VIOD_CHRVO
ID VIOD_CHRVO Reviewed; 373 AA.
AC Q9S3U8; Q9S0N2;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 24-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Protodeoxyviolaceinate monooxygenase {ECO:0000305};
DE EC=1.14.13.217 {ECO:0000269|PubMed:17176066, ECO:0000269|PubMed:17925955};
GN Name=vioD; OrderedLocusNames=CV_3271;
OS Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC
OS 12614 / NCIMB 9131 / NCTC 9757).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Chromobacterium.
OX NCBI_TaxID=243365;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=UQM51;
RX PubMed=11075927;
RA August P.R., Grossman T.H., Minor C., Draper M.P., MacNeil I.A.,
RA Pemberton J.M., Call K.M., Holt D., Osburne M.S.;
RT "Sequence analysis and functional characterization of the violacein
RT biosynthetic pathway from Chromobacterium violaceum.";
RL J. Mol. Microbiol. Biotechnol. 2:513-519(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC
RC 9757;
RA Hoshino T.;
RT "Biosynthetic gene cluster for violacein pigment.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC
RC 9757;
RX PubMed=14500782; DOI=10.1073/pnas.1832124100;
RA Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T.,
RA Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R.,
RA Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F.,
RA Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S.,
RA Belo A., van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M.,
RA Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P.,
RA Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S.,
RA Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N.,
RA Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P.,
RA Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R.,
RA Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B.,
RA Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J.,
RA Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F.,
RA Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z.,
RA de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F.,
RA Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A.,
RA Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C.,
RA Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M.,
RA Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C.,
RA Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R.,
RA Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M.,
RA Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R.,
RA Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.;
RT "The complete genome sequence of Chromobacterium violaceum reveals
RT remarkable and exploitable bacterial adaptability.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC
RC 9757;
RX PubMed=17176066; DOI=10.1021/bi061998z;
RA Balibar C.J., Walsh C.T.;
RT "In vitro biosynthesis of violacein from L-tryptophan by the enzymes VioA-E
RT from Chromobacterium violaceum.";
RL Biochemistry 45:15444-15457(2006).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC
RC 9757;
RX PubMed=17925955; DOI=10.1039/b705358d;
RA Shinoda K., Hasegawa T., Sato H., Shinozaki M., Kuramoto H., Takamiya Y.,
RA Sato T., Nikaidou N., Watanabe T., Hoshino T.;
RT "Biosynthesis of violacein: a genuine intermediate, protoviolaceinic acid,
RT produced by VioABDE, and insight into VioC function.";
RL Chem. Commun. (Camb.) 2007:4140-4142(2007).
CC -!- FUNCTION: Catalyzes the oxygenation of the 6-position of
CC protodeoxyviolaceinate to form proviolacein.
CC {ECO:0000269|PubMed:17176066, ECO:0000269|PubMed:17925955}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADH + O2 + protodeoxyviolaceinate = H2O + NAD(+) +
CC protoviolaceinate; Xref=Rhea:RHEA:49372, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:90898, ChEBI:CHEBI:90907;
CC EC=1.14.13.217; Evidence={ECO:0000269|PubMed:17176066,
CC ECO:0000269|PubMed:17925955};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + O2 + protodeoxyviolaceinate = H2O + NADP(+) +
CC protoviolaceinate; Xref=Rhea:RHEA:49124, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:90898, ChEBI:CHEBI:90907;
CC EC=1.14.13.217; Evidence={ECO:0000269|PubMed:17176066,
CC ECO:0000269|PubMed:17925955};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- PATHWAY: Pigment biosynthesis; violacein biosynthesis.
CC -!- INDUCTION: By N-acylhomoserine lactone (AHL).
CC -!- BIOTECHNOLOGY: Violacein production is used as a biosensor for the
CC detection of quorum-sensing AHL production. Violacein possesses
CC antibacterial, antiviral, antimicrobial, antileishmanial, trypanocidal
CC and potential antitumoral activities.
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DR EMBL; AF172851; AAD51811.1; -; Genomic_DNA.
DR EMBL; AB032799; BAA84785.1; -; Genomic_DNA.
DR EMBL; AE016825; AAQ60935.1; -; Genomic_DNA.
DR RefSeq; WP_011136818.1; NC_005085.1.
DR PDB; 3C4A; X-ray; 2.30 A; A=1-373.
DR PDBsum; 3C4A; -.
DR AlphaFoldDB; Q9S3U8; -.
DR SMR; Q9S3U8; -.
DR STRING; 243365.CV_3271; -.
DR EnsemblBacteria; AAQ60935; AAQ60935; CV_3271.
DR KEGG; cvi:CV_3271; -.
DR eggNOG; COG0654; Bacteria.
DR HOGENOM; CLU_027335_1_0_4; -.
DR OMA; TTHYSIG; -.
DR OrthoDB; 1033671at2; -.
DR BioCyc; MetaCyc:MON-17366; -.
DR BRENDA; 1.14.13.217; 1370.
DR UniPathway; UPA00309; -.
DR EvolutionaryTrace; Q9S3U8; -.
DR Proteomes; UP000001424; Chromosome.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; FAD; Flavoprotein; Monooxygenase;
KW NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..373
FT /note="Protodeoxyviolaceinate monooxygenase"
FT /id="PRO_0000065834"
FT BINDING 2..20
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT CONFLICT 31
FT /note="V -> I (in Ref. 1; AAD51811)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="V -> A (in Ref. 1; AAD51811)"
FT /evidence="ECO:0000305"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:3C4A"
FT HELIX 10..22
FT /evidence="ECO:0007829|PDB:3C4A"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:3C4A"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:3C4A"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:3C4A"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:3C4A"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:3C4A"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:3C4A"
FT STRAND 75..85
FT /evidence="ECO:0007829|PDB:3C4A"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:3C4A"
FT HELIX 97..110
FT /evidence="ECO:0007829|PDB:3C4A"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:3C4A"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:3C4A"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:3C4A"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:3C4A"
FT HELIX 140..144
FT /evidence="ECO:0007829|PDB:3C4A"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:3C4A"
FT STRAND 157..170
FT /evidence="ECO:0007829|PDB:3C4A"
FT STRAND 173..182
FT /evidence="ECO:0007829|PDB:3C4A"
FT STRAND 185..193
FT /evidence="ECO:0007829|PDB:3C4A"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:3C4A"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:3C4A"
FT HELIX 207..212
FT /evidence="ECO:0007829|PDB:3C4A"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:3C4A"
FT HELIX 220..230
FT /evidence="ECO:0007829|PDB:3C4A"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:3C4A"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:3C4A"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:3C4A"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:3C4A"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:3C4A"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:3C4A"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:3C4A"
FT HELIX 281..298
FT /evidence="ECO:0007829|PDB:3C4A"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:3C4A"
FT HELIX 302..332
FT /evidence="ECO:0007829|PDB:3C4A"
FT HELIX 345..348
FT /evidence="ECO:0007829|PDB:3C4A"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:3C4A"
FT TURN 352..355
FT /evidence="ECO:0007829|PDB:3C4A"
FT HELIX 359..370
FT /evidence="ECO:0007829|PDB:3C4A"
SQ SEQUENCE 373 AA; 41623 MW; 64205F8BCED4BC25 CRC64;
MKILVIGAGP AGLVFASQLK QARPLWAIDI VEKNDEQEVL GWGVVLPGRP GQHPANPLSY
LDAPERLNPQ FLEDFKLVHH NEPSLMSTGV LLCGVERRGL VHALRDKCRS QGIAIRFESP
LLEHGELPLA DYDLVVLANG VNHKTAHFTE ALVPQVDYGR NKYIWYGTSQ LFDQMNLVFR
THGKDIFIAH AYKYSDTMST FIVECSEETY ARARLGEMSE EASAEYVAKV FQAELGGHGL
VSQPGLGWRN FMTLSHDRCH DGKLVLLGDA LQSGHFSIGH GTTMAVVVAQ LLVKALCTED
GVPAALKRFE ERALPLVQLF RGHADNSRVW FETVEERMHL SSAEFVQSFD ARRKSLPPMP
EALAQNLRYA LQR
