ID S0EPN7_GIBF5 Unreviewed; 500 AA.
AC S0EPN7;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Related to oxidoreductase {ECO:0000313|EMBL:CCT75470.1};
GN ORFNames=FFUJ_11492 {ECO:0000313|EMBL:CCT75470.1};
OS Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS and foot rot disease fungus) (Fusarium fujikuroi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=1279085 {ECO:0000313|EMBL:CCT75470.1, ECO:0000313|Proteomes:UP000016800};
RN [1] {ECO:0000313|Proteomes:UP000016800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831
RC {ECO:0000313|Proteomes:UP000016800};
RX PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA Wiemann P., Sieber C.M., von Bargen K.W., Studt L., Niehaus E.M.,
RA Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA Proctor R.H., Munsterkotter M., Freitag M., Humpf H.U., Guldener U.,
RA Tudzynski B.;
RT "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT novel metabolites.";
RL PLoS Pathog. 9:E1003475-E1003475(2013).
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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DR EMBL; HF679033; CCT75470.1; -; Genomic_DNA.
DR AlphaFoldDB; S0EPN7; -.
DR STRING; 1279085.S0EPN7; -.
DR EnsemblFungi; CCT75470; CCT75470; FFUJ_11492.
DR VEuPathDB; FungiDB:FFUJ_11492; -.
DR HOGENOM; CLU_018354_0_1_1; -.
DR OrthoDB; 1068078at2759; -.
DR Proteomes; UP000016800; Chromosome 11.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; 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; IPR012951; BBE.
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:SF9; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN-RELATED; 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:UP000016800}.
FT DOMAIN 68..239
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 500 AA; 55076 MW; D5DEF8592DC3DAB2 CRC64;
MEFIAAGASW ALGKAPSPQK ILGRLGLASL VAQNSWPELS SKLSPQASIV LPDESSFSGL
VSRWRDWHGP QPGAVVRTFS ESDVQETIRY ANEHGIPFLA RSGGHGATEA LQLAKDVIVV
DLRDQNDVEI ARDGKSARIG GGASVKKVVN ELWTAGKQTV TGICECVGVS APVLGGGHGW
LQGQYGLASD QVISARVVLP NGDAVTASED SNPDLFWALR GAGHNFGIVT EWKYRIYDIN
NPMWSYEIFI FLGDKLEDVL ELTNKMMKTQ PPHLTHWIYI VNIPEIDPDK PIIWYAVISD
GAAQKARDYA NPLHGLGPIN VNAGEASMPD LAAITLMGDD TVGCAKGFTG LRYPIGLKTY
DLFAVRKVFN EIADMSKRVP EFAGSFFLLE GYSTHGVKAI DAKDSAFPHR DDEILVTPYI
LYKPNATLDG LAQEHGEKLR RHLLEASGDP EHLRAYVNYA HGFESLEEMY GHEPWRIEKL
KALKKKWDPE NRMRFYAPIV
//