ID H0EEI8_GLAL7 Unreviewed; 379 AA.
AC H0EEI8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Putative Phenol 2-monooxygenase {ECO:0000313|EMBL:EHL02901.1};
GN ORFNames=M7I_0866 {ECO:0000313|EMBL:EHL02901.1};
OS Glarea lozoyensis (strain ATCC 74030 / MF5533).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1104152 {ECO:0000313|EMBL:EHL02901.1, ECO:0000313|Proteomes:UP000005446};
RN [1] {ECO:0000313|EMBL:EHL02901.1, ECO:0000313|Proteomes:UP000005446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 74030 / MF5533 {ECO:0000313|Proteomes:UP000005446};
RX PubMed=22302591; DOI=10.1128/EC.05302-11;
RA Youssar L., Gruening B.A., Erxleben A., Guenther S., Huettel W.;
RT "Genome sequence of the fungus Glarea lozoyensis: the first genome sequence
RT of a species from the Helotiaceae family.";
RL Eukaryot. Cell 11:250-250(2012).
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:EHL02901.1}.
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DR EMBL; AGUE01000016; EHL02901.1; -; Genomic_DNA.
DR AlphaFoldDB; H0EEI8; -.
DR HOGENOM; CLU_009665_9_0_1; -.
DR InParanoid; H0EEI8; -.
DR Proteomes; UP000005446; 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: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; 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:EHL02901.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000005446}.
FT DOMAIN 20..126
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 163..344
FT /note="Phenol hydroxylase C-terminal dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07976"
SQ SEQUENCE 379 AA; 42419 MW; A0BA50CC2D4D974D CRC64;
MTTTEKGGGK PLKVDRSNIT PQMILECAQK TIAPYKLTYN YCDWWTAYQI GQRICPSFSA
NERIFLAGDA VHTHSPKAGQ GMNVSMQDTY NLGWKIASVL KGTAHRSILK TYQSERHRIA
QDLIDFDHKF SRLFSGRPAK DVMDEAGISM SEFKSAFEKG NLFASGVAVD YGASILVAKE
GNPQDGANGT NIGISASSVH GKPEVAKNIK MGMRFPSFQV LNQADARPWQ FQERLKSDGR
WRLILFAGNI SNPPQMTRIT NLCANLSPII KRYTPAAQPI DSRIEILTLH SAPRASTELF
SFPELLRPLS DEGWDYWKIF VDDESYHEGH GRAYEGYGAD AERGCLVVVR PDGYVGWEGE
IEDIEDIGRY FEGFMVVQR
//
