ID A0A220UC30_9MICO Unreviewed; 644 AA.
AC A0A220UC30;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Phenol 2-monooxygenase {ECO:0000313|EMBL:ASK65491.1};
DE EC=1.14.13.7 {ECO:0000313|EMBL:ASK65491.1};
GN ORFNames=CFK39_06205 {ECO:0000313|EMBL:ASK65491.1};
OS Brachybacterium avium.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Brachybacterium.
OX NCBI_TaxID=2017485 {ECO:0000313|EMBL:ASK65491.1, ECO:0000313|Proteomes:UP000198398};
RN [1] {ECO:0000313|Proteomes:UP000198398}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VR2415 {ECO:0000313|Proteomes:UP000198398};
RA Tak E.J., Bae J.-W.;
RT "Brachybacterium sp. VR2415.";
RL Submitted (JUL-2017) 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}.
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DR EMBL; CP022316; ASK65491.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A220UC30; -.
DR KEGG; brv:CFK39_06205; -.
DR OrthoDB; 4246007at2; -.
DR Proteomes; UP000198398; Chromosome.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0018662; F:phenol 2-monooxygenase activity; IEA:UniProtKB-EC.
DR CDD; cd02979; PHOX_C; 1.
DR Gene3D; 3.40.30.20; -; 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 InterPro; IPR012941; Phe_hydrox_C_dim_dom.
DR InterPro; IPR038220; PHOX_C_sf.
DR InterPro; IPR036249; Thioredoxin-like_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; PF07976; Phe_hydrox_dim; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW Monooxygenase {ECO:0000313|EMBL:ASK65491.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ASK65491.1}.
FT DOMAIN 33..405
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 436..603
FT /note="Phenol hydroxylase C-terminal dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07976"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 644 AA; 71217 MW; 781D3383F9107E68 CRC64;
MQFHHHGYLS TEPRVAAAAG TGTERPAELP DTMDVLIVGS GPAGVIAAAQ LSQYPDVHTR
IIERRPGRLE LGQADGIQAR SVETFQAFGF AERITAEAYR ITEMNFWAPD PQNPQNIIRT
SRTDDDVRGV SEFPHLIVNQ ARVLDYYLEA AQRGPARIEP DYGWEFTGEL TVTEGAEHPV
AVTLRRTAGP DEGAERTVRA KYVYGCDGAH SRVRKALGCT MKGDKALHAW GVMDVLYDTD
FPDIRTKCAI QSHDGGSILL IPREGGYLIR LYVDLGTVAE DDGGQVRQTP METVVAKANE
ILHPYTIEVR DVAWSSIYEV GHRLTDRFDD VLPEDRGTRT PRVFIAGDAC HTHSAKAGQG
MNVSMQDGFN LAWKLGQVLT GRSPASLLDT YSAERQVVAK DLIDFDREWS SLMAKKPEEL
GSPDEVAEYY VRTSEFPAGF MTEYADSMIT REGVGQELAT GYPIGKRFKS ERVVRVSDAN
PLHLGHHARA DGRWRIYAFA DSAAPSAADS PLRRWAQWML EALDSPVAVH TPTGADLDAL
FDIKVIYQQG HHEFEVTDAP EIFRSRSGPF QLTDYERVFA TDRRDPELFD PVDIFATRGI
SRDGAVVVVR PDQYVAGIFP LTDTAGLAEF FRGHLLPADG ATAP
//