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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei160 – 1601Proton acceptorCurated
Active sitei362 – 3621Proton acceptorSequence analysis

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi16 – 161S → A: 29% reduction of activity. 1 Publication
Mutagenesisi29 – 291S → A: 75% reduction of activity. 1 Publication
Mutagenesisi32 – 321D → A: 86% reduction of activity. 1 Publication
Mutagenesisi68 – 681S → A: No effect. 1 Publication
Mutagenesisi89 – 891C → A: No effect. 1 Publication
Mutagenesisi149 – 1491C → A: 90% reduction of activity. 1 Publication
Mutagenesisi160 – 1601H → A: Total loss of activity. 1 Publication
Mutagenesisi164 – 1641D → A: Total loss of activity. 1 Publication
Mutagenesisi243 – 2431S → A: 83% reduction of activity. 1 Publication
Mutagenesisi293 – 2931N → A: 32% reduction of activity. 1 Publication
Mutagenesisi360 – 3601D → A: No effect. 1 Publication
Mutagenesisi362 – 3621D → A: 65% reduction of activity. 1 Publication
Mutagenesisi413 – 4131S → A: No effect. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 421420Vinorine synthasePRO_0000295862Add
BLAST

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1
421
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 1410Combined sources
Helixi30 – 334Combined sources
Beta strandi37 – 4610Combined sources
Helixi56 – 7015Combined sources
Turni71 – 733Combined sources
Helixi75 – 784Combined sources
Beta strandi79 – 824Combined sources
Turni83 – 853Combined sources
Beta strandi86 – 883Combined sources
Beta strandi94 – 10310Combined sources
Helixi105 – 1095Combined sources
Helixi115 – 1217Combined sources
Beta strandi122 – 1243Combined sources
Beta strandi126 – 1327Combined sources
Beta strandi139 – 1468Combined sources
Beta strandi152 – 1598Combined sources
Turni160 – 1623Combined sources
Helixi165 – 17915Combined sources
Helixi192 – 1965Combined sources
Beta strandi212 – 22110Combined sources
Helixi223 – 23210Combined sources
Helixi244 – 26320Combined sources
Beta strandi270 – 2789Combined sources
Helixi279 – 2813Combined sources
Beta strandi282 – 2843Combined sources
Beta strandi295 – 3028Combined sources
Helixi310 – 3134Combined sources
Helixi314 – 3207Combined sources
Helixi328 – 34013Combined sources
Helixi344 – 3463Combined sources
Beta strandi347 – 3537Combined sources
Helixi358 – 3603Combined sources
Beta strandi363 – 3653Combined sources
Beta strandi369 – 3724Combined sources
Beta strandi381 – 3866Combined sources
Beta strandi390 – 40011Combined sources
Helixi401 – 4066Combined sources
Helixi409 – 4124Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BGHX-ray2.60A/B1-421[»]
ProteinModelPortaliQ70PR7.
SMRiQ70PR7. Positions 4-421.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
2BGHX-ray2.60A/B1-421[»]
ProteinModelPortaliQ70PR7.
SMRiQ70PR7. Positions 4-421.
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...

Publicationsi

  1. "Acetyltransfer in natural product biosynthesis -- functional cloning and molecular analysis of vinorine synthase."
    Bayer A., Ma X., Stoeckigt J.
    Bioorg. Med. Chem. 12:2787-2795(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-21; 132-143; 181-195; 219-225 AND 245-254, MUTAGENESIS OF SER-16; SER-29; ASP-32; SER-68; CYS-89; CYS-149; HIS-160; ASP-164; SER-243; ASN-293; ASP-360; ASP-362 AND SER-413, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
  2. "Crystal structure of vinorine synthase, the first representative of the BAHD superfamily."
    Ma X., Koepke J., Panjikar S., Fritzsch G., Stoeckigt J.
    J. Biol. Chem. 280:13576-13583(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), SUBUNIT.

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: December 9, 2015
This is version 42 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.