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Database: UniProt
Entry: A0A0A2VS14_BEABA
LinkDB: A0A0A2VS14_BEABA
Original site: A0A0A2VS14_BEABA 
ID   A0A0A2VS14_BEABA        Unreviewed;       536 AA.
AC   A0A0A2VS14;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=6-hydroxy-D-nicotine oxidase {ECO:0000313|EMBL:KGQ10423.1};
GN   ORFNames=BBAD15_g4248 {ECO:0000313|EMBL:KGQ10423.1};
OS   Beauveria bassiana D1-5.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ10423.1, ECO:0000313|Proteomes:UP000030106};
RN   [1] {ECO:0000313|EMBL:KGQ10423.1, ECO:0000313|Proteomes:UP000030106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D1-5 {ECO:0000313|EMBL:KGQ10423.1,
RC   ECO:0000313|Proteomes:UP000030106};
RA   Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA   Du Q., Sun Z.;
RT   "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT   bassiana D1-5.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KGQ10423.1}.
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DR   EMBL; ANFO01000322; KGQ10423.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2VS14; -.
DR   HOGENOM; CLU_037328_0_0_1; -.
DR   Proteomes; UP000030106; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.40.462.20; -; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR   PANTHER; PTHR42973:SF39; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 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:UP000030106};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..536
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002006667"
FT   DOMAIN          66..247
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   536 AA;  58791 MW;  66CEFF8F076AB990 CRC64;
     MIFSTIIALF DLVSLVTAGP YIEGTCTRSD GALQWLASRL SKNSAISCLG QPLQLRNANR
     YWGEQFGKNA SVVVYPATTK DVSQAVQAAN WSKFGADFSI VGGAHSQINA SSSYGFVLDM
     SWMNSSRLIR QFRDPAGGKP FAAVEYQGGA NWGQVQSVTN GTGYTAIGAR LASVGAGGFS
     LGGGIGFLAG AHGFATDRLV QMEVVLPSGQ VVTATRTNKH SNLFWALQGG SGQFGIVTRF
     WQRAVVEPKQ STIAFYYIKD TDVLRLRRQV VEFFKTNKDP FSVVYYSFGY LPDNLNDPKP
     ESYAKRTLLI TAHFDDPTNP SQPDNTRAFQ SLLDGIDVSH GIVIPTNHYS NLVFLGGAAY
     PYGYRRGFYG AQTSEIDVDY LAKVTDTFWK YVETLIKRGE KPYSASFVMQ YMYPGLNGHL
     PKSDGDTAWP HARVGHQTLI TPAYKHFEND GLAVAAVQEL NQITYAQQKK VGSFLANYPN
     YIAPGDSGCR VWGHNVKRLA DIKQEYDPGC LIRNGRVFAS HGCRMGGWAN VFDDCA
//
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