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Database: UniProt
Entry: J4WL40_BEAB2
LinkDB: J4WL40_BEAB2
Original site: J4WL40_BEAB2 
ID   J4WL40_BEAB2            Unreviewed;       572 AA.
AC   J4WL40;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Aryl-alcohol oxidase/vanillyl-alcohol oxidase {ECO:0000313|EMBL:EJP70460.1};
GN   ORFNames=BBA_00090 {ECO:0000313|EMBL:EJP70460.1};
OS   Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS   (Tritirachium shiotae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=655819 {ECO:0000313|EMBL:EJP70460.1, ECO:0000313|Proteomes:UP000002762};
RN   [1] {ECO:0000313|EMBL:EJP70460.1, ECO:0000313|Proteomes:UP000002762}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 2860 {ECO:0000313|EMBL:EJP70460.1,
RC   ECO:0000313|Proteomes:UP000002762};
RX   PubMed=22761991; DOI=10.1038/srep00483;
RA   Xiao G., Ying S.H., Zheng P., Wang Z.L., Zhang S., Xie X.Q., Shang Y.,
RA   St Leger R.J., Zhao G.P., Wang C., Feng M.G.;
RT   "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT   Beauveria bassiana.";
RL   Sci. Rep. 2:483-483(2012).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; JH725150; EJP70460.1; -; Genomic_DNA.
DR   RefSeq; XP_008593409.1; XM_008595187.1.
DR   AlphaFoldDB; J4WL40; -.
DR   SMR; J4WL40; -.
DR   STRING; 655819.J4WL40; -.
DR   GeneID; 19883102; -.
DR   HOGENOM; CLU_024402_0_1_1; -.
DR   InParanoid; J4WL40; -.
DR   OrthoDB; 5474593at2759; -.
DR   Proteomes; UP000002762; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.40.462.10; FAD-linked oxidases, C-terminal domain; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR016170; Cytok_DH_C_sf.
DR   InterPro; IPR004113; FAD-bd_oxidored_4_C.
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; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   PANTHER; PTHR11748:SF114; ARYL-ALCOHOL OXIDASE VANILLYL-ALCOHOL OXIDASE (AFU_ORTHOLOGUE AFUA_3G09500)-RELATED; 1.
DR   PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002762}.
FT   DOMAIN          77..280
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   572 AA;  63856 MW;  4291BBFE12E668C4 CRC64;
     MSNTSGSQLG PASRTHPEPI SLPPSTSSAK FHEFLRRASA IVGDENLVVV AGQDQLQQQD
     YMDRSKVHDM FNILEKKTFL HSCTVAPKDV PGVQDIMRLA NEMELPVWPF SMGRNLGYGG
     AAPRVSGSIG LDMGKHMNKV LKVDADSAYA LVEPGVSFFD LHQYLVDHEL RDKVWADCPD
     LGGGSVIGNT IERGIGYTPY GDHWMMHCGL EVVLPDGSLI RTGMGALPNP KADKNAPPHE
     QEPNECWQLF NYGFGPHLDG IFSQSNMGIV TKMGVWLMPN PGGSQTYMIT FPRDDDLNRI
     IEIMRPLRVS MVLQNVPKLD NILVSAAMEG TRSSYTNSKE LLTDAELDAI AEKLGLGRWN
     FYGCIYGPPE VREILWKVIK GAFSQIPGAQ FYFPEDRPHD KALQTRKNTF VGIPSITELD
     WVSWLPNGGH LFFAPIAKLT GDDAEAQYEL TRRRSEEFGF DFLGAFLVGV REIHHIVCII
     FDREDPEMRT RAHKLIKLLI QEAADRGWGE YRAHLALMDQ VAGTYNFNNG AHMKLSEKIK
     DALDPKGILS PGKNGVWPTA YKQYNRQVPN DE
//
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