VIOB_CHRVO
ID VIOB_CHRVO Reviewed; 998 AA.
AC Q9S3V0; Q9S0N4;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 24-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=2-imino-3-(indol-3-yl)propanoate dimerase {ECO:0000305};
DE EC=1.21.98.- {ECO:0000269|PubMed:17176066, ECO:0000269|PubMed:17925955, ECO:0000303|PubMed:21779844};
DE AltName: Full=Catalase;
DE EC=1.11.1.6 {ECO:0000269|PubMed:17176066, ECO:0000269|PubMed:17925955};
DE AltName: Full=Violacein biosynthesis protein VioB;
GN Name=vioB; OrderedLocusNames=CV_3273;
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).
RN [6]
RP REVIEW.
RX PubMed=21779844; DOI=10.1007/s00253-011-3468-z;
RA Hoshino T.;
RT "Violacein and related tryptophan metabolites produced by Chromobacterium
RT violaceum: biosynthetic mechanism and pathway for construction of violacein
RT core.";
RL Appl. Microbiol. Biotechnol. 91:1463-1475(2011).
CC -!- FUNCTION: Catalyzes the hydrogen peroxide-dependent dimerization of two
CC L-tryptophan-derived molecules (imine form of indole 3-pyruvate (IPA)),
CC to form an uncharacterized product suggested to be indole-3-pyruvate
CC imine dimer that can spontaneously convert into dichlorochromopyrrolate
CC (CPA). The uncharacterized product is the substrate of VioE.
CC {ECO:0000269|PubMed:17176066, ECO:0000269|PubMed:17925955}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6;
CC Evidence={ECO:0000269|PubMed:17176066, ECO:0000269|PubMed:17925955};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-iminio-3-(indol-3-yl)propanoate + H2O2 = 2 H2O + indole-3-
CC pyruvate imine dimer; Xref=Rhea:RHEA:51036, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:59193, ChEBI:CHEBI:133928;
CC Evidence={ECO:0000269|PubMed:17176066, ECO:0000269|PubMed:17925955};
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; AAD51809.1; -; Genomic_DNA.
DR EMBL; AB032799; BAA84783.1; -; Genomic_DNA.
DR EMBL; AE016825; AAQ60937.1; -; Genomic_DNA.
DR RefSeq; WP_011136820.1; NC_005085.1.
DR AlphaFoldDB; Q9S3V0; -.
DR STRING; 243365.CV_3273; -.
DR EnsemblBacteria; AAQ60937; AAQ60937; CV_3273.
DR KEGG; cvi:CV_3273; -.
DR eggNOG; COG1633; Bacteria.
DR HOGENOM; CLU_285727_0_0_4; -.
DR OMA; YMPPTRD; -.
DR OrthoDB; 112739at2; -.
DR BioCyc; MetaCyc:MON-17362; -.
DR UniPathway; UPA00309; -.
DR Proteomes; UP000001424; Chromosome.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1260.10; -; 1.
DR InterPro; IPR012347; Ferritin-like.
DR InterPro; IPR030993; VioB.
DR InterPro; IPR026820; VioB/RebD_dom.
DR Pfam; PF12902; Ferritin-like; 1.
DR TIGRFAMs; TIGR04492; VioB; 1.
PE 1: Evidence at protein level;
KW Antibiotic biosynthesis; Multifunctional enzyme; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..998
FT /note="2-imino-3-(indol-3-yl)propanoate dimerase"
FT /id="PRO_0000065832"
FT CONFLICT 19
FT /note="A -> T (in Ref. 1; AAD51809)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="R -> C (in Ref. 1; AAD51809)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="S -> N (in Ref. 1; AAD51809)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="E -> G (in Ref. 1; AAD51809)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="S -> N (in Ref. 2; BAA84783)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="A -> T (in Ref. 1; AAD51809)"
FT /evidence="ECO:0000305"
FT CONFLICT 826
FT /note="M -> L (in Ref. 1; AAD51809)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 998 AA; 111226 MW; 0AD4558A6A17AC7D CRC64;
MSILDFPRIH FRGWARVNAP TANRDPHGHI DMASNTVAMA GEPFDLARHP TEFHRHLRSL
GPRFGLDGRA DPEGPFSLAE GYNAAGNNHF SWESATVSHV QWDGGEADRG DGLVGARLAL
WGHYNDYLRT TFNRARWVDS DPTRRDAAQI YAGQFTISPA GAGPGTPWLF TADIDDSHGA
RWTRGGHIAE RGGHFLDEEF GLARLFQFSV PKDHPHFLFH PGPFDSEAWR RLQLALEDDD
VLGLTVQYAL FNMSTPPQPN SPVFHDMVGV VGLWRRGELA SYPAGRLLRP RQPGLGDLTL
RVSGGRVALN LACAIPFSTR AAQPSAPDRL TPDLGAKLPL GDLLLRDEDG ALLARVPQAL
YQDYWTNHGI VDLPLLREPR GSLTLSSELA EWREQDWVTQ SDASNLYLEA PDRRHGRFFP
ESIALRSYFR GEARARPDIP HRIEGMGLVG VESRQDGDAA EWRLTGLRPG PARIVLDDGA
EAIPLRVLPD DWALDDATVE EVDYAFLYRH VMAYYELVYP FMSDKVFSLA DRCKCETYAR
LMWQMCDPQN RNKSYYMPST RELSAPKARL FLKYLAHVEG QARLQAPPPA GPARIESKAQ
LAAELRKAVD LELSVMLQYL YAAYSIPNYA QGQQRVRDGA WTAEQLQLAC GSGDRRRDGG
IRAALLEIAH EEMIHYLVVN NLLMALGEPF YAGVPLMGEA ARQAFGLDTE FALEPFSEST
LARFVRLEWP HFIPAPGKSI ADCYAAIRQA FLDLPDLFGG EAGKRGGEHH LFLNELTNRA
HPGYQLEVFD RDSALFGIAF VTDQGEGGAL DSPHYEHSHF QRLREMSARI MAQSAPFEPA
LPALRNPVLD ESPGCQRVAD GRARALMALY QGVYELMFAM MAQHFAVKPL GSLRRSRLMN
AAIDLMTGLL RPLSCALMNL PSGIAGRTAG PPLPGPVDTR SYDDYALGCR MLARRCERLL
EQASMLEPGW LPDAQMELLD FYRRQMLDLA CGKLSREA
