ID S0ENS9_GIBF5 Unreviewed; 413 AA.
AC S0ENS9;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Related to salicylate 1-monooxygenase {ECO:0000313|EMBL:CCT75844.1};
GN ORFNames=FFUJ_11888 {ECO:0000313|EMBL:CCT75844.1};
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:CCT75844.1, 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 paxM FAD-dependent monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007992}.
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DR EMBL; HF679033; CCT75844.1; -; Genomic_DNA.
DR AlphaFoldDB; S0ENS9; -.
DR STRING; 1279085.S0ENS9; -.
DR EnsemblFungi; CCT75844; CCT75844; FFUJ_11888.
DR VEuPathDB; FungiDB:FFUJ_11888; -.
DR HOGENOM; CLU_009665_19_0_1; -.
DR OrthoDB; 1113861at2759; -.
DR Proteomes; UP000016800; Chromosome 11.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR13789:SF215; FAD-BINDING DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR13789; MONOOXYGENASE; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Monooxygenase {ECO:0000313|EMBL:CCT75844.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000016800}.
FT DOMAIN 4..360
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 413 AA; 45292 MW; 9412F0ACBEEBA257 CRC64;
MPLKVIIAGA GLGGLGAAIA MARAGHNVEV FEQSRFLNEI GAAIHIAPNA TRVLKSWDID
FTELQAVLCN AIKIYDHTGK LIFVPVKLEE LQKSIGTKDE WLLTHRVDLH STLRKAATGN
TFAGSIKIHT ASKVVKADAE TAEITLADGV KHKGDLLIGA DGVHSKVVSA VAGSPPVRIS
TKQNTFRFLV PIDKLMANPI TGPFFGKLGF DCQHVFTTRD RRMVVYPCRN AKLLNIVAMH
PAEDAGLDSE SSWLAGGRVQ DLLDVYKEFG PELIEMCRIG EDLKLWSLAT RDPPTKFYKG
RTVLLGDAAH PMLPHQGQGG AQSFEDAAAL GVLFPADTTL DDVPQRLELY NKLRYPRSVT
VMFMSKINDE RRGEMMDDLR KFVPDAELPP NIFPYLWNNF VLDDAQKALA AAA
//
