ID   ETFD_BOVIN              Reviewed;         617 AA.
AC   Q2KIG0;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 31.
DE   RecName: Full=Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial;
DE            Short=ETF-ubiquinone oxidoreductase;
DE            Short=ETF-QO;
DE            EC=1.5.5.1;
DE   AltName: Full=Electron-transferring-flavoprotein dehydrogenase;
DE            Short=ETF dehydrogenase;
DE   Flags: Precursor;
GN   Name=ETFDH;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Accepts electrons from ETF and reduces ubiquinone (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Reduced electron-transferring flavoprotein +
CC       ubiquinone = electron-transferring flavoprotein + ubiquinol.
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster (By similarity).
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the ETF-QO/fixC family.
CC   -!- SIMILARITY: Contains 1 4Fe-4S ferredoxin-type domain.
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DR   EMBL; BC112652; AAI12653.1; -; mRNA.
DR   IPI; IPI00694705; -.
DR   RefSeq; NP_001070598.1; -.
DR   UniGene; Bt.42330; -.
DR   SMR; Q2KIG0; 39-617.
DR   Ensembl; ENSBTAG00000016679; Bos taurus.
DR   GeneID; 768074; -.
DR   KEGG; bta:768074; -.
DR   HOVERGEN; Q2KIG0; -.
DR   OMA; Q2KIG0; YTPGMEL.
DR   BRENDA; 1.5.5.1; 251.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0004174; F:electron-transferring-flavoprotein dehydrog...; IEA:EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR007859; ETFD_OxRdtase.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   Pfam; PF05187; ETF_QO; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   2: Evidence at transcript level;
KW   4Fe-4S; Acetylation; Electron transport; FAD; Flavoprotein; Iron;
KW   Iron-sulfur; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Oxidoreductase; Transit peptide;
KW   Transmembrane; Transport; Ubiquinone.
FT   TRANSIT       1     33       Mitochondrion (Potential).
FT   CHAIN        34    617       Electron transfer flavoprotein-ubiquinone
FT                                oxidoreductase, mitochondrial.
FT                                /FTId=PRO_0000285209.
FT   TRANSMEM    458    478       Potential.
FT   DOMAIN      577    606       4Fe-4S ferredoxin-type.
FT   NP_BIND      71     85       FAD (Potential).
FT   METAL       561    561       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       586    586       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       589    589       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       592    592       Iron-sulfur (4Fe-4S) (Potential).
FT   MOD_RES      96     96       N6-acetyllysine (By similarity).
FT   MOD_RES     153    153       N6-acetyllysine (By similarity).
FT   MOD_RES     223    223       N6-acetyllysine (By similarity).
FT   MOD_RES     344    344       N6-acetyllysine (By similarity).
SQ   SEQUENCE   617 AA;  68612 MW;  3ABDAE292A4C4920 CRC64;
     MQVLLARLAC PVYQCFHAIK IKKNYLPLCA TRWSSTSVVP RITTHYTVYP RDQDKRWEGV
     NMERFAEEAD VVIVGAGPAG LSAAARLKQL AAQHEKDIRV CLVEKAAQIG AHTLSGACLD
     PRALQELFPD WKEKGAPLNT PVTEDRFGIL TEKYRIPVPI LPGLPMNNHG NYIVRLGHLV
     SWMGEQAEAL GVEVYPGYAA AEVLFHEDGS VKGIATNDVG IQKDGAPKTT FERGLELHAK
     VTIFAEGCHG HLAKQLYRKF DLRANCEPQT YGIGLKELWV IDEKKWKPGR VDHTVGWPLD
     RHTYGGSFLY HLNEGEPLVA LGFVVGLDYQ NPYLSPFREF QRWKHHPSIQ PTLEGGKRIA
     YGARALNEGG LQCIPKLTFP GGLLIGCSPG FMNVPKIKGT HTAMKSGILA AESIFNQLTN
     ENLQSKTIGL DVTEYEDNLK KSWVWKELYA VRNIRPSCHS ILGVYGGMIY TGIFYWIFRG
     MEPWTLKHKG SDSDKLKPAK DCTPIEYPKP DGQISFDLLS SVALSGTNHE HDQPAHLTLK
     DDSVPVNRNL SIYDGPEQRF CPAGVYEFVP VEQGDGFRLQ INAQNCVHCK TCDIKDPSQN
     INWVVPEGGG GPAYNGM
//