ID W9YJ74_9EURO Unreviewed; 812 AA.
AC W9YJ74;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Phenol 2-monooxygenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A1O3_01483 {ECO:0000313|EMBL:EXJ92927.1};
OS Capronia epimyces CBS 606.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182542 {ECO:0000313|EMBL:EXJ92927.1, ECO:0000313|Proteomes:UP000019478};
RN [1] {ECO:0000313|EMBL:EXJ92927.1, ECO:0000313|Proteomes:UP000019478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ92927.1,
RC ECO:0000313|Proteomes:UP000019478};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia epimyces CBS 606.96.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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:EXJ92927.1}.
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DR EMBL; AMGY01000001; EXJ92927.1; -; Genomic_DNA.
DR RefSeq; XP_007729817.1; XM_007731627.1.
DR AlphaFoldDB; W9YJ74; -.
DR STRING; 1182542.W9YJ74; -.
DR GeneID; 19165617; -.
DR eggNOG; KOG3855; Eukaryota.
DR HOGENOM; CLU_009665_9_2_1; -.
DR OrthoDB; 1386239at2759; -.
DR Proteomes; UP000019478; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 2.
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:SF10; 2-MONOOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G11480)-RELATED; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000019478};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 71..92
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 69..475
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 605..772
FT /note="Phenol hydroxylase C-terminal dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07976"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 812 AA; 89490 MW; 2E9B37CB6EFD9662 CRC64;
MAEQEFGRES DRESDHDRDS KREGQPALEG QPERQAEHEA EHEDEGESRP EHEGQGTRQQ
QQQQKPEHVD VLICGAGSAG LCAALWLAIY GIRSVKILER RAGPLTMGQA DGVQCRTVEV
FESFGLAEEV LREAYHVLEV AFWAPGPAPD DTTRTRTNTA YEGINQDPTN TAHEGINQDP
TRTTTTTTTT TTLRRTSRAA DTQPGLSHLP HVILNQARIN GLMLDKMRGL GGHDVAYGYT
VKSVAVDVDV DADTNIDTNI DTNIDTDTHN TLATSESDPT AYPCSVVAEK DGQEELFRAK
YVLGCDGAHS MVRKSLGFKM VGDTTDAVWA VMDVYARTNF PDIRRKATIH SHAGTVLVIP
REGGSLVRLY IEFPAGTTVE SIQLSDVHAK AGQIFAPFEL DIAQTAWWSC YCIGQRLADR
FSLLNRVFLT GDAFHTHSPK AGQGMNVSLQ DGYNIGWKLG MVLKAGNDQD QDQTQTQAQA
RSCSRAHARA RARPNRLLST YTLERGRTAA DLIDFDRWFT KLFSRKTSVG NHHHQPGTGT
GTVADTNAVA VTDDVAGTGT GTRTGTRTVA DADADADKGT EPEHDGETAW TPEQFSQHFI
RAGRYTAGLT AKYEDSSITS CATSKQELAQ NILVGMRFPS AQVVRFCDAK AMPLVQALRA
DGRWRLVFFA GTIGHPHTLP RLQKMANYLD SPAGPVRRYT PSSSDVDSFL EPIVVLAGER
VKLEQEDIPL FFWPVTGKWK MRDLHKIFID DESYNSGHGH AYEKYAIDPE IGATVIVRPD
QYVSKVLSID DTLGIGELFD QFMVPEVQNR SL
//
