ID A0A0M9VXD9_9HYPO Unreviewed; 473 AA.
AC A0A0M9VXD9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=6-hydroxy-D-nicotine oxidase {ECO:0000313|EMBL:KOS23055.1};
GN ORFNames=ESCO_003776 {ECO:0000313|EMBL:KOS23055.1};
OS Escovopsis weberi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Escovopsis.
OX NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS23055.1, ECO:0000313|Proteomes:UP000053831};
RN [1] {ECO:0000313|EMBL:KOS23055.1, ECO:0000313|Proteomes:UP000053831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA Currie C., Gerardo N.M.;
RT "The genome of the fungus Escovopsis weberi, a specialized disease agent of
RT ant agriculture.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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:KOS23055.1}.
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DR EMBL; LGSR01000002; KOS23055.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M9VXD9; -.
DR STRING; 150374.A0A0M9VXD9; -.
DR OrthoDB; 1641938at2759; -.
DR Proteomes; UP000053831; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.465.10; -; 3.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR13878; GULONOLACTONE OXIDASE; 1.
DR PANTHER; PTHR13878:SF91; L-GULONOLACTONE OXIDASE 3; 1.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000053831}.
FT DOMAIN 23..245
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 473 AA; 52230 MW; 42A73C66FE9B3392 CRC64;
MWPVWQGMTC LPTEKGASST CSLGGYPVYA VNATSVAQIQ AAVNFARNKA LRLVVKNTGH
DYMGKSVGAG ALSIWTHHLT QIEYIPEYTS SDFRGKAAVA GAGVRTFDIA KIAHENGASL
VGGQCATVGF AAVQIVTPDG VHRTVNAESH PDLFWAIRGG GASTWGVVTS VTVRLHPRHP
LTSCWISFHT SAEVSKETFW KGVRAYAENF EHFADAGFYG FTNIRRNHAG YNGSDFSLGI
EPMLAPNMSM ESFDEVTRPF FDQLAALGIP FQAERRYFDS FHEGWAEIWP SEILVVAEPL
DTPGSRLFPR EVWTDPEGLT AILDTFRNIS ELGYDVTGFL IAPQNPFNVD NAVSPALRHA
LGYFSTSVEF PGNATSEHKA AAQEELMRNI LDPWREVAPS SKFGGSYLNE ANPMEPFWQD
DLYGGNYPRL LEIKRKYDPN SLFYAVTGVG SEEWEVRSTE QGFRTQNGRL CRV
//