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P55931 (ETFD_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial
Short name=ETF-QO
Short name=ETF-ubiquinone oxidoreductase
EC=1.5.5.1
Alternative name(s):
Electron-transferring-flavoprotein dehydrogenase
Short name=ETF dehydrogenase
Gene names
Name:ETFDH
OrganismSus scrofa (Pig) [Complete proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length617 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Accepts electrons from ETF and reduces ubiquinone.

Catalytic activity

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

Cofactor

Binds 1 4Fe-4S cluster.

FAD.

Subunit structure

Monomer. Ref.3

Subcellular location

Mitochondrion inner membrane By similarity.

Sequence similarities

Contains 1 4Fe-4S ferredoxin-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3333Mitochondrion Potential
Chain34 – 617584Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial
PRO_0000008663

Regions

Intramembrane109 – 13022
Intramembrane428 – 44720
Domain577 – 606304Fe-4S ferredoxin-type
Nucleotide binding75 – 806FAD

Sites

Metal binding5611Iron-sulfur (4Fe-4S)
Metal binding5861Iron-sulfur (4Fe-4S)
Metal binding5891Iron-sulfur (4Fe-4S)
Metal binding5921Iron-sulfur (4Fe-4S)
Binding site3051Ubiquinone; via carbonyl oxygen
Binding site3061Ubiquinone; via amide nitrogen

Amino acid modifications

Modified residue961N6-acetyllysine By similarity
Modified residue1531N6-acetyllysine By similarity
Modified residue2231N6-acetyllysine By similarity
Modified residue3441N6-acetyllysine By similarity

Experimental info

Sequence conflict371C → S in EW134518. Ref.2

Secondary structure

1 ................................................................................................................... 617
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P55931 [UniParc].

Last modified June 15, 2010. Version 2.
Checksum: 6129A764E2B76393

FASTA61768,632
        10         20         30         40         50         60 
MMVPLAKLAS PAYQCFHALK IKKNYLPLCA TRWSSTCKVP RITTHYTIYP RDQDKRWEGV 

        70         80         90        100        110        120 
NMERFAEEAD VVIVGAGPAG LSAATRLKQL AAQHEKDLRV CLVEKAAHIG AHTLSGACLD 

       130        140        150        160        170        180 
PRAFEELFPD WKEKGAPLNT PVTEDRFGIL TEKYRIPVPI LPGLPMNNHG NYVVRLGHLV 

       190        200        210        220        230        240 
SWMGEQAEAL GVEVYPGYAA AEILFHEDGS VKGIATNDVG IQKDGAPKTT FERGLELHAK 

       250        260        270        280        290        300 
VTIFAEGCHG HLAKQLYKKF DLRANCEPQT YGIGLKELWV IDEKKWKPGR VDHTVGWPLD 

       310        320        330        340        350        360 
RHTYGGSFLY HLNEGEPLLA LGFVVGLDYQ NPYLSPFREF QRWKHHPSIK PTLEGGKRIA 

       370        380        390        400        410        420 
YGARALNEGG FQSIPKLTFP GGLLIGCSPG FMNVPKIKGT HTAMKSGTLA AESIFNQLTS 

       430        440        450        460        470        480 
ENLQSKTIGL HVTEYEDNLK NSWVWKELYS VRNIRPSCHG ILGVYGGMIY TGIFYWIFRG 

       490        500        510        520        530        540 
MEPWTLKHKG SDSDQLKPAK DCTPIEYPKP DGQISFDLLS SVALSGTNHE HDQPAHLTLK 

       550        560        570        580        590        600 
DDSVPVNRNL SIYDGPEQRF CPAGVYEFVP LEQGDGFRLQ INAQNCVHCK TCDIKDPSQN 

       610 
INWVVPEGGG GPAYNGM

« Hide

References

[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: 8306995] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-617, PARTIAL PROTEIN SEQUENCE.
Tissue: Fetal liver.
[2]"Porcine transcriptome analysis based on 97 non-normalized cDNA libraries and assembly of 1,021,891 expressed sequence tags."
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. expand/collapse author list , 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.
Genome Biol. 8:R45.1-R45.16(2007) [PubMed: 17407547] [Abstract]
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: 17050691] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 24-607 IN COMPLEX WITH FAD AND UBIQUINONE, SUBUNIT, IRON-SULFUR BINDING SITES.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		EW134518 mRNA. No translation available.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GMHX-ray2.50A/B34-617[»]
2GMJX-ray2.60A/B34-617[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGP55931.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

GeneTreeENSGT00390000010773.
HOVERGENHBG005615.
OrthoDBEOG42RD6T.

Family and domain databases

InterProIPR017896. 4Fe4S_Fe-S-bd.
IPR007859. ETFD_OxRdtase.
[Graphical view]
PfamPF05187. ETF_QO. 1 hit.
[Graphical view]
PROSITEPS51379. 4FE4S_FER_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameETFD_PIG
AccessionPrimary (citable) accession number: P55931
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 15, 2010
Last modified: October 19, 2011
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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