ID S0E5Y7_GIBF5 Unreviewed; 563 AA.
AC S0E5Y7;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Related to 4-cresol dehydrogenase flavoprotein subunit {ECO:0000313|EMBL:CCT67978.1};
GN ORFNames=FFUJ_06729 {ECO:0000313|EMBL:CCT67978.1};
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:CCT67978.1, 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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; HF679027; CCT67978.1; -; Genomic_DNA.
DR AlphaFoldDB; S0E5Y7; -.
DR STRING; 1279085.S0E5Y7; -.
DR EnsemblFungi; CCT67978; CCT67978; FFUJ_06729.
DR VEuPathDB; FungiDB:FFUJ_06729; -.
DR HOGENOM; CLU_024402_0_0_1; -.
DR OrthoDB; 5474593at2759; -.
DR Proteomes; UP000016800; Chromosome 5.
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:UP000016800}.
FT DOMAIN 64..267
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 563 AA; 62641 MW; 852BFCE3FEBBD656 CRC64;
MTTVNPLVLP PGIAPSVFHQ FISEVTEVTT AENVIIISNP GQLDKQDYRD PSKMHDMFDI
TSKQHFVSSA VVTPRDVAEV QAIVKLCNKF EIPLWPFSIG RNVGYGGAAP RVPGSIGLDL
GKHMNKILKV DVDGAYALVE PGVTYTDLHQ YLVDNNLRDK LWIDVPDLGG GSVLGNTTER
GVGYTPYGDH FMMHCGMEVV LPYGTLVRTG MGALPNPDAD PNAPPHEQEP NSAWQLFNYG
FGPYNDGIFT QSSLGIVVKM GIWLMVNPGG YQSYLITIPK DEDLHQAIEI IRPLRTSMVL
QNVPTVRHVL LDAAVMGSRD KYTTSKKPLN DKELDEIAEK LNLGRWNFYG ALYGPEPIRK
VMWEVVKGAF SAIPGAKFYF PEDMPDNLVL QTRHLTLQGI PTMTELEWVN WLPNGAHLFF
SPIAKVTGDD AVAQYALTRK RCEEAGFDFI GTFVVGMREM HHIVCLVFDR LDPESCRRAH
NLIIQLIDDA AKKGWGEYRT HLALMDQIAQ TYHFNNNAQM HLNTTIKNAL DPKGILAPGK
NGIWPSGYNA KDFAVSPQRS TKL
//
