ETFD_PONAB
ID ETFD_PONAB Reviewed; 617 AA.
AC Q5RDD3;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial;
DE Short=ETF-QO;
DE Short=ETF-ubiquinone oxidoreductase;
DE EC=1.5.5.1;
DE AltName: Full=Electron-transferring-flavoprotein dehydrogenase;
DE Short=ETF dehydrogenase;
DE Flags: Precursor;
GN Name=ETFDH;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Accepts electrons from ETF and reduces ubiquinone.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ubiquinone + reduced [electron-transfer flavoprotein] = a
CC ubiquinol + H(+) + oxidized [electron-transfer flavoprotein];
CC Xref=Rhea:RHEA:24052, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566,
CC Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307; EC=1.5.5.1;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ETF-QO/FixC family. {ECO:0000305}.
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DR EMBL; CR857981; CAH90224.1; -; mRNA.
DR RefSeq; NP_001125091.1; NM_001131619.1.
DR AlphaFoldDB; Q5RDD3; -.
DR SMR; Q5RDD3; -.
DR STRING; 9601.ENSPPYP00000016941; -.
DR GeneID; 100171973; -.
DR KEGG; pon:100171973; -.
DR CTD; 2110; -.
DR eggNOG; KOG2415; Eukaryota.
DR InParanoid; Q5RDD3; -.
DR OrthoDB; 293434at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004174; F:electron-transferring-flavoprotein dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR040156; ETF-QO.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR10617; PTHR10617; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Acetylation; Electron transport; FAD; Flavoprotein; Iron;
KW Iron-sulfur; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Transit peptide; Transport; Ubiquinone.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 34..617
FT /note="Electron transfer flavoprotein-ubiquinone
FT oxidoreductase, mitochondrial"
FT /id="PRO_0000285847"
FT INTRAMEM 109..130
FT /evidence="ECO:0000250"
FT INTRAMEM 428..447
FT /evidence="ECO:0000250"
FT DOMAIN 577..606
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 71..85
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 305
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250"
FT BINDING 306
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250"
FT BINDING 561
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 586
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 589
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 592
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT MOD_RES 96
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q921G7"
FT MOD_RES 132
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q921G7"
FT MOD_RES 223
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q921G7"
FT MOD_RES 357
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q921G7"
FT MOD_RES 551
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16134"
SQ SEQUENCE 617 AA; 68397 MW; F90CFB115AF3D5A2 CRC64;
MLVPLAKLSC PAYQCFHALK IKKNYLPLCA TRWSSTSTVP RITTHYTIYP RDKDKRWEGV
NMERFAEGAD VVIVGAGPAG LSAAVRLKQL AAAHEKDIRV CLVEKAAQIG AHTLSGACLD
PGAFKELFPD WKEKGAPLNT PVTEDRFGIL TEKYRIPVPI LPGLPMNNHG NYIVRLGHLV
SWMGEQAEAL GVEVYPGYAA AEVLFHDDGS VKGIATNDVG IQKDGAPKAT FERGLELHAK
VTIFAEGCHG HLAKQLYKKF DLRANCEPQT YGIGLKELWV IDEKNWKPGR VDHTVGWPLD
RHTYGGSFLY HLNEGEPLVA LGLVVGLDYQ NPYLSPFREF QRWKHHPSIR PTLEGGKRIA
YGARALNEGG FQSIPKLTFP GGLLIGCSPG FMNVPKIKGT HTAMKSGILA AESIFNQLTS
ENLQSKTMGL HVTEYEDNLK NSWVWKELYS VRNIRPSCHG VLGVYGGMIY TGIFYWILRG
MEPWTLKHKG SDFERLKPAK DCTPIEYPKP DGQISFDLLS SVALSGTNHE HDQPAHLTLR
DDSIPVNRNL SIYDGPEQRF CPAGVYEFVP VEQGDGFRLQ INAQNCVHCK TCDIKDPSQN
INWVVPEGGG GPAYNGM
