VIOC_CHRVO
ID VIOC_CHRVO Reviewed; 429 AA.
AC Q9S3U9; Q9S0N3;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 24-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Violacein synthase {ECO:0000305};
DE EC=1.14.13.224 {ECO:0000269|PubMed:17176066, ECO:0000269|PubMed:17925955};
GN Name=vioC; OrderedLocusNames=CV_3272;
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 hydroxylation of the 16-position of
CC protoviolaceinate and protodeoxyviolaceinate to form violacein and
CC deoxyviolacein, respectively. {ECO:0000269|PubMed:17176066,
CC ECO:0000269|PubMed:17925955}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + O2 + protoviolaceinate = H2O + NADP(+) +
CC violaceinate; Xref=Rhea:RHEA:49120, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:90898, ChEBI:CHEBI:90900;
CC EC=1.14.13.224; Evidence={ECO:0000269|PubMed:17176066,
CC ECO:0000269|PubMed:17925955};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADH + O2 + protoviolaceinate = H2O + NAD(+) +
CC violaceinate; Xref=Rhea:RHEA:49652, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:90898, ChEBI:CHEBI:90900;
CC EC=1.14.13.224; Evidence={ECO:0000269|PubMed:17176066,
CC ECO:0000269|PubMed:17925955};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + O2 + protodeoxyviolaceinate = deoxyviolaceinate
CC + H2O + NADP(+); Xref=Rhea:RHEA:49116, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:90907, ChEBI:CHEBI:90910;
CC EC=1.14.13.224; Evidence={ECO:0000269|PubMed:17176066,
CC ECO:0000269|PubMed:17925955};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADH + O2 + protodeoxyviolaceinate = deoxyviolaceinate
CC + H2O + NAD(+); Xref=Rhea:RHEA:49668, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:90907, ChEBI:CHEBI:90910;
CC EC=1.14.13.224; 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; AAD51810.1; -; Genomic_DNA.
DR EMBL; AB032799; BAA84784.1; -; Genomic_DNA.
DR EMBL; AE016825; AAQ60936.1; -; Genomic_DNA.
DR RefSeq; WP_011136819.1; NC_005085.1.
DR AlphaFoldDB; Q9S3U9; -.
DR SMR; Q9S3U9; -.
DR STRING; 243365.CV_3272; -.
DR EnsemblBacteria; AAQ60936; AAQ60936; CV_3272.
DR GeneID; 66364494; -.
DR KEGG; cvi:CV_3272; -.
DR eggNOG; COG0654; Bacteria.
DR HOGENOM; CLU_023210_0_1_4; -.
DR OMA; EALHVWP; -.
DR OrthoDB; 504558at2; -.
DR BioCyc; MetaCyc:MON-17365; -.
DR BRENDA; 1.14.13.224; 1370.
DR UniPathway; UPA00309; -.
DR Proteomes; UP000001424; Chromosome.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
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; IPR029058; AB_hydrolase.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Antibiotic biosynthesis; FAD; Flavoprotein; Monooxygenase; NAD; NADP;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..429
FT /note="Violacein synthase"
FT /id="PRO_0000065833"
FT BINDING 3..21
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT CONFLICT 38
FT /note="R -> Q (in Ref. 1; AAD51810)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 429 AA; 47976 MW; CE5CE4FC5641C536 CRC64;
MKRAIIVGGG LAGGLTAIYL AKRGYEVHVV EKRGDPLRDL SSYVDVVSSR AIGVSMTVRG
IKSVLAAGIP RAELDACGEP IVAMAFSVGG QYRMRELKPL EDFRPLSLNR AAFQKLLNKY
ANLAGVRYYF EHKCLDVDLD GKSVLIQGKD GQPQRLQGDM IIGADGAHSA VRQAMQSGLR
RFEFQQTFFR HGYKTLVLPD AQALGYRKDT LYFFGMDSGG LFAGRAATIP DGSVSIAVCL
PYSGSPSLTT TDEPTMRAFF DRYFGGLPRD ARDEMLRQFL AKPSNDLINV RSSTFHYKGN
VLLLGDAAHA TAPFLGQGMN MALEDARTFV ELLDRHQGDQ DKAFPEFTEL RKVQADAMQD
MARANYDVLS CSNPIFFMRA RYTRYMHSKF PGLYPPDMAE KLYFTSEPYD RLQQIQRKQN
VWYKIGRVN
