ETFA_DICDI
ID ETFA_DICDI Reviewed; 355 AA.
AC Q54FD7;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Electron transfer flavoprotein subunit alpha, mitochondrial;
DE Short=Alpha-ETF;
DE Flags: Precursor;
GN Name=etfa; ORFNames=DDB_G0290927;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: The electron transfer flavoprotein serves as a specific
CC electron acceptor for several dehydrogenases, including five acyl-CoA
CC dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers
CC the electrons to the main mitochondrial respiratory chain via ETF-
CC ubiquinone oxidoreductase (ETF dehydrogenase) (By similarity).
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per dimer. {ECO:0000250};
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ETF alpha-subunit/FixB family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000172; EAL61979.1; -; Genomic_DNA.
DR RefSeq; XP_635485.1; XM_630393.1.
DR AlphaFoldDB; Q54FD7; -.
DR SMR; Q54FD7; -.
DR STRING; 44689.DDB0267017; -.
DR PaxDb; Q54FD7; -.
DR EnsemblProtists; EAL61979; EAL61979; DDB_G0290927.
DR GeneID; 8627901; -.
DR KEGG; ddi:DDB_G0290927; -.
DR dictyBase; DDB_G0290927; etfa.
DR eggNOG; KOG3954; Eukaryota.
DR HOGENOM; CLU_034178_0_0_1; -.
DR InParanoid; Q54FD7; -.
DR OMA; LFVRPIY; -.
DR PhylomeDB; Q54FD7; -.
DR Reactome; R-DDI-611105; Respiratory electron transport.
DR PRO; PR:Q54FD7; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IBA:GO_Central.
DR CDD; cd01715; ETF_alpha; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR014730; ETF_a/b_N.
DR InterPro; IPR001308; ETF_a/FixB.
DR InterPro; IPR033947; ETF_alpha_N.
DR InterPro; IPR014731; ETF_asu_C.
DR InterPro; IPR018206; ETF_asu_C_CS.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR43153; PTHR43153; 1.
DR Pfam; PF01012; ETF; 1.
DR Pfam; PF00766; ETF_alpha; 1.
DR PIRSF; PIRSF000089; Electra_flavoP_a; 1.
DR SMART; SM00893; ETF; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR PROSITE; PS00696; ETF_ALPHA; 1.
PE 3: Inferred from homology;
KW Electron transport; FAD; Flavoprotein; Mitochondrion; Reference proteome;
KW Transit peptide; Transport.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..355
FT /note="Electron transfer flavoprotein subunit alpha,
FT mitochondrial"
FT /id="PRO_0000327541"
FT BINDING 295..323
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
SQ SEQUENCE 355 AA; 37579 MW; 935C9A75259A9C9F CRC64;
MIGRLNLITK SNLFKNVNNL NNKNYYSTCL VIAEHDNNQL LNSTLNTITA ASKLGVTNIS
VLVAGSKCGP VADSVSKVSG VTNVVCVDHP TLEHSLAETI TPIIVKLQSS SSKEGDEITH
IFTPASNFGK NFLPRVAALL NVSQISEITK VKDAETFQRP IYAGNAIATV KSTDKCKVGT
VRTTAFDKAP TSGGSAKVVS ANDWAVPLIE KAISETNIKW ESSEVKKSER PELTSARVVV
SGGRGMKNGE NFKMLEELAD TLGGAVGASR AAVDSGFVSN DLQVGQTGKI VAPELYIAVG
ISGAIQHLAG MKDSKVIVAI NKDPEAPIFQ VADVGLVGDL FNEVPKLTES IKKSK