ID A0A0D7BI64_9AGAR Unreviewed; 714 AA.
AC A0A0D7BI64;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=electron-transferring-flavoprotein dehydrogenase {ECO:0000256|ARBA:ARBA00012696};
DE EC=1.5.5.1 {ECO:0000256|ARBA:ARBA00012696};
DE AltName: Full=Electron-transferring-flavoprotein dehydrogenase {ECO:0000256|ARBA:ARBA00032754};
GN ORFNames=CYLTODRAFT_435905 {ECO:0000313|EMBL:KIY69920.1};
OS Cylindrobasidium torrendii FP15055 ss-10.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae;
OC Cylindrobasidium.
OX NCBI_TaxID=1314674 {ECO:0000313|EMBL:KIY69920.1, ECO:0000313|Proteomes:UP000054007};
RN [1] {ECO:0000313|EMBL:KIY69920.1, ECO:0000313|Proteomes:UP000054007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FP15055 ss-10 {ECO:0000313|EMBL:KIY69920.1,
RC ECO:0000313|Proteomes:UP000054007};
RX PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA Hibbett D.S.;
RT "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL Fungal Genet. Biol. 76:78-92(2015).
CC -!- FUNCTION: Accepts electrons from ETF and reduces ubiquinone.
CC {ECO:0000256|ARBA:ARBA00002819}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; KN880476; KIY69920.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D7BI64; -.
DR STRING; 1314674.A0A0D7BI64; -.
DR OrthoDB; 275372at2759; -.
DR Proteomes; UP000054007; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProt.
DR GO; GO:0004174; F:electron-transferring-flavoprotein dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.30.9.90; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR040156; ETF-QO.
DR InterPro; IPR049398; ETF-QO/FixC_UQ-bd.
DR InterPro; IPR007859; ETF-QO/FixX_C.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR10617; ELECTRON TRANSFER FLAVOPROTEIN-UBIQUINONE OXIDOREDUCTASE; 1.
DR PANTHER; PTHR10617:SF107; ELECTRON TRANSFER FLAVOPROTEIN-UBIQUINONE OXIDOREDUCTASE, MITOCHONDRIAL; 1.
DR Pfam; PF05187; ETF_QO; 1.
DR Pfam; PF21162; ETFQO_UQ-bd; 1.
DR Pfam; PF13450; NAD_binding_8; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 4: Predicted;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000054007};
KW Transport {ECO:0000256|ARBA:ARBA00022448};
KW Ubiquinone {ECO:0000256|ARBA:ARBA00023075}.
FT DOMAIN 656..685
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 714 AA; 77457 MW; 10CBFE628F4ACCB5 CRC64;
MCHCADQRCD IVDAPSISLF SSKGGDVKDD VKKAHGSSTR RDEEVYNPKA VERVEDEVDV
CIVGAGPAGL SAAIRIKQLE RERGKEVRVV VLEKGGEVGA HILSGAVLEP RALYELLGDP
STYEEAYGSP APLGQPATSS KMKFLTNSAA IPLPHPPQMN NKGNHIISLS ALTRWLAQVA
EEHYGVEIYP GFSGSGLIYS EDADAQDPWT GWAGRWGKDV TRINPTPATP SSDKVHSVQG
IYTNDLGVSK SGHMKPSFEA GMGFRARVTL LAEGAHGSLS KLALAKYNLR AESEPQTYGF
GMKEVWRIAP EDGSSSDGRY RAGEVVHTLG FPMDTQTYGG GWVYHMENGL VSLGLVVGAD
WKNPYRSPYR DFQKMKHHPY LRKLLTASDS FTPSRIAYGA RVLSEGGLQS VPLLHFPGGA
LIGCSAGFVN ITKIKGIHNA MKTGMLGAEG AFEALHPADG SEADPSKPAD LSSYSEAFTK
SWVHEDLKEV RNVRPSFATK LGMWGGVAWS GLDSLILRGK TPFTFRHTKE ESRTRYINAS
PSLDSAHTEP ASKHKPIDYP AFEPPLSTDL MTSVSLTGTN HAEDQVAHLR VMDSNEYLQE
WYGDAEPASE DVALERKHKH TSRNVDEFAG LLGRACPAGV YEYVDDPASK EAVDGKKLVI
NAQNCIHCKL CDVKVPTQDI TWTVPEGGGG PKYIRVVQAR AGCTDMSSDA SRTT
//