ID   ETFD_CAEEL              Reviewed;         597 AA.
AC   Q11190;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 2.
DT   16-JUN-2009, entry version 70.
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   AltName: Full=Lethal protein 721;
DE   Flags: Precursor;
GN   Name=let-721; ORFNames=C05D11.12;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U00048; AAB53835.2; -; Genomic_DNA.
DR   PIR; D88483; D88483.
DR   RefSeq; NP_498415.2; -.
DR   UniGene; Cel.17705; -.
DR   Ensembl; C05D11.12; Caenorhabditis elegans.
DR   GeneID; 175916; -.
DR   KEGG; cel:C05D11.12; -.
DR   WormBase; WBGene00002855; let-721.
DR   WormPep; C05D11.12; CE29662.
DR   OMA; Q11190; KGIHTAM.
DR   BRENDA; 1.5.5.1; 672.
DR   NextBio; 890294; -.
DR   ArrayExpress; Q11190; -.
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:0010171; P:body morphogenesis; IMP:WormBase.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0009792; P:embryonic development ending in birth or eg...; IMP:WormBase.
DR   GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR   GO; GO:0040010; P:positive regulation of growth rate; IMP:WormBase.
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; Complete proteome; Electron transport; FAD; Flavoprotein;
KW   Iron; Iron-sulfur; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Oxidoreductase; Transit peptide;
KW   Transmembrane; Transport; Ubiquinone.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    597       Electron transfer flavoprotein-ubiquinone
FT                                oxidoreductase, mitochondrial.
FT                                /FTId=PRO_0000008665.
FT   TRANSMEM    437    457       Potential.
FT   DOMAIN      557    586       4Fe-4S ferredoxin-type.
FT   NP_BIND      53     67       FAD (Potential).
FT   METAL       540    540       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       566    566       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       569    569       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       572    572       Iron-sulfur (4Fe-4S) (Potential).
SQ   SEQUENCE   597 AA;  65335 MW;  C0FF09F185A017FB CRC64;
     MRISGVTLFR VSSQLRNVVN GQWTTTHYTV KDRSTDPRWK DVDLARESDV YDVVIVGGGP
     SGLSAAIRLR QLAEKAQKEL RVCVVEKASV IGGHTLSGAV IETRALDELI PNWKELGAPV
     YQQVTSESIA ILTESGRIPV PVLPGVPLAN HGNYIVRLGK VVQWLGEQAE AAGVEVWPEI
     AASEVLYNED GSVKGIATSD VGIGKDGAPK DGFARGMEFH AKCTIFAEGC RGHLSKQVLD
     KFDLRTHAMT YGIGLKELWE IDPAKHRPGY VEHTMGWPLN VDQYGGSFLY HIEDQGQPLV
     SVGFVVALDY ANPNLNPYKE FQKYKTHPSI SKQLEGGKRI GYGARALNEG GFQSIPKLHF
     PGGCLVGCSA GFLNVAKLKG THNAMKSGMV AAESIFEDIQ QKGEDVQTID PATYDKNIRD
     TYVVKELKAT RNIRPSFNTS LGYIGGLIYS GIFYVFGRGI EPWTLGHGKK DNEKLIPVKD
     AKEIDYPKPD GKLTFDLLTS VSLTGTNHTE DQPAHLTLKN DQVPLDVNLA VYGGPEARFC
     PAGVYEFVPS EADESKKRLQ INAQNCIHCK TCDIKDPQQN INWVTPEGGG GPKYEGM
//