ID T5A7T0_OPHSC Unreviewed; 646 AA.
AC T5A7T0;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Phenol 2-monooxygenase {ECO:0000313|EMBL:EQK97801.1};
GN ORFNames=OCS_06487 {ECO:0000313|EMBL:EQK97801.1};
OS Ophiocordyceps sinensis (strain Co18 / CGMCC 3.14243) (Yarsagumba
OS caterpillar fungus) (Hirsutella sinensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=911162 {ECO:0000313|EMBL:EQK97801.1, ECO:0000313|Proteomes:UP000019374};
RN [1] {ECO:0000313|EMBL:EQK97801.1, ECO:0000313|Proteomes:UP000019374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Co18 / CGMCC 3.14243 {ECO:0000313|Proteomes:UP000019374};
RC TISSUE=Fruit-body {ECO:0000313|EMBL:EQK97801.1};
RX DOI=10.1007/s11434-013-5929-5;
RA Hu X., Zhang Y., Xiao G., Zheng P., Xia Y., Zhang X., St Leger R.J.,
RA Liu X., Wang C.;
RT "Genome survey uncovers the secrets of sex and lifestyle in caterpillar
RT fungus.";
RL Chin. Sci. Bull. 58:2846-2854(2013).
CC -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007801}.
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DR EMBL; KE656598; EQK97801.1; -; Genomic_DNA.
DR AlphaFoldDB; T5A7T0; -.
DR eggNOG; KOG3855; Eukaryota.
DR HOGENOM; CLU_009665_9_3_1; -.
DR Proteomes; UP000019374; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase 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 Monooxygenase {ECO:0000313|EMBL:EQK97801.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000019374}.
FT DOMAIN 50..389
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 415..580
FT /note="Phenol hydroxylase C-terminal dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07976"
SQ SEQUENCE 646 AA; 71560 MW; 817BB19324C5D259 CRC64;
MVPGILDGSS ALDAPLVDVE HQLAPVDEDQ EMDAVADLTM LRSFPEPPLE CQVCVVGAGP
AGLMLAATLT RCGIHVEVVD DRADQTPTAA PGRHSAPTWC PRLRHLLLAP PAEEPLHRLG
REVHYPPIID VLDPYILLVH QGIVESLFID DMKKRGKDVR RNTAYDSYDY AAGKSGQLQV
NCRVNVTHDK RTIMAQYLVG CDGAHSKVRK SIPDVEAVGM SQAAIWGVLD GELITDFPDI
WSKTLVYSEE YGSILIIPRE RNMTRFYIEL KACTSTDRRQ LGQSFVMQQA RKIMAPFSID
WRYIEWFGRY QVGQRVASRF ADAKTRVFLS GDASHTHSPK AAQGMNTSMH DSWNLSWKLN
LAVRGLAKPE LLESYEEERR KIALDLVNFD YEHANQIAGG DAVALAKNFK ANVRFISGIG
AEYDDSSINR ADLSDGPPPV GDARPGCLLP PAKVTRYIDS NPVDVQLDIP MLGQFRIFLL
MWDVQQAAPF LTTFCRAIAD AGSFVSQLSA AASTSYAAQP RLGSPEDVYI RPERYTAVSH
LFTFALITTM AKAEIEISDL PAMLQDSRWT MYLDDIPEKD TRGQLCTDKW LGSLEPGDVA
IVNVRPDGYV GSVCRWDSSV DDAGVEAARW VDDYYGGFMR IPTATA
//
