ETFD_PIG
ID ETFD_PIG Reviewed; 617 AA.
AC P55931;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 125.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-617, AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Fetal liver;
RX PubMed=8306995; DOI=10.1111/j.1432-1033.1994.tb19939.x;
RA Goodman S.I., Axtell K.M., Bindoff L.A., Beard S.E., Gill R.E.,
RA Frerman F.E.;
RT "Molecular cloning and expression of a cDNA encoding human electron
RT transfer flavoprotein-ubiquinone oxidoreductase.";
RL Eur. J. Biochem. 219:277-286(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-103.
RX PubMed=17407547; DOI=10.1186/gb-2007-8-4-r45;
RA Gorodkin J., Cirera S., Hedegaard J., Gilchrist M.J., Panitz F.,
RA Jorgensen C.B., Scheibye-Knudsen K., Arvin T., Lumholdt S., Sawera M.,
RA Green T., Nielsen B.J., Havgaard J.H., Rosenkilde C., Wang J., Li H.,
RA Li R., Liu B., Hu S., Dong W., Li W., Yu J., Wang J., Staerfeldt H.H.,
RA Wernersson R., Madsen L.B., Thomsen B., Hornshoj H., Bujie Z., Wang X.,
RA Wang X., Bolund L., Brunak S., Yang H., Bendixen C., Fredholm M.;
RT "Porcine transcriptome analysis based on 97 non-normalized cDNA libraries
RT and assembly of 1,021,891 expressed sequence tags.";
RL Genome Biol. 8:R45.1-R45.16(2007).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 24-607 IN COMPLEX WITH FAD AND
RP UBIQUINONE, SUBUNIT, AND IRON-SULFUR BINDING SITES.
RX PubMed=17050691; DOI=10.1073/pnas.0604567103;
RA Zhang J., Frerman F.E., Kim J.J.;
RT "Structure of electron transfer flavoprotein-ubiquinone oxidoreductase and
RT electron transfer to the mitochondrial ubiquinone pool.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:16212-16217(2006).
CC -!- FUNCTION: Accepts electrons from ETF and reduces ubiquinone.
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;
CC Note=Binds 1 [4Fe-4S] cluster.;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17050691}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}.
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DR EMBL; EW134518; -; NOT_ANNOTATED_CDS; mRNA.
DR PDB; 2GMH; X-ray; 2.50 A; A/B=34-617.
DR PDB; 2GMJ; X-ray; 2.60 A; A/B=34-617.
DR PDBsum; 2GMH; -.
DR PDBsum; 2GMJ; -.
DR AlphaFoldDB; P55931; -.
DR SMR; P55931; -.
DR STRING; 9823.ENSSSCP00000009469; -.
DR PaxDb; P55931; -.
DR PeptideAtlas; P55931; -.
DR PRIDE; P55931; -.
DR eggNOG; KOG2415; Eukaryota.
DR InParanoid; P55931; -.
DR EvolutionaryTrace; P55931; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0009055; F:electron transfer activity; IDA:UniProtKB.
DR GO; GO:0004174; F:electron-transferring-flavoprotein dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0048039; F:ubiquinone binding; IDA:UniProtKB.
DR GO; GO:0022900; P:electron transport chain; IDA:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Acetylation; Direct protein sequencing;
KW Electron transport; FAD; Flavoprotein; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW Phosphoprotein; 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_0000008663"
FT INTRAMEM 109..130
FT INTRAMEM 428..447
FT DOMAIN 577..606
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 75..80
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17050691"
FT BINDING 305
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000269|PubMed:17050691"
FT BINDING 306
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000269|PubMed:17050691"
FT BINDING 561
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 586
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 589
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 592
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
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"
FT CONFLICT 37
FT /note="C -> S (in Ref. 2; EW134518)"
FT /evidence="ECO:0000305"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:2GMH"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:2GMH"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:2GMH"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:2GMH"
FT HELIX 78..93
FT /evidence="ECO:0007829|PDB:2GMH"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:2GMH"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:2GMH"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:2GMH"
FT HELIX 122..127
FT /evidence="ECO:0007829|PDB:2GMH"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:2GMH"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:2GMH"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:2GMH"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:2GMJ"
FT HELIX 176..189
FT /evidence="ECO:0007829|PDB:2GMH"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:2GMH"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:2GMH"
FT STRAND 209..216
FT /evidence="ECO:0007829|PDB:2GMH"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:2GMH"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:2GMH"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:2GMH"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:2GMH"
FT HELIX 251..259
FT /evidence="ECO:0007829|PDB:2GMH"
FT TURN 260..265
FT /evidence="ECO:0007829|PDB:2GMH"
FT STRAND 271..280
FT /evidence="ECO:0007829|PDB:2GMH"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:2GMH"
FT STRAND 290..296
FT /evidence="ECO:0007829|PDB:2GMH"
FT STRAND 305..311
FT /evidence="ECO:0007829|PDB:2GMH"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:2GMH"
FT STRAND 318..326
FT /evidence="ECO:0007829|PDB:2GMH"
FT HELIX 336..343
FT /evidence="ECO:0007829|PDB:2GMH"
FT TURN 347..349
FT /evidence="ECO:0007829|PDB:2GMH"
FT HELIX 350..353
FT /evidence="ECO:0007829|PDB:2GMH"
FT STRAND 357..367
FT /evidence="ECO:0007829|PDB:2GMH"
FT HELIX 370..373
FT /evidence="ECO:0007829|PDB:2GMH"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:2GMH"
FT TURN 386..389
FT /evidence="ECO:0007829|PDB:2GMH"
FT TURN 394..397
FT /evidence="ECO:0007829|PDB:2GMH"
FT HELIX 400..418
FT /evidence="ECO:0007829|PDB:2GMH"
FT STRAND 426..429
FT /evidence="ECO:0007829|PDB:2GMH"
FT HELIX 434..440
FT /evidence="ECO:0007829|PDB:2GMH"
FT HELIX 443..450
FT /evidence="ECO:0007829|PDB:2GMH"
FT TURN 451..455
FT /evidence="ECO:0007829|PDB:2GMH"
FT HELIX 456..459
FT /evidence="ECO:0007829|PDB:2GMH"
FT TURN 461..463
FT /evidence="ECO:0007829|PDB:2GMH"
FT HELIX 464..474
FT /evidence="ECO:0007829|PDB:2GMH"
FT TURN 475..480
FT /evidence="ECO:0007829|PDB:2GMH"
FT HELIX 492..494
FT /evidence="ECO:0007829|PDB:2GMH"
FT HELIX 499..501
FT /evidence="ECO:0007829|PDB:2GMH"
FT STRAND 512..515
FT /evidence="ECO:0007829|PDB:2GMH"
FT HELIX 518..523
FT /evidence="ECO:0007829|PDB:2GMH"
FT TURN 524..526
FT /evidence="ECO:0007829|PDB:2GMH"
FT STRAND 531..533
FT /evidence="ECO:0007829|PDB:2GMH"
FT STRAND 536..541
FT /evidence="ECO:0007829|PDB:2GMH"
FT HELIX 544..547
FT /evidence="ECO:0007829|PDB:2GMH"
FT HELIX 549..553
FT /evidence="ECO:0007829|PDB:2GMH"
FT HELIX 557..560
FT /evidence="ECO:0007829|PDB:2GMH"
FT STRAND 566..570
FT /evidence="ECO:0007829|PDB:2GMH"
FT STRAND 572..575
FT /evidence="ECO:0007829|PDB:2GMH"
FT STRAND 577..581
FT /evidence="ECO:0007829|PDB:2GMH"
FT HELIX 583..585
FT /evidence="ECO:0007829|PDB:2GMH"
FT HELIX 591..595
FT /evidence="ECO:0007829|PDB:2GMH"
FT STRAND 601..603
FT /evidence="ECO:0007829|PDB:2GMH"
SQ SEQUENCE 617 AA; 68632 MW; 6129A764E2B76393 CRC64;
MMVPLAKLAS PAYQCFHALK IKKNYLPLCA TRWSSTCKVP RITTHYTIYP RDQDKRWEGV
NMERFAEEAD VVIVGAGPAG LSAATRLKQL AAQHEKDLRV CLVEKAAHIG AHTLSGACLD
PRAFEELFPD WKEKGAPLNT PVTEDRFGIL TEKYRIPVPI LPGLPMNNHG NYVVRLGHLV
SWMGEQAEAL GVEVYPGYAA AEILFHEDGS VKGIATNDVG IQKDGAPKTT FERGLELHAK
VTIFAEGCHG HLAKQLYKKF DLRANCEPQT YGIGLKELWV IDEKKWKPGR VDHTVGWPLD
RHTYGGSFLY HLNEGEPLLA LGFVVGLDYQ NPYLSPFREF QRWKHHPSIK PTLEGGKRIA
YGARALNEGG FQSIPKLTFP GGLLIGCSPG FMNVPKIKGT HTAMKSGTLA AESIFNQLTS
ENLQSKTIGL HVTEYEDNLK NSWVWKELYS VRNIRPSCHG ILGVYGGMIY TGIFYWIFRG
MEPWTLKHKG SDSDQLKPAK DCTPIEYPKP DGQISFDLLS SVALSGTNHE HDQPAHLTLK
DDSVPVNRNL SIYDGPEQRF CPAGVYEFVP LEQGDGFRLQ INAQNCVHCK TCDIKDPSQN
INWVVPEGGG GPAYNGM
