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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)DescriptionActionsGraphical viewLength
Binding sitei305Ubiquinone; via carbonyl oxygen1 Publication1
Binding sitei306Ubiquinone; via amide nitrogen1 Publication1
Metal bindingi561Iron-sulfur (4Fe-4S)1
Metal bindingi586Iron-sulfur (4Fe-4S)1
Metal bindingi589Iron-sulfur (4Fe-4S)1
Metal bindingi592Iron-sulfur (4Fe-4S)1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi75 – 80FAD1 Publication6

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

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)DescriptionActionsGraphical viewLength
Intramembranei109 – 130Add BLAST22
Intramembranei428 – 447Add BLAST20

GO - Cellular componenti

  • integral component of mitochondrial inner membrane Source: GO_Central
  • membrane Source: UniProtKB
  • mitochondrial electron transfer flavoprotein complex Source: GO_Central
  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 33MitochondrionSequence analysisAdd BLAST33
ChainiPRO_000000866334 – 617Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrialAdd BLAST584

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei96N6-acetyllysineBy similarity1
Modified residuei132N6-acetyllysineBy similarity1
Modified residuei223N6-acetyllysineBy similarity1
Modified residuei357N6-acetyllysineBy similarity1
Modified residuei551PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP55931.
PeptideAtlasiP55931.
PRIDEiP55931.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000009469.

Structurei

Secondary structure

1617
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni46 – 48Combined sources3
Helixi55 – 57Combined sources3
Beta strandi66 – 68Combined sources3
Beta strandi70 – 74Combined sources5
Helixi78 – 93Combined sources16
Beta strandi100 – 103Combined sources4
Beta strandi105 – 108Combined sources4
Turni109 – 112Combined sources4
Helixi122 – 127Combined sources6
Helixi131 – 134Combined sources4
Beta strandi144 – 150Combined sources7
Beta strandi155 – 157Combined sources3
Beta strandi162 – 164Combined sources3
Helixi176 – 189Combined sources14
Beta strandi193 – 195Combined sources3
Beta strandi200 – 205Combined sources6
Beta strandi209 – 216Combined sources8
Beta strandi219 – 221Combined sources3
Beta strandi227 – 232Combined sources6
Beta strandi236 – 238Combined sources3
Beta strandi240 – 244Combined sources5
Helixi251 – 259Combined sources9
Turni260 – 265Combined sources6
Beta strandi271 – 280Combined sources10
Helixi283 – 285Combined sources3
Beta strandi290 – 296Combined sources7
Beta strandi305 – 311Combined sources7
Beta strandi314 – 316Combined sources3
Beta strandi318 – 326Combined sources9
Helixi336 – 343Combined sources8
Turni347 – 349Combined sources3
Helixi350 – 353Combined sources4
Beta strandi357 – 367Combined sources11
Helixi370 – 373Combined sources4
Beta strandi382 – 384Combined sources3
Turni386 – 389Combined sources4
Turni394 – 397Combined sources4
Helixi400 – 418Combined sources19
Beta strandi426 – 429Combined sources4
Helixi434 – 440Combined sources7
Helixi443 – 450Combined sources8
Turni451 – 455Combined sources5
Helixi456 – 459Combined sources4
Turni461 – 463Combined sources3
Helixi464 – 474Combined sources11
Turni475 – 480Combined sources6
Helixi492 – 494Combined sources3
Helixi499 – 501Combined sources3
Beta strandi512 – 515Combined sources4
Helixi518 – 523Combined sources6
Turni524 – 526Combined sources3
Beta strandi531 – 533Combined sources3
Beta strandi536 – 541Combined sources6
Helixi544 – 547Combined sources4
Helixi549 – 553Combined sources5
Helixi557 – 560Combined sources4
Beta strandi566 – 570Combined sources5
Beta strandi572 – 575Combined sources4
Beta strandi577 – 581Combined sources5
Helixi583 – 585Combined sources3
Helixi591 – 595Combined sources5
Beta strandi601 – 603Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GMHX-ray2.50A/B34-617[»]
2GMJX-ray2.60A/B34-617[»]
SMRiP55931.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP55931.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini577 – 6064Fe-4S ferredoxin-typePROSITE-ProRule annotationAdd BLAST30

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)DescriptionActionsGraphical viewLength
Sequence conflicti37C → S in EW134518 (PubMed:17407547).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GMHX-ray2.50A/B34-617[»]
2GMJX-ray2.60A/B34-617[»]
SMRiP55931.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000009469.

Proteomic databases

PaxDbiP55931.
PeptideAtlasiP55931.
PRIDEiP55931.

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...

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: November 30, 2016
This is version 105 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.