VIOA_CHRVO
ID VIOA_CHRVO Reviewed; 418 AA.
AC Q9S3V1; Q9S0N5;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 24-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Flavin-dependent L-tryptophan oxidase VioA;
DE EC=1.4.3.23 {ECO:0000269|PubMed:27466367};
GN Name=vioA; OrderedLocusNames=CV_3274;
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 X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH
RP FADH(2) AND INHIBITOR, COFACTOR, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
RP SUBSTRATE SPECIFICITY, AND MUTAGENESIS OF ARG-64; HIS-163; LYS-269;
RP TYR-309; VAL-363 AND TRP-397.
RX PubMed=27466367; DOI=10.1074/jbc.m116.741561;
RA Fuller J.J., Ropke R., Krausze J., Rennhack K.E., Daniel N.P.,
RA Blankenfeldt W., Schulz S., Jahn D., Moser J.;
RT "Biosynthesis of violacein, structure and function of L-tryptophan oxidase
RT VioA from Chromobacterium violaceum.";
RL J. Biol. Chem. 291:20068-20084(2016).
CC -!- FUNCTION: The enzyme generates the imine form of indole 3-pyruvate
CC (IPA) from L-tryptophan (L-Trp), with concomitant two-electron
CC reduction of O(2) to H(2)O(2). {ECO:0000269|PubMed:27466367}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tryptophan + O2 = 2-iminio-3-(indol-3-yl)propanoate + H2O2;
CC Xref=Rhea:RHEA:49024, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57912, ChEBI:CHEBI:59193; EC=1.4.3.23;
CC Evidence={ECO:0000269|PubMed:27466367};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-chloro-L-tryptophan + O2 = 3-(7-chloroindol-3-yl)-2-
CC iminopropanoate + H2O2; Xref=Rhea:RHEA:27302, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:58713, ChEBI:CHEBI:59194; EC=1.4.3.23;
CC Evidence={ECO:0000269|PubMed:27466367};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:27466367};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:27466367};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:27466367};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:27466367};
CC -!- PATHWAY: Pigment biosynthesis; violacein biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:27466367}.
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.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000305}.
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DR EMBL; AF172851; AAD51808.1; -; Genomic_DNA.
DR EMBL; AB032799; BAA84782.1; -; Genomic_DNA.
DR EMBL; AE016825; AAQ60938.1; -; Genomic_DNA.
DR RefSeq; WP_011136821.1; NC_005085.1.
DR PDB; 5G3S; X-ray; 2.08 A; A/B=1-418.
DR PDB; 5G3T; X-ray; 1.80 A; A/B/C/D=1-418.
DR PDB; 5G3U; X-ray; 2.38 A; A/B=1-418.
DR PDB; 5ZBC; X-ray; 2.20 A; A/B=1-418.
DR PDB; 5ZBD; X-ray; 1.80 A; A/B=1-418.
DR PDB; 6ESD; X-ray; 2.60 A; A/B=2-417.
DR PDB; 6FW7; X-ray; 3.00 A; A/B=2-418.
DR PDB; 6FW8; X-ray; 2.40 A; A/B=2-418.
DR PDB; 6FW9; X-ray; 2.74 A; A/B=2-418.
DR PDB; 6FWA; X-ray; 2.85 A; A/B=2-418.
DR PDB; 6G2P; X-ray; 2.60 A; A/B=2-418.
DR PDBsum; 5G3S; -.
DR PDBsum; 5G3T; -.
DR PDBsum; 5G3U; -.
DR PDBsum; 5ZBC; -.
DR PDBsum; 5ZBD; -.
DR PDBsum; 6ESD; -.
DR PDBsum; 6FW7; -.
DR PDBsum; 6FW8; -.
DR PDBsum; 6FW9; -.
DR PDBsum; 6FWA; -.
DR PDBsum; 6G2P; -.
DR AlphaFoldDB; Q9S3V1; -.
DR SMR; Q9S3V1; -.
DR STRING; 243365.CV_3274; -.
DR EnsemblBacteria; AAQ60938; AAQ60938; CV_3274.
DR KEGG; cvi:CV_3274; -.
DR eggNOG; COG1231; Bacteria.
DR HOGENOM; CLU_650243_0_0_4; -.
DR OMA; WMEGGLL; -.
DR OrthoDB; 1442136at2; -.
DR BioCyc; MetaCyc:MON-17361; -.
DR UniPathway; UPA00309; -.
DR Proteomes; UP000001424; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; FAD; Flavoprotein; Magnesium;
KW Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..418
FT /note="Flavin-dependent L-tryptophan oxidase VioA"
FT /id="PRO_0000099880"
FT BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:27466367"
FT BINDING 15
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:27466367"
FT BINDING 16
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:27466367"
FT BINDING 38
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:27466367"
FT BINDING 46
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:27466367"
FT BINDING 64
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:27466367"
FT BINDING 64
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27466367"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27466367"
FT BINDING 208
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:27466367"
FT BINDING 240
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:27466367"
FT BINDING 309
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27466367"
FT BINDING 398
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:27466367"
FT MUTAGEN 64
FT /note="R->Q,S: No activity."
FT /evidence="ECO:0000269|PubMed:27466367"
FT MUTAGEN 163
FT /note="H->A: Almost no effect on activity."
FT /evidence="ECO:0000269|PubMed:27466367"
FT MUTAGEN 163
FT /note="H->N: Retains 8% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:27466367"
FT MUTAGEN 269
FT /note="K->Q,S: Retains less than 2% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:27466367"
FT MUTAGEN 309
FT /note="Y->A: Retains 5% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:27466367"
FT MUTAGEN 363
FT /note="V->A: Retains 50% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:27466367"
FT MUTAGEN 363
FT /note="V->Q: Retains 17% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:27466367"
FT MUTAGEN 397
FT /note="W->A: No activity."
FT /evidence="ECO:0000269|PubMed:27466367"
FT MUTAGEN 397
FT /note="W->Y: Retains 60% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:27466367"
FT CONFLICT 344
FT /note="V -> A (in Ref. 1; AAD51808)"
FT /evidence="ECO:0000305"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:5G3T"
FT HELIX 14..24
FT /evidence="ECO:0007829|PDB:5G3T"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:5G3T"
FT STRAND 34..43
FT /evidence="ECO:0007829|PDB:5G3T"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:5G3T"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:5G3T"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:5G3T"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:5G3T"
FT HELIX 71..79
FT /evidence="ECO:0007829|PDB:5G3T"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:5G3T"
FT HELIX 97..109
FT /evidence="ECO:0007829|PDB:5G3T"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:5G3T"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:5G3T"
FT HELIX 121..129
FT /evidence="ECO:0007829|PDB:5G3T"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:5G3T"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:5G3T"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:6FW7"
FT HELIX 153..161
FT /evidence="ECO:0007829|PDB:5G3T"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:5G3T"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:5G3T"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:5G3T"
FT HELIX 185..197
FT /evidence="ECO:0007829|PDB:5G3T"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:5G3T"
FT STRAND 206..214
FT /evidence="ECO:0007829|PDB:5G3T"
FT STRAND 217..224
FT /evidence="ECO:0007829|PDB:5G3T"
FT STRAND 229..239
FT /evidence="ECO:0007829|PDB:5G3T"
FT HELIX 243..247
FT /evidence="ECO:0007829|PDB:5G3T"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:5G3T"
FT TURN 253..257
FT /evidence="ECO:0007829|PDB:5G3T"
FT STRAND 262..273
FT /evidence="ECO:0007829|PDB:5G3T"
FT HELIX 278..282
FT /evidence="ECO:0007829|PDB:5G3T"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:5G3T"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:6ESD"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:5G3T"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:5G3T"
FT STRAND 305..311
FT /evidence="ECO:0007829|PDB:5G3T"
FT HELIX 312..324
FT /evidence="ECO:0007829|PDB:5G3T"
FT HELIX 326..341
FT /evidence="ECO:0007829|PDB:5G3T"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:5G3T"
FT STRAND 352..366
FT /evidence="ECO:0007829|PDB:5G3T"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:5G3T"
FT TURN 380..382
FT /evidence="ECO:0007829|PDB:5G3T"
FT STRAND 385..387
FT /evidence="ECO:0007829|PDB:5G3T"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:5G3T"
FT TURN 393..396
FT /evidence="ECO:0007829|PDB:5G3T"
FT HELIX 398..417
FT /evidence="ECO:0007829|PDB:5G3T"
SQ SEQUENCE 418 AA; 46748 MW; E2D07C8AC28133D3 CRC64;
MKHSSDICIV GAGISGLTCA SHLLDSPACR GLSLRIFDMQ QEAGGRIRSK MLDGKASIEL
GAGRYSPQLH PHFQSAMQHY SQKSEVYPFT QLKFKSHVQQ KLKRAMNELS PRLKEHGKES
FLQFVSRYQG HDSAVGMIRS MGYDALFLPD ISAEMAYDIV GKHPEIQSVT DNDANQWFAA
ETGFAGLIQG IKAKVKAAGA RFSLGYRLLS VRTDGDGYLL QLAGDDGWKL EHRTRHLILA
IPPSAMAGLN VDFPEAWSGA RYGSLPLFKG FLTYGEPWWL DYKLDDQVLI VDNPLRKIYF
KGDKYLFFYT DSEMANYWRG CVAEGEDGYL EQIRTHLASA LGIVRERIPQ PLAHVHKYWA
HGVEFCRDSD IDHPSALSHR DSGIIACSDA YTEHCGWMEG GLLSAREASR LLLQRIAA
