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Database: UniProt
Entry: A0A0L0FSY5_9EUKA
LinkDB: A0A0L0FSY5_9EUKA
Original site: A0A0L0FSY5_9EUKA 
ID   A0A0L0FSY5_9EUKA        Unreviewed;       341 AA.
AC   A0A0L0FSY5;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Electron transfer flavoprotein subunit alpha {ECO:0000256|PIRNR:PIRNR000089};
DE            Short=Alpha-ETF {ECO:0000256|PIRNR:PIRNR000089};
GN   ORFNames=SARC_07823 {ECO:0000313|EMBL:KNC79794.1};
OS   Sphaeroforma arctica JP610.
OC   Eukaryota; Ichthyosporea; Ichthyophonida; Sphaeroforma.
OX   NCBI_TaxID=667725 {ECO:0000313|EMBL:KNC79794.1, ECO:0000313|Proteomes:UP000054560};
RN   [1] {ECO:0000313|EMBL:KNC79794.1, ECO:0000313|Proteomes:UP000054560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP610 {ECO:0000313|EMBL:KNC79794.1,
RC   ECO:0000313|Proteomes:UP000054560};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Cuomo C., Young S.K., Zeng Q., Gargeya S., Alvarado L., Berlin A.,
RA   Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E., Heiman D., Howarth C., Mehta T., Neiman D.,
RA   Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA   Sykes S., White J., Yandava C., Burger G., Gray M.W., Holland P.W.H.,
RA   King N., Lang F.B.F., Roger A.J., Ruiz-Trillo I., Haas B., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Sphaeroforma arctica JP610.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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).
CC       {ECO:0000256|PIRNR:PIRNR000089}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000089,
CC         ECO:0000256|PIRSR:PIRSR000089-1};
CC       Note=Binds 1 FAD per dimer. {ECO:0000256|PIRNR:PIRNR000089,
CC       ECO:0000256|PIRSR:PIRSR000089-1};
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC       {ECO:0000256|PIRNR:PIRNR000089}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000256|PIRNR:PIRNR000089}.
CC   -!- SIMILARITY: Belongs to the ETF alpha-subunit/FixB family.
CC       {ECO:0000256|ARBA:ARBA00005817, ECO:0000256|PIRNR:PIRNR000089}.
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DR   EMBL; KQ242244; KNC79794.1; -; Genomic_DNA.
DR   RefSeq; XP_014153696.1; XM_014298221.1.
DR   AlphaFoldDB; A0A0L0FSY5; -.
DR   STRING; 667725.A0A0L0FSY5; -.
DR   EnsemblProtists; KNC79794; KNC79794; SARC_07823.
DR   GeneID; 25908327; -.
DR   eggNOG; KOG3954; Eukaryota.
DR   OrthoDB; 5481222at2759; -.
DR   Proteomes; UP000054560; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   CDD; cd01715; ETF_alpha; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 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; ELECTRON TRANSFER FLAVOPROTEIN ALPHA; 1.
DR   PANTHER; PTHR43153:SF1; ELECTRON TRANSFER FLAVOPROTEIN SUBUNIT ALPHA, MITOCHONDRIAL; 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; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR   PROSITE; PS00696; ETF_ALPHA; 1.
PE   3: Inferred from homology;
KW   Electron transport {ECO:0000256|PIRNR:PIRNR000089};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR000089};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|PIRNR:PIRNR000089};
KW   Mitochondrion {ECO:0000256|PIRNR:PIRNR000089};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054560};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000089}.
FT   DOMAIN          33..214
FT                   /note="Electron transfer flavoprotein alpha/beta-subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00893"
FT   BINDING         234
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         259..260
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         273..277
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         290..297
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         311
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
SQ   SEQUENCE   341 AA;  35068 MW;  0098001446DF59B5 CRC64;
     MLSAIRTSAF SNGRCAVMAA AARRCYSAGA SNTLVYVEHD NAKVLKPTLH TITAAKAIGG
     PVTCMIVGCG CGPVVEQLSK VAGVDKILVA DDEIFKGHLP EAVAPAIVAA QKQFNFSHIV
     ASATAIGKNV APRVAALLDV QSISDITGVV DANTFTRPIY AGNAVAKVQS SDDIKVVTVR
     ATAFAAADET GGSAENESVA AGEAQSLSKF VGQELSKSDR PELGSARVVV SGGRALKSGE
     NFEILYSLAD KLSAGVGASR AAVDAGYVPN DMQIGQTGKI VAPELYIAVG ISGAIQHLAG
     MKDSKTIVAI NKDPDAPIFQ VADYGLVGDL FKVVPELEKA L
//
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