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Protein

Flavin-dependent L-tryptophan oxidase VioA

Gene

vioA

Organism
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

The enzyme generates the imine form of indole 3-pyruvate (IPA) from L-tryptophan (L-Trp), with concomitant two-electron reduction of O2 to H2O2.1 Publication

Catalytic activityi

L-tryptophan + O2 = 2-iminoindole pyruvate + H2O2.1 Publication
7-chloro-L-tryptophan + O2 = 2-imino-3-(7-chloroindol-3-yl)propanoate + H2O2.1 Publication

Cofactori

Protein has several cofactor binding sites:

Pathwayi: violacein biosynthesis

This protein is involved in the pathway violacein biosynthesis, which is part of Pigment biosynthesis.
View all proteins of this organism that are known to be involved in the pathway violacein biosynthesis and in Pigment biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi13Magnesium; via amide nitrogen1 Publication1
Binding sitei15FAD1 Publication1
Metal bindingi16Magnesium; via amide nitrogen1 Publication1
Binding sitei38FAD1 Publication1
Binding sitei46FAD1 Publication1
Binding sitei64FAD1 Publication1
Binding sitei64Substrate1 Publication1
Binding sitei163Substrate; via tele nitrogen1 Publication1
Binding sitei208FAD; via amide nitrogen and carbonyl oxygen1 Publication1
Metal bindingi240Magnesium; via amide nitrogen1 Publication1
Binding sitei309Substrate1 Publication1
Binding sitei398FAD; via amide nitrogen1 Publication1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processAntibiotic biosynthesis
LigandFAD, Flavoprotein, Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciCVIO243365:G1G08-3290-MONOMER
MetaCyc:MONOMER-17361
UniPathwayiUPA00309

Names & Taxonomyi

Protein namesi
Recommended name:
Flavin-dependent L-tryptophan oxidase VioA (EC:1.4.3.231 Publication)
Gene namesi
Name:vioA
Ordered Locus Names:CV_3274
OrganismiChromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Taxonomic identifieri243365 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesChromobacteriaceaeChromobacterium
Proteomesi
  • UP000001424 Componenti: Chromosome

Pathology & Biotechi

Biotechnological usei

Violacein production is used as a biosensor for the detection of quorum-sensing AHL production. Violacein possesses antibacterial, antiviral, antimicrobial, antileishmanial, trypanocidal and potential antitumoral activities.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi64R → Q or S: No activity. 1 Publication1
Mutagenesisi163H → A: Almost no effect on activity. 1 Publication1
Mutagenesisi163H → N: Retains 8% of wild-type activity. 1 Publication1
Mutagenesisi269K → Q or S: Retains less than 2% of wild-type activity. 1 Publication1
Mutagenesisi309Y → A: Retains 5% of wild-type activity. 1 Publication1
Mutagenesisi363V → A: Retains 50% of wild-type activity. 1 Publication1
Mutagenesisi363V → Q: Retains 17% of wild-type activity. 1 Publication1
Mutagenesisi397W → A: No activity. 1 Publication1
Mutagenesisi397W → Y: Retains 60% of wild-type activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000998801 – 418Flavin-dependent L-tryptophan oxidase VioAAdd BLAST418

Expressioni

Inductioni

By N-acylhomoserine lactone (AHL).

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi243365.CV_3274

Structurei

Secondary structure

1418
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 10Combined sources7
Helixi14 – 24Combined sources11
Helixi27 – 29Combined sources3
Beta strandi34 – 43Combined sources10
Beta strandi49 – 52Combined sources4
Turni53 – 55Combined sources3
Beta strandi56 – 61Combined sources6
Turni67 – 69Combined sources3
Helixi71 – 79Combined sources9
Beta strandi84 – 86Combined sources3
Helixi97 – 109Combined sources13
Helixi110 – 112Combined sources3
Helixi113 – 116Combined sources4
Helixi121 – 129Combined sources9
Helixi131 – 139Combined sources9
Helixi144 – 147Combined sources4
Helixi153 – 161Combined sources9
Turni164 – 166Combined sources3
Helixi167 – 170Combined sources4
Beta strandi178 – 182Combined sources5
Helixi185 – 197Combined sources13
Beta strandi201 – 204Combined sources4
Beta strandi206 – 214Combined sources9
Beta strandi217 – 224Combined sources8
Beta strandi229 – 239Combined sources11
Helixi243 – 247Combined sources5
Beta strandi249 – 251Combined sources3
Turni253 – 257Combined sources5
Beta strandi262 – 273Combined sources12
Helixi278 – 282Combined sources5
Beta strandi288 – 290Combined sources3
Beta strandi292 – 295Combined sources4
Beta strandi297 – 301Combined sources5
Turni302 – 304Combined sources3
Beta strandi305 – 311Combined sources7
Helixi312 – 324Combined sources13
Helixi326 – 341Combined sources16
Helixi345 – 347Combined sources3
Beta strandi352 – 366Combined sources15
Beta strandi375 – 378Combined sources4
Turni380 – 382Combined sources3
Beta strandi385 – 387Combined sources3
Helixi389 – 391Combined sources3
Turni393 – 396Combined sources4
Helixi398 – 417Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5G3SX-ray2.08A/B1-418[»]
5G3TX-ray1.80A/B/C/D1-418[»]
5G3UX-ray2.38A/B1-418[»]
6ESDX-ray2.60A/B2-417[»]
6ESEX-ray2.60A/B2-418[»]
ProteinModelPortaliQ9S3V1
SMRiQ9S3V1
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the flavin monoamine oxidase family.Curated

Phylogenomic databases

eggNOGiENOG4108173 Bacteria
ENOG410ZIW7 LUCA
KOiK20086
OMAiWMEGGLL
OrthoDBiPOG091H0GKA

Family and domain databases

Gene3Di3.50.50.60, 1 hit
InterProiView protein in InterPro
IPR002937 Amino_oxidase
IPR036188 FAD/NAD-bd_sf
PfamiView protein in Pfam
PF01593 Amino_oxidase, 1 hit
SUPFAMiSSF51905 SSF51905, 2 hits

Sequencei

Sequence statusi: Complete.

Q9S3V1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKHSSDICIV GAGISGLTCA SHLLDSPACR GLSLRIFDMQ QEAGGRIRSK
60 70 80 90 100
MLDGKASIEL GAGRYSPQLH PHFQSAMQHY SQKSEVYPFT QLKFKSHVQQ
110 120 130 140 150
KLKRAMNELS PRLKEHGKES FLQFVSRYQG HDSAVGMIRS MGYDALFLPD
160 170 180 190 200
ISAEMAYDIV GKHPEIQSVT DNDANQWFAA ETGFAGLIQG IKAKVKAAGA
210 220 230 240 250
RFSLGYRLLS VRTDGDGYLL QLAGDDGWKL EHRTRHLILA IPPSAMAGLN
260 270 280 290 300
VDFPEAWSGA RYGSLPLFKG FLTYGEPWWL DYKLDDQVLI VDNPLRKIYF
310 320 330 340 350
KGDKYLFFYT DSEMANYWRG CVAEGEDGYL EQIRTHLASA LGIVRERIPQ
360 370 380 390 400
PLAHVHKYWA HGVEFCRDSD IDHPSALSHR DSGIIACSDA YTEHCGWMEG
410
GLLSAREASR LLLQRIAA
Length:418
Mass (Da):46,748
Last modified:October 24, 2003 - v2
Checksum:iE2D07C8AC28133D3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti344V → A in AAD51808 (PubMed:11075927).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF172851 Genomic DNA Translation: AAD51808.1
AB032799 Genomic DNA Translation: BAA84782.1
AE016825 Genomic DNA Translation: AAQ60938.1
RefSeqiWP_011136821.1, NC_005085.1

Genome annotation databases

EnsemblBacteriaiAAQ60938; AAQ60938; CV_3274
GeneIDi24947400
KEGGicvi:CV_3274

Similar proteinsi

Entry informationi

Entry nameiVIOA_CHRVO
AccessioniPrimary (citable) accession number: Q9S3V1
Secondary accession number(s): Q9S0N5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: October 24, 2003
Last modified: June 20, 2018
This is version 92 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

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