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Protein

Vinorine synthase

Gene

ACT

Organism
Rauvolfia serpentina (Serpentine wood) (Ophioxylon serpentinum)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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.

Enzyme 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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Alkaloid 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
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 14Combined sources10
Helixi30 – 33Combined sources4
Beta strandi37 – 46Combined sources10
Helixi56 – 70Combined sources15
Turni71 – 73Combined sources3
Helixi75 – 78Combined sources4
Beta strandi79 – 82Combined sources4
Turni83 – 85Combined sources3
Beta strandi86 – 88Combined sources3
Beta strandi94 – 103Combined sources10
Helixi105 – 109Combined sources5
Helixi115 – 121Combined sources7
Beta strandi122 – 124Combined sources3
Beta strandi126 – 132Combined sources7
Beta strandi139 – 146Combined sources8
Beta strandi152 – 159Combined sources8
Turni160 – 162Combined sources3
Helixi165 – 179Combined sources15
Helixi192 – 196Combined sources5
Beta strandi212 – 221Combined sources10
Helixi223 – 232Combined sources10
Helixi244 – 263Combined sources20
Beta strandi270 – 278Combined sources9
Helixi279 – 281Combined sources3
Beta strandi282 – 284Combined sources3
Beta strandi295 – 302Combined sources8
Helixi310 – 313Combined sources4
Helixi314 – 320Combined sources7
Helixi328 – 340Combined sources13
Helixi344 – 346Combined sources3
Beta strandi347 – 353Combined sources7
Helixi358 – 360Combined sources3
Beta strandi363 – 365Combined sources3
Beta strandi369 – 372Combined sources4
Beta strandi381 – 386Combined sources6
Beta strandi390 – 400Combined sources11
Helixi401 – 406Combined sources6
Helixi409 – 412Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BGHX-ray2.60A/B1-421[»]
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.
InterProiIPR023213. CAT-like_dom.
IPR003480. Transferase.
[Graphical view]
PfamiPF02458. Transferase. 1 hit.
[Graphical view]

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.

Cross-referencesi

Sequence databases

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BGHX-ray2.60A/B1-421[»]
ProteinModelPortaliQ70PR7.
SMRiQ70PR7.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:CAD89104.

Phylogenomic databases

KOiK12694.

Enzyme and pathway databases

BRENDAi2.3.1.160. 5309.

Miscellaneous databases

EvolutionaryTraceiQ70PR7.

Family and domain databases

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

Entry informationi

Entry nameiVINSY_RAUSE
AccessioniPrimary (citable) accession number: Q70PR7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: February 15, 2005
Last modified: November 2, 2016
This is version 44 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.