ID   A0A2G5I4H8_CERBT        Unreviewed;       457 AA.
AC   A0A2G5I4H8;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Putative oxidoreductase OrdL {ECO:0000313|EMBL:PIA99412.1};
GN   ORFNames=CB0940_02641 {ECO:0000313|EMBL:PIA99412.1};
OS   Cercospora beticola (Sugarbeet leaf spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX   NCBI_TaxID=122368 {ECO:0000313|EMBL:PIA99412.1, ECO:0000313|Proteomes:UP000230605};
RN   [1] {ECO:0000313|EMBL:PIA99412.1, ECO:0000313|Proteomes:UP000230605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=09-40 {ECO:0000313|EMBL:PIA99412.1,
RC   ECO:0000313|Proteomes:UP000230605};
RA   De Jonge R., Ebert M.K., Suttle J.C., Jurick Ii W.M., Secor G.A.,
RA   Thomma B.P., Van De Peer Y., Bolton M.D.;
RT   "The cercosporin biosynthetic gene cluster was horizontally transferred to
RT   several fungal lineages and shown to be expanded in Cercospora beticola
RT   based on microsynteny with recipient genomes.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:PIA99412.1}.
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DR   EMBL; LKMD01000101; PIA99412.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5I4H8; -.
DR   OrthoDB; 2600928at2759; -.
DR   Proteomes; UP000230605; Chromosome 3.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR13847:SF279; FAD DEPENDENT OXIDOREDUCTASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF01266; DAO; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
FT   DOMAIN          34..411
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   457 AA;  50000 MW;  AF21511C168F41DB CRC64;
     MAVPVPNATQ SFWRSDLHAL DDHRTTERLP AEADIVIIGA GYAGASLAYH LLEKSETSQK
     PVSIVLLEAR QACSGATGRN GGHLKPDPYY RAAGALKTHG REAAEEVASF EARQVKEIQK
     LVEKEAIDCD FVVTRATDVC MYESAHRELK QGLDALHDAN ISTASEVHYS GPRTAQGISG
     IKGAKACFTY TAAHVWPYKL VLHLLQKAVG KGVNLQTHTP VKSVKPAGGS GRWAVETERG
     TMQAAKVIYA SNAYTSSLLP EYKGKIIGVR GICSRIVSTK PDAPLLTNSY IMRLAPGEYD
     YLIPRSDGSI IVGGGRRDYF KQLDSWYDNY DDSKLIESAK HYFDGYMQRH FRGWEDSGAY
     TDACWSGIMG YSSNGFPHVG EVPGKKGQYI CAGFSGHGMP QIFLSAKAVA SMVLEDKRAD
     EVDLPRLYRS SQARLDSTLN VTLEGWDNTH AKSTAKL
//