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Database: UniProt
Entry: A0A0N0GQD2_9NEIS
LinkDB: A0A0N0GQD2_9NEIS
Original site: A0A0N0GQD2_9NEIS 
ID   A0A0N0GQD2_9NEIS        Unreviewed;       511 AA.
AC   A0A0N0GQD2;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=2,4-dichlorophenol 6-monooxygenase {ECO:0000313|EMBL:KPC54573.1};
DE            EC=1.14.13.20 {ECO:0000313|EMBL:KPC54573.1};
GN   Name=tfdB {ECO:0000313|EMBL:KPC54573.1};
GN   ORFNames=WG78_03340 {ECO:0000313|EMBL:KPC54573.1};
OS   Amantichitinum ursilacus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chitinibacteraceae; Amantichitinum.
OX   NCBI_TaxID=857265 {ECO:0000313|EMBL:KPC54573.1, ECO:0000313|Proteomes:UP000037939};
RN   [1] {ECO:0000313|EMBL:KPC54573.1, ECO:0000313|Proteomes:UP000037939}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IGB-41 {ECO:0000313|EMBL:KPC54573.1,
RC   ECO:0000313|Proteomes:UP000037939};
RA   Kirstahler P., Guenther M., Grumaz C., Rupp S., Zibek S., Sohn K.;
RT   "Draft genome sequence of the Amantichitinum ursilacus IGB-41, a new
RT   chitin-degrading bacterium.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00007801}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPC54573.1}.
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DR   EMBL; LAQT01000002; KPC54573.1; -; Genomic_DNA.
DR   RefSeq; WP_053936358.1; NZ_LAQT01000002.1.
DR   AlphaFoldDB; A0A0N0GQD2; -.
DR   STRING; 857265.WG78_03340; -.
DR   PATRIC; fig|857265.3.peg.682; -.
DR   OrthoDB; 3443359at2; -.
DR   Proteomes; UP000037939; Unassembled WGS sequence.
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:SF6; FAD_NAD(P)-BINDING OXIDOREDUCTASE FAMILY PROTEIN; 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:KPC54573.1};
KW   Oxidoreductase {ECO:0000313|EMBL:KPC54573.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037939}.
FT   DOMAIN          4..345
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   511 AA;  55526 MW;  BD355B267EC36404 CRC64;
     MRHVPVLIVG GSLVGLSASL FLRHHGVPHL LIDKHRGSAS HPRAMGFTET TLEHYRACGI
     ADRIPQADPG ARLRRVTVAT LFGDWIAETE WTPGEPAQRS AALSPCTGAA IAQDKLEPIL
     RAAALEAGAE MNLGVELISL IQDDARATAT VRNRNDGAEE IITADWVIAC DGANSTIRDG
     LGISRSGVGH LRTLRSVLFH CPDADAVLDR GAQQFEIKQA GFNAFLTTYG DGRWVLMFDD
     DQERDTDELK EAVLRALGRE LPFEIITTGR WELAGRIADR YREGRVFLAG DAAHQLPPTR
     GGFGANTGID DVWNLSWKLA AVLQGMAADR LLDTYHAERH AIGWLRHQQT FSRPDYAKWA
     PATFKPEPLL ANDAMEFGQL NRSMAVVGAG PELPAAATPK EWAGQPGTRA PHVWEQGASG
     TRSTLDLFGK AYVLLSANRA WIELAQRLQV VSVLVGQDFV FPDEQPFAAV FDIKDAGATL
     VRPDGVIAWR SDAQPDAVAQ DAIDQLIAAR A
//
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