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Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial (ETF-QO) (ETF-ubiquinone oxidoreductase) (EC 1.5.5.1) (Electron-transferring-flavoprotein dehydrogenase) (ETF dehydrogenase)

 ETFD_PIG                Reviewed;         617 AA.
P55931;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
15-JUN-2010, sequence version 2.
05-DEC-2018, entry version 113.
RecName: Full=Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial;
Short=ETF-QO;
Short=ETF-ubiquinone oxidoreductase;
EC=1.5.5.1;
AltName: Full=Electron-transferring-flavoprotein dehydrogenase;
Short=ETF dehydrogenase;
Flags: Precursor;
Name=ETFDH;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA] OF 11-617, AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Fetal liver;
PubMed=8306995; DOI=10.1111/j.1432-1033.1994.tb19939.x;
Goodman S.I., Axtell K.M., Bindoff L.A., Beard S.E., Gill R.E.,
Frerman F.E.;
"Molecular cloning and expression of a cDNA encoding human electron
transfer flavoprotein-ubiquinone oxidoreductase.";
Eur. J. Biochem. 219:277-286(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-103.
PubMed=17407547; DOI=10.1186/gb-2007-8-4-r45;
Gorodkin J., Cirera S., Hedegaard J., Gilchrist M.J., Panitz F.,
Jorgensen C.B., Scheibye-Knudsen K., Arvin T., Lumholdt S., Sawera M.,
Green T., Nielsen B.J., Havgaard J.H., Rosenkilde C., Wang J., Li H.,
Li R., Liu B., Hu S., Dong W., Li W., Yu J., Wang J., Staerfeldt H.H.,
Wernersson R., Madsen L.B., Thomsen B., Hornshoj H., Bujie Z.,
Wang X., Wang X., Bolund L., Brunak S., Yang H., Bendixen C.,
Fredholm M.;
"Porcine transcriptome analysis based on 97 non-normalized cDNA
libraries and assembly of 1,021,891 expressed sequence tags.";
Genome Biol. 8:R45.1-R45.16(2007).
[3]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 24-607 IN COMPLEX WITH FAD
AND UBIQUINONE, SUBUNIT, AND IRON-SULFUR BINDING SITES.
PubMed=17050691; DOI=10.1073/pnas.0604567103;
Zhang J., Frerman F.E., Kim J.J.;
"Structure of electron transfer flavoprotein-ubiquinone oxidoreductase
and electron transfer to the mitochondrial ubiquinone pool.";
Proc. Natl. Acad. Sci. U.S.A. 103:16212-16217(2006).
-!- FUNCTION: Accepts electrons from ETF and reduces ubiquinone.
-!- CATALYTIC ACTIVITY:
Reaction=a ubiquinone + reduced [electron-transfer flavoprotein] =
a ubiquinol + H(+) + oxidized [electron-transfer flavoprotein];
Xref=Rhea:RHEA:24052, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566,
Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57692,
ChEBI:CHEBI:58307; EC=1.5.5.1;
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Note=Binds 1 [4Fe-4S] cluster.;
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17050691}.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}.
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EMBL; EW134518; -; NOT_ANNOTATED_CDS; mRNA.
UniGene; Ssc.6919; -.
PDB; 2GMH; X-ray; 2.50 A; A/B=34-617.
PDB; 2GMJ; X-ray; 2.60 A; A/B=34-617.
PDBsum; 2GMH; -.
PDBsum; 2GMJ; -.
SMR; P55931; -.
STRING; 9823.ENSSSCP00000009469; -.
PaxDb; P55931; -.
PeptideAtlas; P55931; -.
PRIDE; P55931; -.
eggNOG; KOG2415; Eukaryota.
eggNOG; COG0644; LUCA.
HOGENOM; HOG000259450; -.
HOVERGEN; HBG005615; -.
InParanoid; P55931; -.
EvolutionaryTrace; P55931; -.
Proteomes; UP000008227; Unplaced.
GO; GO:0031305; C:integral component of mitochondrial inner membrane; IBA:GO_Central.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:UniProtKB.
GO; GO:0009055; F:electron transfer activity; IDA:UniProtKB.
GO; GO:0004174; F:electron-transferring-flavoprotein dehydrogenase activity; IDA:UniProtKB.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
GO; GO:0051536; F:iron-sulfur cluster binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
GO; GO:0043783; F:oxidoreductase activity, oxidizing metal ions with flavin as acceptor; IDA:UniProtKB.
GO; GO:0048039; F:ubiquinone binding; IDA:UniProtKB.
GO; GO:0022900; P:electron transport chain; IDA:UniProtKB.
GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
Gene3D; 3.50.50.60; -; 1.
InterPro; IPR017896; 4Fe4S_Fe-S-bd.
InterPro; IPR040156; ETF-QO.
InterPro; IPR036188; FAD/NAD-bd_sf.
PANTHER; PTHR10617; PTHR10617; 1.
SUPFAM; SSF51905; SSF51905; 1.
PROSITE; PS51379; 4FE4S_FER_2; 1.
1: Evidence at protein level;
3D-structure; 4Fe-4S; Acetylation; Complete proteome;
Direct protein sequencing; Electron transport; FAD; Flavoprotein;
Iron; Iron-sulfur; Membrane; Metal-binding; Mitochondrion;
Mitochondrion inner membrane; Oxidoreductase; Phosphoprotein;
Reference proteome; Transit peptide; Transport; Ubiquinone.
TRANSIT 1 33 Mitochondrion. {ECO:0000255}.
CHAIN 34 617 Electron transfer flavoprotein-ubiquinone
oxidoreductase, mitochondrial.
/FTId=PRO_0000008663.
INTRAMEM 109 130
INTRAMEM 428 447
DOMAIN 577 606 4Fe-4S ferredoxin-type.
{ECO:0000255|PROSITE-ProRule:PRU00711}.
NP_BIND 75 80 FAD. {ECO:0000269|PubMed:17050691}.
METAL 561 561 Iron-sulfur (4Fe-4S).
METAL 586 586 Iron-sulfur (4Fe-4S).
METAL 589 589 Iron-sulfur (4Fe-4S).
METAL 592 592 Iron-sulfur (4Fe-4S).
BINDING 305 305 Ubiquinone; via carbonyl oxygen.
{ECO:0000269|PubMed:17050691}.
BINDING 306 306 Ubiquinone; via amide nitrogen.
{ECO:0000269|PubMed:17050691}.
MOD_RES 96 96 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q921G7}.
MOD_RES 132 132 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q921G7}.
MOD_RES 223 223 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q921G7}.
MOD_RES 357 357 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q921G7}.
MOD_RES 551 551 Phosphoserine.
{ECO:0000250|UniProtKB:Q16134}.
CONFLICT 37 37 C -> S (in Ref. 2; EW134518).
{ECO:0000305}.
TURN 46 48 {ECO:0000244|PDB:2GMH}.
HELIX 55 57 {ECO:0000244|PDB:2GMH}.
STRAND 66 68 {ECO:0000244|PDB:2GMH}.
STRAND 70 74 {ECO:0000244|PDB:2GMH}.
HELIX 78 93 {ECO:0000244|PDB:2GMH}.
STRAND 100 103 {ECO:0000244|PDB:2GMH}.
STRAND 105 108 {ECO:0000244|PDB:2GMH}.
TURN 109 112 {ECO:0000244|PDB:2GMH}.
HELIX 122 127 {ECO:0000244|PDB:2GMH}.
HELIX 131 134 {ECO:0000244|PDB:2GMH}.
STRAND 144 150 {ECO:0000244|PDB:2GMH}.
STRAND 155 157 {ECO:0000244|PDB:2GMH}.
STRAND 162 164 {ECO:0000244|PDB:2GMJ}.
HELIX 176 189 {ECO:0000244|PDB:2GMH}.
STRAND 193 195 {ECO:0000244|PDB:2GMH}.
STRAND 200 205 {ECO:0000244|PDB:2GMH}.
STRAND 209 216 {ECO:0000244|PDB:2GMH}.
STRAND 219 221 {ECO:0000244|PDB:2GMH}.
STRAND 227 232 {ECO:0000244|PDB:2GMH}.
STRAND 236 238 {ECO:0000244|PDB:2GMH}.
STRAND 240 244 {ECO:0000244|PDB:2GMH}.
HELIX 251 259 {ECO:0000244|PDB:2GMH}.
TURN 260 265 {ECO:0000244|PDB:2GMH}.
STRAND 271 280 {ECO:0000244|PDB:2GMH}.
HELIX 283 285 {ECO:0000244|PDB:2GMH}.
STRAND 290 296 {ECO:0000244|PDB:2GMH}.
STRAND 305 311 {ECO:0000244|PDB:2GMH}.
STRAND 314 316 {ECO:0000244|PDB:2GMH}.
STRAND 318 326 {ECO:0000244|PDB:2GMH}.
HELIX 336 343 {ECO:0000244|PDB:2GMH}.
TURN 347 349 {ECO:0000244|PDB:2GMH}.
HELIX 350 353 {ECO:0000244|PDB:2GMH}.
STRAND 357 367 {ECO:0000244|PDB:2GMH}.
HELIX 370 373 {ECO:0000244|PDB:2GMH}.
STRAND 382 384 {ECO:0000244|PDB:2GMH}.
TURN 386 389 {ECO:0000244|PDB:2GMH}.
TURN 394 397 {ECO:0000244|PDB:2GMH}.
HELIX 400 418 {ECO:0000244|PDB:2GMH}.
STRAND 426 429 {ECO:0000244|PDB:2GMH}.
HELIX 434 440 {ECO:0000244|PDB:2GMH}.
HELIX 443 450 {ECO:0000244|PDB:2GMH}.
TURN 451 455 {ECO:0000244|PDB:2GMH}.
HELIX 456 459 {ECO:0000244|PDB:2GMH}.
TURN 461 463 {ECO:0000244|PDB:2GMH}.
HELIX 464 474 {ECO:0000244|PDB:2GMH}.
TURN 475 480 {ECO:0000244|PDB:2GMH}.
HELIX 492 494 {ECO:0000244|PDB:2GMH}.
HELIX 499 501 {ECO:0000244|PDB:2GMH}.
STRAND 512 515 {ECO:0000244|PDB:2GMH}.
HELIX 518 523 {ECO:0000244|PDB:2GMH}.
TURN 524 526 {ECO:0000244|PDB:2GMH}.
STRAND 531 533 {ECO:0000244|PDB:2GMH}.
STRAND 536 541 {ECO:0000244|PDB:2GMH}.
HELIX 544 547 {ECO:0000244|PDB:2GMH}.
HELIX 549 553 {ECO:0000244|PDB:2GMH}.
HELIX 557 560 {ECO:0000244|PDB:2GMH}.
STRAND 566 570 {ECO:0000244|PDB:2GMH}.
STRAND 572 575 {ECO:0000244|PDB:2GMH}.
STRAND 577 581 {ECO:0000244|PDB:2GMH}.
HELIX 583 585 {ECO:0000244|PDB:2GMH}.
HELIX 591 595 {ECO:0000244|PDB:2GMH}.
STRAND 601 603 {ECO:0000244|PDB:2GMH}.
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


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