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Enzyme Nomenclature
Information on EC 1.14.13.217 - protodeoxyviolaceinate monooxygenase
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1.14.13.217 protodeoxyviolaceinate monooxygenaseIUBMB Comments
The enzyme, characterized from the bacterium Chromobacterium violaceum, participates in the biosynthesis of the violet pigment violacein. The product, protoviolaceinate, can be acted upon by EC 1.14.13.224, violacein synthase, leading to violacein production. However, it is very labile, and in the presence of oxygen can undergo non-enzymic autooxidation to the shunt product proviolacein.
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The enzyme appears in viruses and cellular organisms
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
VioD
VioD oxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
protodeoxyviolaceinate + NAD(P)H + O2 = protoviolaceinate + NAD(P)+ + H2O
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
protodeoxyviolaceinate,NAD(P)H:O2 oxidoreductase
The enzyme, characterized from the bacterium Chromobacterium violaceum, participates in the biosynthesis of the violet pigment violacein. The product, protoviolaceinate, can be acted upon by EC 1.14.13.224, violacein synthase, leading to violacein production. However, it is very labile, and in the presence of oxygen can undergo non-enzymic autooxidation to the shunt product proviolacein.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
protodeoxyviolaceinate + NAD(P)H + H+ + O2
protoviolaceinate + NAD(P)+
-
-
?
protodeoxyviolaceinate + NAD(P)H + H+ + O2
protoviolaceinate + NAD(P)+
-
-
?
protodeoxyviolaceinate + NAD(P)H + H+ + O2
protoviolaceinate + NAD(P)+
enzyme VioD hydroxylates one indole ring at the 5-position to yield proviolacein
-
?
protodeoxyviolaceinate + NAD(P)H + H+ + O2
protoviolaceinate + NAD(P)+
-
-
?
protodeoxyviolaceinate + NAD(P)H + H+ + O2
protoviolaceinate + NAD(P)+
enzyme VioD hydroxylates one indole ring at the 5-position to yield proviolacein
-
?
protodeoxyviolaceinate + NAD(P)H + H+ + O2
protoviolaceinate + NAD(P)+
Chromobacterium violaceum JCM 1249
-
-
?
protodeoxyviolaceinate + NAD(P)H + H+ + O2
protoviolaceinate + NAD(P)+
-
-
-
?
protodeoxyviolaceinate + NAD(P)H + H+ + O2
protoviolaceinate + NAD(P)+
-
-
-
?
protodeoxyviolaceinate + NAD(P)H + H+ + O2
protoviolaceinate + NAD(P)+
-
-
?
protodeoxyviolaceinate + NAD(P)H + H+ + O2
protoviolaceinate + NAD(P)+
-
-
?
protodeoxyviolaceinate + NADPH + H+ + O2
protoviolaceinate + NADP+
enzyme VioD is a monooxygenase catalyzing the incorporation of O2 into 6-postion
-
?
protodeoxyviolaceinate + NADPH + H+ + O2
protoviolaceinate + NADP+
VioD catalyses the oxygenation reaction at the 6-position
i.e. 5-(5-hydroxy-1H-indol-3-yl)-3-(1H-indol-3-yl)-1H-pyrrole-2-carboxylic acid
?
protodeoxyviolaceinate + NADPH + H+ + O2
protoviolaceinate + NADP+
Chromobacterium violaceum JCM 1249
enzyme VioD is a monooxygenase catalyzing the incorporation of O2 into 6-postion
-
?
protodeoxyviolaceinate + NADPH + H+ + O2
protoviolaceinate + NADP+
Chromobacterium violaceum JCM 1249
VioD catalyses the oxygenation reaction at the 6-position
i.e. 5-(5-hydroxy-1H-indol-3-yl)-3-(1H-indol-3-yl)-1H-pyrrole-2-carboxylic acid
?
additional information
?
-
enzyme VioD is a flavin-dependent oxygenase that catalyzes the hydroxylation of the intermediate product prodeoxyviolaceinic acid at the 5-position of one indole ring to yield proviolacein
-
?
additional information
?
-
VioD is no tryptophan 5-hydroxylase
-
?
additional information
?
-
the recombinant enzyme shows no ability to hydroxylate L-tryptophan. The enzyme does not hydroxylate deoxyviolacein
-
?
additional information
?
-
the recombinant enzyme shows no ability to hydroxylate L-tryptophan. The enzyme does not hydroxylate deoxyviolacein
-
?
additional information
?
-
Chromobacterium violaceum JCM 1249
VioD is no tryptophan 5-hydroxylase
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
protodeoxyviolaceinate + NAD(P)H + H+ + O2
protoviolaceinate + NAD(P)+
-
-
-
?
protodeoxyviolaceinate + NAD(P)H + H+ + O2
protoviolaceinate + NAD(P)+
-
-
-
?
protodeoxyviolaceinate + NAD(P)H + H+ + O2
protoviolaceinate + NAD(P)+
enzyme VioD hydroxylates one indole ring at the 5-position to yield proviolacein
-
-
?
protodeoxyviolaceinate + NAD(P)H + H+ + O2
protoviolaceinate + NAD(P)+
enzyme VioD hydroxylates one indole ring at the 5-position to yield proviolacein
-
-
?
protodeoxyviolaceinate + NAD(P)H + H+ + O2
protoviolaceinate + NAD(P)+
Chromobacterium violaceum JCM 1249
-
-
-
?
protodeoxyviolaceinate + NAD(P)H + H+ + O2
protoviolaceinate + NAD(P)+
-
-
-
-
?
protodeoxyviolaceinate + NAD(P)H + H+ + O2
protoviolaceinate + NAD(P)+
-
-
-
-
?
protodeoxyviolaceinate + NAD(P)H + H+ + O2
protoviolaceinate + NAD(P)+
-
-
-
?
protodeoxyviolaceinate + NAD(P)H + H+ + O2
protoviolaceinate + NAD(P)+
-
-
-
?
protodeoxyviolaceinate + NADPH + H+ + O2
protoviolaceinate + NADP+
enzyme VioD is a monooxygenase catalyzing the incorporation of O2 into 6-postion
-
-
?
protodeoxyviolaceinate + NADPH + H+ + O2
protoviolaceinate + NADP+
Chromobacterium violaceum JCM 1249
enzyme VioD is a monooxygenase catalyzing the incorporation of O2 into 6-postion
-
-
?
additional information
?
-
enzyme VioD is a flavin-dependent oxygenase that catalyzes the hydroxylation of the intermediate product prodeoxyviolaceinic acid at the 5-position of one indole ring to yield proviolacein
-
-
?
additional information
?
-
VioD is no tryptophan 5-hydroxylase
-
-
?
additional information
?
-
Chromobacterium violaceum JCM 1249
VioD is no tryptophan 5-hydroxylase
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Chromobacterium violaceum JCM 1249
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
-
genes vioA, vioC and vioD encode nucleotide-dependent monooxygenases
evolution
VioD belongs to the family of flavin-containing NAD(P)H-dependent monooxygenases
evolution
Chromobacterium violaceum JCM 1249
-
VioD belongs to the family of flavin-containing NAD(P)H-dependent monooxygenases
malfunction
-
biosynthetic pathway of L-tryptophan to violacein in the wild-type and and deoxyviolacein in the vioD deletion mutant, overview
malfunction
-
disruption of vioA or vioB completely abrogates the biosynthesis of violacein intermediates, while disruption of the vioC or vioD genes results in the production of violacein precursors
malfunction
disruption of vioA or vioB completely abrogates the biosynthesis of violacein intermediates, while disruption of vioC or vioD results in the production of violacein precursors. Gene vioE is essential for violacein biosynthesis. Enzymes VioC and VioD are responsible for the oxygenations at the ox-indole and hydroxyindole, respectively. In the absence of VioC, the expected proviolaceins are accompanied by other compounds: deoxychromoviridans, chromoviridans, and oxychromoviridans
malfunction
formation of deoxyviolacein and prodeoxyviolacein occurs due to the insufficient amount of VioD
malfunction
-
biosynthetic pathway of L-tryptophan to violacein in the wild-type and and deoxyviolacein in the vioD deletion mutant, overview
malfunction
Chromobacterium violaceum JCM 1249
-
formation of deoxyviolacein and prodeoxyviolacein occurs due to the insufficient amount of VioD
malfunction
Chromobacterium violaceum JCM 1249
-
disruption of vioA or vioB completely abrogates the biosynthesis of violacein intermediates, while disruption of vioC or vioD results in the production of violacein precursors. Gene vioE is essential for violacein biosynthesis. Enzymes VioC and VioD are responsible for the oxygenations at the ox-indole and hydroxyindole, respectively. In the absence of VioC, the expected proviolaceins are accompanied by other compounds: deoxychromoviridans, chromoviridans, and oxychromoviridans
metabolism
-
biosynthetic pathway of L-tryptophan to violacein in the wild-type and and deoxyviolacein in the vioD deletion mutant, NMR analysis of reactio products and intermediates, overview
metabolism
the biosynthesis of violacein from 2 molecules of L-tryptophan requires five contiguously encoded proteins VioA-E. VioC and VioD act sequentially, VioD hydroxylates one indole ring at the 5-position to yield proviolacein, and VioC then acts on the other indole ring at the 2-position to create the oxindole and complete violacein formation. the order of hydroxylation on route to violacein is VioD followed by VioC. L-tryptophan, and not 5-hydroxy-L-tryptophan, is the sole precursor to violacein
metabolism
-
the enzyme is involved in the violacein biosynthetic pathway from Chromobacterium violaceum, sequence analysis and functional characterization, overview. The four genes vioABCD are necessary for violacein production
metabolism
the enzyme is involved in the violacein biosynthetic pathway, which is proposed to consist of the reactions of enzymes VioA -> VioB -> VioE -> VioD -> VioC
metabolism
vioD is one gene encoding violacein biosynthesis, VioD appears to act on late steps of violacein biosynthesis, overview
metabolism
violacein, a natural purple secondary metabolite, is sequentially biosynthesized by five enzymes in the following pathway: VioA-VioB-VioE-VioD-VioC. VioD, a flavin-dependent oxygenase, catalyzes the hydroxylation of the intermediate product prodeoxyviolaceinic acid at the 5-position of one indole ring to yield proviolacein
metabolism
-
the biosynthesis of violacein from 2 molecules of L-tryptophan requires five contiguously encoded proteins VioA-E. VioC and VioD act sequentially, VioD hydroxylates one indole ring at the 5-position to yield proviolacein, and VioC then acts on the other indole ring at the 2-position to create the oxindole and complete violacein formation. the order of hydroxylation on route to violacein is VioD followed by VioC. L-tryptophan, and not 5-hydroxy-L-tryptophan, is the sole precursor to violacein
metabolism
-
biosynthetic pathway of L-tryptophan to violacein in the wild-type and and deoxyviolacein in the vioD deletion mutant, NMR analysis of reactio products and intermediates, overview
metabolism
Chromobacterium violaceum JCM 1249
-
the enzyme is involved in the violacein biosynthetic pathway, which is proposed to consist of the reactions of enzymes VioA -> VioB -> VioE -> VioD -> VioC
metabolism
Chromobacterium violaceum JCM 1249
-
vioD is one gene encoding violacein biosynthesis, VioD appears to act on late steps of violacein biosynthesis, overview
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). VIOD_CHRVO
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
373
0
41623
Swiss-Prot
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, sitting drop vapour diffusion method, mixing of 0.001 ml of 7.5-15 mg/ml protein in 20 mM Tris–HCl pH 8.0, 300 mM NaCl, 10% glycerol, with 0.001 ml of reservoir solution containing 3.5 M sodium formate pH 7.0, and equilibration against 0.05 ml of reservoir solution, 2 weeks, X-ray diffraction structure determination and analysis at 1.7 A resolution, solvent-content calculation and molecular-replacement results suggest the presence of two molecules of VioD in the asymmetric unit
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
additional coexpression of vioC and/or vioD in Streptomyces albus. Disruption of vioA or vioB completely abrogates the biosynthesis of violacein intermediates, while disruption of vioC or vioD results in the production of violacein precursors
additional information
Chromobacterium violaceum JCM 1249
-
additional coexpression of vioC and/or vioD in Streptomyces albus. Disruption of vioA or vioB completely abrogates the biosynthesis of violacein intermediates, while disruption of vioC or vioD results in the production of violacein precursors
additional information
-
deletion of gene vioD from the vioabcde gene cluster and recombinant expression of the modified vioabce gene cluster in Citrobacter freundii strain ACCC 05411, biosynthetic pathway of L-tryptophan to violacein in the wild-type and and deoxyviolacein in the vioD deletion mutant, overview. The absence of gene vioD appears to have no effect on cell growth of Citrobacter freundii compard to the untransfected wild-type
additional information
-
deletion of gene vioD from the vioabcde gene cluster and recombinant expression of the modified vioabce gene cluster in Citrobacter freundii strain ACCC 05411, biosynthetic pathway of L-tryptophan to violacein in the wild-type and and deoxyviolacein in the vioD deletion mutant, overview. The absence of gene vioD appears to have no effect on cell growth of Citrobacter freundii compard to the untransfected wild-type
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography, ultrafiltration, and gel filtration
recombinant His6-tagged enzyme from Escherichia coli strain BL21 (DE3) to homogeneity by nickel affinity chromatography and gel filtration in tandem
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
biosynthetic gene cluster vioABCD, DNA sequencing, transposon mutagenesis, and chemical analysis of the pathway intermediates produced heterologously in Escherichia coli
-
gene vioD, cloned under control of the PTAC promoter and inserted into the fuc locus of Escherichia coli strain BW25113, functional.expression of the vioABCE cluster from Chromobacterium violaceum strain ATCC 12472 under control of the inducible araC system and the vioD gene of Janthinobacterium lividum strain DSM 1522, which enables exclusive production of violacein in Escherichia coli K-12 MG1655 dVio-1
gene vioD, recombinant expression in Escherichia coli strain DH10B and Streptomyces albus strain J1074, coexpression with the other genes of the violacein biosynthesis pathway, reevaluation, overview
gene vioD, recombinant expression of His-tagged enzyme in Escherichia coli
gene vioD, reconstruction of the violacein biosynthesis pathway in Escherichia coli strain BL21 (DE3), recombinant expression of the C-terminally His6-tagged enzyme
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ran, T.; Gao, M.; Wei, Q.; He, J.; Tang, L.; Wang, W.; Xu, D.
Expression, crystallization and preliminary crystallographic data analysis of VioD, a hydroxylase in the violacein-biosynthesis pathway
Acta crystallogr. Sect. F
71
149-152
2015
Chromobacterium violaceum (A0A024AX32)
brenda
Jiang, P.X.; Wang, H.S.; Xiao, S.; Fang, M.Y.; Zhang, R.P.; He, S.Y.; Lou, K.; Xing, X.H.
Pathway redesign for deoxyviolacein biosynthesis in Citrobacter freundii and characterization of this pigment
Appl. Microbiol. Biotechnol.
94
1521-1532
2012
Duganella sp., Duganella sp. B2
brenda
Balibar, C.J.; Walsh, C.T.
In vitro biosynthesis of violacein from L-tryptophan by the enzymes VioA-E from Chromobacterium violaceum
Biochemistry
45
15444-15457
2006
Chromobacterium violaceum (Q9S3U8), Chromobacterium violaceum ATCC 12472 (Q9S3U8)
brenda
Shinoda, K.; Hasegawa, T.; Sato, H.; Shinozaki, M.; Kuramoto, H.; Takamiya, Y.; Sato, T.; Nikaidou, N.; Watanabe, T.; Hoshino, T.
Biosynthesis of violacein: A genuine intermediate, protoviolaceinic acid, produced by VioABDE, and insight into VioC function
Chem. Commun. (Camb.)
2007
4140-4142
2007
Chromobacterium violaceum (Q9S3U8), Chromobacterium violaceum JCM 1249 (Q9S3U8)
brenda
Sanchez, C.; Brana, A.F.; Mendez, C.; Salas, J.A.
Reevaluation of the violacein biosynthetic pathway and its relationship to indolocarbazole biosynthesis
ChemBioChem
7
1231-1240
2006
Chromobacterium violaceum (Q9S3U8), Chromobacterium violaceum JCM 1249 (Q9S3U8)
brenda
August, P.R.; Grossman, T.H.; Minor, C.; Draper, M.P.; MacNeil, I.A.; Pemberton, J.M.; Call, K.M.; Holt, D.; Osburne, M.S.
Sequence analysis and functional characterization of the violacein biosynthetic pathway from Chromobacterium violaceum
J. Mol. Microbiol. Biotechnol.
2
513-519
2000
Chromobacterium violaceum
brenda
Rodrigues, A.L.; Trachtmann, N.; Becker, J.; Lohanatha, A.F.; Blotenberg, J.; Bolten, C.J.; Korneli, C.; de Souza Lima, A.O.; Porto, L.M.; Sprenger, G.A.; Wittmann, C.
Systems metabolic engineering of Escherichia coli for production of the antitumor drugs violacein and deoxyviolacein
Metab. Eng.
20
29-41
2013
Janthinobacterium lividum (A1X1N6), Janthinobacterium lividum DSM 1522 (A1X1N6)
brenda
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EXTERNAL LINKS (specific for EC-Number 1.14.13.217)
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