ID R4G4R6_RHOPR Unreviewed; 330 AA.
AC R4G4R6;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Electron transfer flavoprotein subunit alpha {ECO:0000256|PIRNR:PIRNR000089};
DE Short=Alpha-ETF {ECO:0000256|PIRNR:PIRNR000089};
OS Rhodnius prolixus (Triatomid bug).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC Cimicomorpha; Reduviidae; Triatominae; Rhodnius.
OX NCBI_TaxID=13249 {ECO:0000313|EMBL:JAA76964.1};
RN [1] {ECO:0000313|EMBL:JAA76964.1}
RP NUCLEOTIDE SEQUENCE.
RA Ribeiro J.M.C., Genta F.A., Sorgine M.H.F., Paiva-Silva G.O.,
RA Majerowicz D., Medeiros M., Koerich L., Terra W.R., Ferreira C.,
RA Pimentel A.C., Bisch P.M., Diniz M.M.P., Nascimento R., Salmon D.,
RA Silber A.M., Alves M., Oliveira M.F., Gondim K.C., Silva Neto M.A.C.,
RA Atella G.C., Araujo H., Dias F.S., Polycarpo C.R., Fampa P., Melo A.C.,
RA Tanaka A.S., Balczun C., Oliveira J.H.M., Goncalves R., Lazoski C.,
RA Pereira M.A., Rivera-Pomar R., Diambra L., Schaub G.A., Garcia E.S.,
RA Azambuja P., Braz G.R.C., Oliveira P.L.;
RT "An insight into the transcriptome of the digestive tract of the blood
RT sucking bug, Rhodnius prolixus.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000015103}
RP NUCLEOTIDE SEQUENCE.
RA Wilson R.K., Warren W., Dotson E., Oliveira P.L.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:RPRC011302-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-2015) to UniProtKB.
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}.
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; ACPB03011704; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GAHY01000546; JAA76964.1; -; mRNA.
DR AlphaFoldDB; R4G4R6; -.
DR STRING; 13249.R4G4R6; -.
DR EnsemblMetazoa; RPRC011302-RA; RPRC011302-PA; RPRC011302.
DR VEuPathDB; VectorBase:RPRC011302; -.
DR eggNOG; KOG3954; Eukaryota.
DR HOGENOM; CLU_034178_0_0_1; -.
DR InParanoid; R4G4R6; -.
DR OMA; WRPYAEQ; -.
DR OrthoDB; 5481222at2759; -.
DR Proteomes; UP000015103; 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 2: Evidence at transcript level;
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:UP000015103};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000089}.
FT DOMAIN 22..208
FT /note="Electron transfer flavoprotein alpha/beta-subunit N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00893"
FT BINDING 223
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT BINDING 248..249
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT BINDING 262..266
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT BINDING 279..286
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT BINDING 300
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
SQ SEQUENCE 330 AA; 34423 MW; FC9FEEEA6D280CE8 CRC64;
MFTTFRKLSS PGSKIVKRLQ STLVVAEHDN DKILPITRNT ITAAGKVGGD ISLLVAGDNC
AKAVAEAGTL PGISKVLTAD NPCFKGFLAE SITSLIIACH NQFKYSHIMA GATAQGKALL
PRVAALLDVS PVSDIIGIAG PDTFIRTIYA GNAVMTLKCK DPVKVLTVRG TAFAPAEGEG
SPAKEDAPTG DYKAPGTTFV AQEIKKSDRP ELTAAKIIIS GGRGMKSGDN FKLLYTLADK
LGAAVGASRA AVDAGFVSND LQIGQTGKIV APELYIAIGI SGAIQHLAGM KDSKTIVAIN
KDPEAPIFQV ADYGLVEDLF KAVPELTEKI
//
