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Protein

Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial

Gene

ETFDH

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Accepts electrons from ETF and reduces ubiquinone.

Catalytic activityi

Reduced electron-transferring flavoprotein + ubiquinone = electron-transferring flavoprotein + ubiquinol.

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei305 – 3051Ubiquinone; via carbonyl oxygen1 Publication
Binding sitei306 – 3061Ubiquinone; via amide nitrogen1 Publication
Metal bindingi561 – 5611Iron-sulfur (4Fe-4S)
Metal bindingi586 – 5861Iron-sulfur (4Fe-4S)
Metal bindingi589 – 5891Iron-sulfur (4Fe-4S)
Metal bindingi592 – 5921Iron-sulfur (4Fe-4S)

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi75 – 806FAD1 Publication

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: UniProtKB
  • electron carrier activity Source: UniProtKB
  • electron-transferring-flavoprotein dehydrogenase activity Source: UniProtKB
  • flavin adenine dinucleotide binding Source: UniProtKB
  • iron-sulfur cluster binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • oxidoreductase activity Source: UniProtKB
  • oxidoreductase activity, oxidizing metal ions with flavin as acceptor Source: UniProtKB
  • ubiquinone binding Source: UniProtKB

GO - Biological processi

  • electron transport chain Source: UniProtKB
  • response to oxidative stress Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

4Fe-4S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Ubiquinone

Names & Taxonomyi

Protein namesi
Recommended name:
Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial (EC:1.5.5.1)
Short name:
ETF-QO
Short name:
ETF-ubiquinone oxidoreductase
Alternative name(s):
Electron-transferring-flavoprotein dehydrogenase
Short name:
ETF dehydrogenase
Gene namesi
Name:ETFDH
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Intramembranei109 – 13022Add
BLAST
Intramembranei428 – 44720Add
BLAST

GO - Cellular componenti

  • membrane Source: UniProtKB
  • mitochondrial inner membrane Source: UniProtKB-SubCell
  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3333MitochondrionSequence analysisAdd
BLAST
Chaini34 – 617584Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrialPRO_0000008663Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei96 – 961N6-acetyllysineBy similarity
Modified residuei132 – 1321N6-acetyllysineBy similarity
Modified residuei223 – 2231N6-acetyllysineBy similarity
Modified residuei357 – 3571N6-acetyllysineBy similarity
Modified residuei551 – 5511PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP55931.
PeptideAtlasiP55931.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000009469.

Structurei

Secondary structure

1
617
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni46 – 483Combined sources
Helixi55 – 573Combined sources
Beta strandi66 – 683Combined sources
Beta strandi70 – 745Combined sources
Helixi78 – 9316Combined sources
Beta strandi100 – 1034Combined sources
Beta strandi105 – 1084Combined sources
Turni109 – 1124Combined sources
Helixi122 – 1276Combined sources
Helixi131 – 1344Combined sources
Beta strandi144 – 1507Combined sources
Beta strandi155 – 1573Combined sources
Beta strandi162 – 1643Combined sources
Helixi176 – 18914Combined sources
Beta strandi193 – 1953Combined sources
Beta strandi200 – 2056Combined sources
Beta strandi209 – 2168Combined sources
Beta strandi219 – 2213Combined sources
Beta strandi227 – 2326Combined sources
Beta strandi236 – 2383Combined sources
Beta strandi240 – 2445Combined sources
Helixi251 – 2599Combined sources
Turni260 – 2656Combined sources
Beta strandi271 – 28010Combined sources
Helixi283 – 2853Combined sources
Beta strandi290 – 2967Combined sources
Beta strandi305 – 3117Combined sources
Beta strandi314 – 3163Combined sources
Beta strandi318 – 3269Combined sources
Helixi336 – 3438Combined sources
Turni347 – 3493Combined sources
Helixi350 – 3534Combined sources
Beta strandi357 – 36711Combined sources
Helixi370 – 3734Combined sources
Beta strandi382 – 3843Combined sources
Turni386 – 3894Combined sources
Turni394 – 3974Combined sources
Helixi400 – 41819Combined sources
Beta strandi426 – 4294Combined sources
Helixi434 – 4407Combined sources
Helixi443 – 4508Combined sources
Turni451 – 4555Combined sources
Helixi456 – 4594Combined sources
Turni461 – 4633Combined sources
Helixi464 – 47411Combined sources
Turni475 – 4806Combined sources
Helixi492 – 4943Combined sources
Helixi499 – 5013Combined sources
Beta strandi512 – 5154Combined sources
Helixi518 – 5236Combined sources
Turni524 – 5263Combined sources
Beta strandi531 – 5333Combined sources
Beta strandi536 – 5416Combined sources
Helixi544 – 5474Combined sources
Helixi549 – 5535Combined sources
Helixi557 – 5604Combined sources
Beta strandi566 – 5705Combined sources
Beta strandi572 – 5754Combined sources
Beta strandi577 – 5815Combined sources
Helixi583 – 5853Combined sources
Helixi591 – 5955Combined sources
Beta strandi601 – 6033Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GMHX-ray2.50A/B34-617[»]
2GMJX-ray2.60A/B34-617[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP55931.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini577 – 606304Fe-4S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 4Fe-4S ferredoxin-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2415. Eukaryota.
COG0644. LUCA.
HOGENOMiHOG000259450.
HOVERGENiHBG005615.
InParanoidiP55931.

Family and domain databases

Gene3Di3.50.50.60. 1 hit.
InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR007859. ETFD_OxRdtase/FixX.
IPR023753. FAD/NAD-binding_dom.
[Graphical view]
PANTHERiPTHR10617:SF107. PTHR10617:SF107. 1 hit.
PfamiPF05187. ETF_QO. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
PROSITEiPS51379. 4FE4S_FER_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P55931-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMVPLAKLAS PAYQCFHALK IKKNYLPLCA TRWSSTCKVP RITTHYTIYP
60 70 80 90 100
RDQDKRWEGV NMERFAEEAD VVIVGAGPAG LSAATRLKQL AAQHEKDLRV
110 120 130 140 150
CLVEKAAHIG AHTLSGACLD PRAFEELFPD WKEKGAPLNT PVTEDRFGIL
160 170 180 190 200
TEKYRIPVPI LPGLPMNNHG NYVVRLGHLV SWMGEQAEAL GVEVYPGYAA
210 220 230 240 250
AEILFHEDGS VKGIATNDVG IQKDGAPKTT FERGLELHAK VTIFAEGCHG
260 270 280 290 300
HLAKQLYKKF DLRANCEPQT YGIGLKELWV IDEKKWKPGR VDHTVGWPLD
310 320 330 340 350
RHTYGGSFLY HLNEGEPLLA LGFVVGLDYQ NPYLSPFREF QRWKHHPSIK
360 370 380 390 400
PTLEGGKRIA YGARALNEGG FQSIPKLTFP GGLLIGCSPG FMNVPKIKGT
410 420 430 440 450
HTAMKSGTLA AESIFNQLTS ENLQSKTIGL HVTEYEDNLK NSWVWKELYS
460 470 480 490 500
VRNIRPSCHG ILGVYGGMIY TGIFYWIFRG MEPWTLKHKG SDSDQLKPAK
510 520 530 540 550
DCTPIEYPKP DGQISFDLLS SVALSGTNHE HDQPAHLTLK DDSVPVNRNL
560 570 580 590 600
SIYDGPEQRF CPAGVYEFVP LEQGDGFRLQ INAQNCVHCK TCDIKDPSQN
610
INWVVPEGGG GPAYNGM
Length:617
Mass (Da):68,632
Last modified:June 15, 2010 - v2
Checksum:i6129A764E2B76393
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 371C → S in EW134518 (PubMed:17407547).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EW134518 mRNA. No translation available.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EW134518 mRNA. No translation available.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GMHX-ray2.50A/B34-617[»]
2GMJX-ray2.60A/B34-617[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000009469.

Proteomic databases

PaxDbiP55931.
PeptideAtlasiP55931.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG2415. Eukaryota.
COG0644. LUCA.
HOGENOMiHOG000259450.
HOVERGENiHBG005615.
InParanoidiP55931.

Miscellaneous databases

EvolutionaryTraceiP55931.

Family and domain databases

Gene3Di3.50.50.60. 1 hit.
InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR007859. ETFD_OxRdtase/FixX.
IPR023753. FAD/NAD-binding_dom.
[Graphical view]
PANTHERiPTHR10617:SF107. PTHR10617:SF107. 1 hit.
PfamiPF05187. ETF_QO. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
PROSITEiPS51379. 4FE4S_FER_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning and expression of a cDNA encoding human electron transfer flavoprotein-ubiquinone oxidoreductase."
    Goodman S.I., Axtell K.M., Bindoff L.A., Beard S.E., Gill R.E., Frerman F.E.
    Eur. J. Biochem. 219:277-286(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-617, PARTIAL PROTEIN SEQUENCE.
    Tissue: Fetal liver.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-103.
  3. "Structure of electron transfer flavoprotein-ubiquinone oxidoreductase and electron transfer to the mitochondrial ubiquinone pool."
    Zhang J., Frerman F.E., Kim J.J.
    Proc. Natl. Acad. Sci. U.S.A. 103:16212-16217(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 24-607 IN COMPLEX WITH FAD AND UBIQUINONE, SUBUNIT, IRON-SULFUR BINDING SITES.

Entry informationi

Entry nameiETFD_PIG
AccessioniPrimary (citable) accession number: P55931
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 15, 2010
Last modified: July 6, 2016
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.