ID A0A0D2D7M9_9EURO Unreviewed; 255 AA.
AC A0A0D2D7M9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Probable electron transfer flavoprotein subunit beta {ECO:0000256|PIRNR:PIRNR000090};
GN ORFNames=PV06_09372 {ECO:0000313|EMBL:KIW38405.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW38405.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW38405.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW38405.1,
RC ECO:0000313|Proteomes:UP000053342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL Submitted (JAN-2015) 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|ARBA:ARBA00025416, ECO:0000256|PIRNR:PIRNR000090}.
CC -!- COFACTOR:
CC Name=AMP; Xref=ChEBI:CHEBI:456215;
CC Evidence={ECO:0000256|PIRNR:PIRNR000090};
CC Note=Binds 1 AMP per subunit. {ECO:0000256|PIRNR:PIRNR000090};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRNR:PIRNR000090};
CC Note=Binds 1 FAD per dimer. {ECO:0000256|PIRNR:PIRNR000090};
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC {ECO:0000256|PIRNR:PIRNR000090}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|PIRNR:PIRNR000090}.
CC -!- SIMILARITY: Belongs to the ETF beta-subunit/FixA family.
CC {ECO:0000256|ARBA:ARBA00007557, ECO:0000256|PIRNR:PIRNR000090}.
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DR EMBL; KN847341; KIW38405.1; -; Genomic_DNA.
DR RefSeq; XP_016258621.1; XM_016410814.1.
DR AlphaFoldDB; A0A0D2D7M9; -.
DR STRING; 215243.A0A0D2D7M9; -.
DR GeneID; 27361446; -.
DR VEuPathDB; FungiDB:PV06_09372; -.
DR HOGENOM; CLU_060196_0_0_1; -.
DR OrthoDB; 5476365at2759; -.
DR Proteomes; UP000053342; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR CDD; cd01714; ETF_beta; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR000049; ET-Flavoprotein_bsu_CS.
DR InterPro; IPR014730; ETF_a/b_N.
DR InterPro; IPR012255; ETF_b.
DR InterPro; IPR033948; ETF_beta_N.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR21294; ELECTRON TRANSFER FLAVOPROTEIN BETA-SUBUNIT; 1.
DR PANTHER; PTHR21294:SF8; ELECTRON TRANSFER FLAVOPROTEIN SUBUNIT BETA; 1.
DR Pfam; PF01012; ETF; 1.
DR PIRSF; PIRSF000090; Beta-ETF; 1.
DR SMART; SM00893; ETF; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR PROSITE; PS01065; ETF_BETA; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|PIRNR:PIRNR000090};
KW Mitochondrion {ECO:0000256|PIRNR:PIRNR000090};
KW Reference proteome {ECO:0000313|Proteomes:UP000053342};
KW Transport {ECO:0000256|PIRNR:PIRNR000090}.
FT DOMAIN 27..218
FT /note="Electron transfer flavoprotein alpha/beta-subunit N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00893"
SQ SEQUENCE 255 AA; 27725 MW; D7F3E89FE99B9203 CRC64;
MSSKLRILVP VKRVIDYAVK PRVKSDRTGV ETANVKHSLN PFDELSIEEA VRLRERKLAV
DDILAVSAGP AKCADTLRTA MAMGADRSIH VDVPEDKPLE PLGVAKLLKA IAEKEQSNLI
FVGKQAIDDD AGQTGQMLAG LLNWPQATQA SKVEIDGEEV TVTKEVDGGV ETLKARLPMI
ITTDLRLNEP RYASLPNIMK AKKKKLEKKT LADYGVDGKA RLKTVKVEEP PARQGGGKVE
DVDGMISKLK ELGAI
//
