ID G4U601_NEUT9 Unreviewed; 656 AA.
AC G4U601;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Phenol 2-monooxygenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=NEUTE2DRAFT_98322 {ECO:0000313|EMBL:EGZ76465.1};
OS Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ76465.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ76465.1, ECO:0000313|Proteomes:UP000008513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Genetics 189:55-69(2011).
CC -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007801}.
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DR EMBL; GL890999; EGZ76465.1; -; Genomic_DNA.
DR AlphaFoldDB; G4U601; -.
DR STRING; 510952.G4U601; -.
DR eggNOG; KOG3855; Eukaryota.
DR HOGENOM; CLU_009665_9_3_1; -.
DR Proteomes; UP000008513; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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:SF4; FAD_BINDING_3 DOMAIN-CONTAINING 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 FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008513}.
FT DOMAIN 44..399
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 425..585
FT /note="Phenol hydroxylase C-terminal dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07976"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 656 AA; 73471 MW; 6E8D118BA3507228 CRC64;
MAPGVLEKPA EEQQGGDLHM TNAADDSCVD RLTLLRSMPE PPVECQVCVV GAGPAGLMLA
CNLGRFGVKV EVVDDRADQT PVGRADGLQP KTIETFRQMR LADPLLQRGV RVYDIAFWRS
TTDEPLHRLG REIHYPPIID VLDPYILLVH QGMVESLFIE DLKKRGVEVR RNTAFDSYSV
CDGNNGPLQV NCLANVTQDR KTILTQYLVG CDGAHSKVRK SIPDAKPIGL SQPSLWGVLD
GELDTDFPDI WSKTLVYSQE HGSILIIPRE RNMTRFYIEL KSSTKGDRNM LGQEFVMQRA
REIMAPFSVK WKYIEWFGRY QIGQRVANRF QDPHTRAFLA GDASHTHSPK AAQGMNTSMH
DAWNIGWKLN FAARGLAKPA LLESYEQERR KIALDLVNFD YEHANQIAGG DAVALAENFK
TNVRFISGIG AEYGENAINM VEPQSWVMGD AKPGCLLPPA KVTRYLDSNP VDVQLDIPML
GQFRIYLLMW DVHQSRIFLD GFCAALNSPD SLMNQLSAAA NISYAKQPRL PAPEDIYLRP
ERYTAVSHLF TFGLITTMPK SEIEITDLPA LFQDSRWTFY LDDIPELDTR GQLCTNKWLG
SLGPGEVAIV NVRPDGYVGS IGRWDSSVDD AGEEAAKWLD TYYDRFLQVP PSPAMD
//
