ID B8MBT5_TALSN Unreviewed; 237 AA.
AC B8MBT5;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Probable electron transfer flavoprotein subunit beta {ECO:0000256|PIRNR:PIRNR000090};
GN ORFNames=TSTA_119760 {ECO:0000313|EMBL:EED18218.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED18218.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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; EQ962655; EED18218.1; -; Genomic_DNA.
DR RefSeq; XP_002482210.1; XM_002482165.1.
DR AlphaFoldDB; B8MBT5; -.
DR GeneID; 8105251; -.
DR VEuPathDB; FungiDB:TSTA_119760; -.
DR OrthoDB; 5476365at2759; -.
DR PhylomeDB; B8MBT5; -.
DR Proteomes; UP000001745; 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:UP000001745};
KW Transport {ECO:0000256|PIRNR:PIRNR000090}.
FT DOMAIN 27..224
FT /note="Electron transfer flavoprotein alpha/beta-subunit N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00893"
SQ SEQUENCE 237 AA; 25617 MW; 332CC89A563887BC CRC64;
MASGLRILVP VKRVIDYAMK PRINKTQTGV ETAGVKHSLN PFDEIGVEEA VRLRERKGPL
KVENILALSA GGAKCVDTLR TAMAMGADKA LLIDVPESAD GGPEPLTIAK LLKSVVQKEN
INMVLLGKQA IDGDQGQTGQ MLAGLLGWSQ ATQASKVDIK DESGTVEVTR EVDGGVETLR
AKLPIVITTD LRLNEPRYTS LPNIMKAKKK PLEKKTLADF GVEDKRRLKT VKVTGKL
//
