last modified:February 15, 2005 - v2
Checksum:i3C96D9872358CFA4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ556780 mRNA Translation: CAD89104.2

Genome annotation databases

KEGGiag:CAD89104

Similar proteinsi

Entry informationi

Entry nameiVINSY_RAUSE
AccessioniPrimary (citable) accession number: Q70PR7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: February 15, 2005
Last modified: September 12, 2018
This is version 47 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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