ID A0A0A2VGH2_BEABA Unreviewed; 604 AA.
AC A0A0A2VGH2;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=6-hydroxy-D-nicotine oxidase {ECO:0000313|EMBL:KGQ06986.1};
GN ORFNames=BBAD15_g7711 {ECO:0000313|EMBL:KGQ06986.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ06986.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ06986.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ06986.1,
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 -!- 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:KGQ06986.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ANFO01000738; KGQ06986.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2VGH2; -.
DR STRING; 1245745.A0A0A2VGH2; -.
DR eggNOG; ENOG502QQWK; Eukaryota.
DR HOGENOM; CLU_018354_4_4_1; -.
DR Proteomes; UP000030106; 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; -; 2.
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:SF155; ALCOHOL OXIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G00430)-RELATED; 1.
DR PANTHER; PTHR13878; GULONOLACTONE OXIDASE; 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:UP000030106};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..604
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002006437"
FT DOMAIN 122..305
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 604 AA; 65143 MW; D9DB1A2874702F6B CRC64;
MRLITAATSL TLMLGSVHGA ALQTSNAQCR CRPNDPCWPS QSQWASLNAS VSGNLVALRP
VAHVCHDPGY DAAACNASKA LSESSVWRDQ NPGAVQWTNW EAWPERNETC SFSLPRDVAC
RQGRVPLFSV VAETAQHIQE AVRFAASHNI RLVIKNTGHC FLGRSSAPES LQIATYKMKK
MEFVDDFVPE GSGNKSMGSA LILGAGVVLM DIYSETSKRN LTAVVGLSHT VGAAGGYIQG
GGHSPLGPWK GMASDNALQF EVVTADGKLL VTNQYQNRDL FWALRGGGGG TFGVVVSVTI
RTFPDVPALA LMSSITFPGP ADDRFWDVMA ALHQRLPALA DVGGSGYYVF LPNSVQNSTS
TASINIVMFF PNKTEKAPIA KIADGFIQAA RKSAPDANYT LQLAPSLGGS IAYELAKTPY
DATGGTVIIG SRLISRKLLS QKDGAQRLGK ALRGIYEGSG NTGYTGHFIA DGAVAKNAGK
VDSALNPAWR KTITHITFGR DWAPDATLAE QKAVQNKLTN VEVPILKALE RDMGAYLNEA
DAFETDFQES FWGDNYKRLY RIKQHTDPRG LFIVRRGVGS EDWDAEGLCR VRKPSLGDDS
RLQL
//