ID F4G7J3_ALIDK Unreviewed; 587 AA.
AC F4G7J3;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=2,4-dichlorophenol 6-monooxygenase {ECO:0000313|EMBL:AEB86590.1};
DE EC=1.14.13.20 {ECO:0000313|EMBL:AEB86590.1};
GN OrderedLocusNames=Alide2_4275 {ECO:0000313|EMBL:AEB86590.1};
OS Alicycliphilus denitrificans (strain DSM 14773 / CIP 107495 / K601).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Alicycliphilus.
OX NCBI_TaxID=596154 {ECO:0000313|EMBL:AEB86590.1, ECO:0000313|Proteomes:UP000007938};
RN [1] {ECO:0000313|EMBL:AEB86590.1, ECO:0000313|Proteomes:UP000007938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14773 / CIP 107495 / K601
RC {ECO:0000313|Proteomes:UP000007938};
RX PubMed=21742888; DOI=10.1128/JB.00365-11;
RA Oosterkamp M.J., Veuskens T., Plugge C.M., Langenhoff A.A., Gerritse J.,
RA van Berkel W.J., Pieper D.H., Junca H., Goodwin L.A., Daligault H.E.,
RA Bruce D.C., Detter J.C., Tapia R., Han C.S., Land M.L., Hauser L.J.,
RA Smidt H., Stams A.J.;
RT "Genome Sequences of Alicycliphilus denitrificans Strains BC and K601T.";
RL J. Bacteriol. 193:5028-5029(2011).
RN [2] {ECO:0000313|EMBL:AEB86590.1, ECO:0000313|Proteomes:UP000007938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14773 / CIP 107495 / K601
RC {ECO:0000313|Proteomes:UP000007938};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Zeytun A., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Oosterkamp M.,
RA Pieper D., van Berkel W., Langenhoff A., Smidt H., Stams A., Woyke T.;
RT "Complete sequence of chromosome of Alicycliphilus denitrificans K601.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007801}.
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DR EMBL; CP002657; AEB86590.1; -; Genomic_DNA.
DR RefSeq; WP_013723093.1; NC_015422.1.
DR AlphaFoldDB; F4G7J3; -.
DR SMR; F4G7J3; -.
DR STRING; 596154.Alide2_4275; -.
DR KEGG; adk:Alide2_4275; -.
DR eggNOG; COG0654; Bacteria.
DR HOGENOM; CLU_009665_14_0_4; -.
DR OrthoDB; 3443359at2; -.
DR Proteomes; UP000007938; Chromosome.
DR GO; GO:0018666; F:2,4-dichlorophenol 6-monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.40.30.120; -; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR43004:SF8; FAD-BINDING DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR43004; TRK SYSTEM POTASSIUM UPTAKE PROTEIN; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR Pfam; PF21274; Rng_hyd_C; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Monooxygenase {ECO:0000313|EMBL:AEB86590.1};
KW Oxidoreductase {ECO:0000313|EMBL:AEB86590.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007938}.
FT DOMAIN 6..367
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 587 AA; 63677 MW; 40CD59C6F7D7A9F9 CRC64;
MRTIEIPVLV VGAGPAGLSA TCLLATQGVR TLTITRYPGT ANSPRAHITN QRTMEVFRDL
GIEDRMYEVA TPQALMSNNV WATSFAGVEI ARLQAWGSGP ERRVDYELAS PSSMCNLPQH
VMEPVLLAAA RERGGQFLFS TELVAMRQEG DKVVSRLVDR ISGEEIEVVS DWAIGCDGDN
SVVVRELGFE TEGQMNLGAA MNVWLEADLT QYTAHRPGTL YWMTQPGNNY WVGSGTWICV
RPWTEWVLLF MYDPSQGEPD TSEAALIERA QATIGDPSIP VRIKAASKWT INQVVAKSMR
KGRVFIAGNA AHRHPPANGL GTNTCVQDGF NLAWKLAMVI KGQAGDGLLD SYSDERQPVG
ENVVRRAMQS VRDMLPISDA LGFEPGQDEA AGWANVDQLF SNTAHGRERR RKLRDAVALQ
NYQFNCHGVE LGQVYASSAV IGDGSAPPEP ARDPELYYHP STRPGASLPH AWLRQGRRQV
STLDLVGKGR FTLLTGVGGG AWKAAAQGAA EALGIELPVV SIGGPDCDAQ DVYSRWADLA
GIGESGALLV RPDRHVAWRQ QDDAQAGGDA LVQALSQILD QRAPARS
//