GenomeNet

Database: UniProt
Entry: N4UET0_FUSC1
LinkDB: N4UET0_FUSC1
Original site: N4UET0_FUSC1 
ID   N4UET0_FUSC1            Unreviewed;       268 AA.
AC   N4UET0;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Probable electron transfer flavoprotein subunit alpha {ECO:0000256|PIRNR:PIRNR000089};
GN   ORFNames=FOC1_g10004910 {ECO:0000313|EMBL:ENH74303.1};
OS   Fusarium oxysporum f. sp. cubense (strain race 1) (Panama disease fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=1229664 {ECO:0000313|EMBL:ENH74303.1, ECO:0000313|Proteomes:UP000016928};
RN   [1] {ECO:0000313|Proteomes:UP000016928}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RA   Fang X., Huang J.;
RT   "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT   banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000016928}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RX   PubMed=24743270;
RA   Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA   Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA   Fang X., Peng M., Huang J.;
RT   "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT   oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL   PLoS ONE 9:E95543-E95543(2014).
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|ARBA:ARBA00025416, 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KB730036; ENH74303.1; -; Genomic_DNA.
DR   AlphaFoldDB; N4UET0; -.
DR   STRING; 1229664.N4UET0; -.
DR   VEuPathDB; FungiDB:FOC1_g10004910; -.
DR   HOGENOM; CLU_034178_0_0_1; -.
DR   Proteomes; UP000016928; 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   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; 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   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:UP000016928};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000089}.
FT   DOMAIN          2..120
FT                   /note="Electron transfer flavoprotein alpha/beta-subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01012"
FT   DOMAIN          146..226
FT                   /note="Electron transfer flavoprotein alpha subunit C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00766"
FT   BINDING         157
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         183..184
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         197..201
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         214..221
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         235
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
SQ   SEQUENCE   268 AA;  27849 MW;  F7B85642CCBB1A3B CRC64;
     MKGLNKVIAG TQEQHHARLP ESVAAVVASH AEQGKYTHVV AANSVFSRDA LIRAAALNGH
     QPISDVTSVE SEDVFVRPIY AGNAVMTVKS SDDVKYLTVR ASAFPAAEAA DGPAPIVTYT
     ENSSSGNSRS AEWVQEDLVK SDRPELGTAE RVVSGGRGLK SKEAFDQVLL PLANSLRAAV
     GASRAAVDSG FADNSLQVGQ TGNVVAPELY VAVGISGAIQ HLAGMKDSKV IAAINKDPDA
     PIFQVADVGL VGDLFEAVPE LTKSCSSA
//
DBGET integrated database retrieval system