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Database: UniProt
Entry: A0A2T9YKS5_9FUNG
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ID   A0A2T9YKS5_9FUNG        Unreviewed;       254 AA.
AC   A0A2T9YKS5;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Probable electron transfer flavoprotein subunit beta {ECO:0000256|PIRNR:PIRNR000090};
GN   ORFNames=BB561_003540 {ECO:0000313|EMBL:PVU92937.1};
OS   Smittium simulii.
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC   Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX   NCBI_TaxID=133385 {ECO:0000313|EMBL:PVU92937.1, ECO:0000313|Proteomes:UP000245383};
RN   [1] {ECO:0000313|EMBL:PVU92937.1, ECO:0000313|Proteomes:UP000245383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SWE-8-4 {ECO:0000313|EMBL:PVU92937.1,
RC   ECO:0000313|Proteomes:UP000245383};
RX   PubMed=29764946;
RA   Wang Y., Stata M., Wang W., Stajich J.E., White M.M., Moncalvo J.M.;
RT   "Comparative Genomics Reveals the Core Gene Toolbox for the Fungus-Insect
RT   Symbiosis.";
RL   MBio 9:e00636-e00618(2018).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PVU92937.1}.
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DR   EMBL; MBFR01000144; PVU92937.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T9YKS5; -.
DR   STRING; 133385.A0A2T9YKS5; -.
DR   Proteomes; UP000245383; 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; 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.
PE   3: Inferred from homology;
KW   Electron transport {ECO:0000256|PIRNR:PIRNR000090};
KW   Mitochondrion {ECO:0000256|PIRNR:PIRNR000090};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245383};
KW   Transport {ECO:0000256|PIRNR:PIRNR000090}.
FT   DOMAIN          23..216
FT                   /note="Electron transfer flavoprotein alpha/beta-subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00893"
SQ   SEQUENCE   254 AA;  27562 MW;  A070953F317E3355 CRC64;
     MKILVGVKRV VDYAVKIRVN SAKTAVETAN VKHSINPFDE IAVEEAVRLR EKLPKGSVSE
     IVALSCGPAK CSEVLRTALA MGADRAIHVE VPQNTTLEPL IVAKLFSAVA KKENPSLIIM
     GKQAIDDDAC QTGQMLAGLL DYPQANFVAK LDVADNKVTA SCEIDGGLET VECEMPAIIT
     TDLRLNEPRY ATLPNIMKAK KKPLDKLTPA DLKVDIISKL KVLKVEEPAK RKAGIMVGSV
     EELIKKLRDE AKVL
//
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