ID A0A061H7J1_9BASI Unreviewed; 749 AA.
AC A0A061H7J1;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Phenol 2-monooxygenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PFL1_04307 {ECO:0000313|EMBL:EPQ27980.1};
OS Pseudozyma flocculosa PF-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ27980.1, ECO:0000313|Proteomes:UP000053664};
RN [1] {ECO:0000313|EMBL:EPQ27980.1, ECO:0000313|Proteomes:UP000053664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF-1 {ECO:0000313|EMBL:EPQ27980.1,
RC ECO:0000313|Proteomes:UP000053664};
RX PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA Bakkeren G., Belanger R.R.;
RT "The transition from a phytopathogenic smut ancestor to an anamorphic
RT biocontrol agent deciphered by comparative whole-genome analysis.";
RL Plant Cell 25:1946-1959(2013).
CC -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007801}.
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DR EMBL; KE361636; EPQ27980.1; -; Genomic_DNA.
DR RefSeq; XP_007880024.1; XM_007881833.1.
DR AlphaFoldDB; A0A061H7J1; -.
DR GeneID; 19318412; -.
DR KEGG; pfp:PFL1_04307; -.
DR eggNOG; KOG3855; Eukaryota.
DR HOGENOM; CLU_009665_9_2_1; -.
DR OrthoDB; 1386239at2759; -.
DR Proteomes; UP000053664; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
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:SF20; 2-MONOOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G13660)-RELATED; 1.
DR PANTHER; PTHR43004; TRK SYSTEM POTASSIUM UPTAKE PROTEIN; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR Pfam; PF07976; Phe_hydrox_dim; 2.
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:UP000053664}.
FT DOMAIN 16..431
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 470..626
FT /note="Phenol hydroxylase C-terminal dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07976"
FT DOMAIN 645..676
FT /note="Phenol hydroxylase C-terminal dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07976"
FT REGION 175..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 749 AA; 81964 MW; 902DBF3ADBD30031 CRC64;
MPAPPTPTPA ATHSKVDLLI IGAGPAGLMA ANWAVSLGCR SVRVVDKRNT KIFTGQADGL
QCRTLEVLHS FGMAQDIVRQ SNHMLEVCFW NPVDGTLRRT GRIPDTIPGI SRWQQVVLHQ
GRIERAFLDR IHAQSHGEVQ VERAKLPERL DVDTDLVEST HPDVYPVRVQ VRQLSEDEAT
PSQMGKSTPN GLFRSALAPD DTPELLSSSS SSVSGTKAGA VGSRQVIHAK YVIGCDGAHS
WTRKQMGIDM AGEQTDYIWG VLDAVPVTDF PDIRMRCAIH SANDGSVMII PREDGLVRFY
IQISSTSDGA ADAATKVDRH NITWQRILKA AQTIIKPYRL EISERDLHWW TAYQIGQRVA
SGFSLHDRVF IAGDACHTHS PKAGQGMNVS MMDTYNLVWK VAKVLQRQSP RSILPTYQAE
RRRVAQELIA FDHRFSRLFS GKPQAAEDAA REAGVDLAEF RNVFAKGNRF ASGTAVEYGP
SLLVGRGGDA TELGDGTDVV GPGALSRPEL SAEGCGESRI VVGQRLNTAQ VVCVADARPW
QLVDWLPSDG RWRLLLFCGN LVDAAQRPRI EAFARYLETQ LLPRYTPARH DVDSVIDCLT
ISSTPRTACE LSDYPAILHP LTTKWHRPGS ASAAAGDVGE ARAKSQDYWK IFCDDESYHA
GHGRAYEKYG IDAQRGAVVV ARPDGYVSLL VALDDVDRID AFFDKCMLPA EMHLPFASRD
KPSGAVDGAE TKGVPPVPSK EAGEVAQAL
//
