NUCLEOTIDE SEQUENCE, AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Fetal liver;
PubMed=8306995 [NCBI, ExPASy, EBI, Israel, Japan]
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).

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.
COFACTOR: FAD.
SUBUNIT: Monomer (By similarity).
SUBCELLULAR LOCATION: Mitochondrion inner membrane (By similarity).
SIMILARITY: Contains 1 4Fe-4S ferredoxin-type domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

3D structure databases

PDB

2GMH; X-ray; 2.50 A; A/B=24-607.	[ExPASy / RCSB / EBI]
2GMJ; X-ray; 2.60 A; A/B=24-607.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

2GMH; -.
2GMJ; -.

ModBase

P55931.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005743;	Cellular component: mitochondrial inner membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0051539;	Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004174;	Molecular function: electron-transferring-flavoprotein dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0022900;	Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0006810;	Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR007859; ETFD_OxRdtase.
IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR000103; Pyridine_nuc-diS_OxRdtase_2.
Graphical view of domain structure.

Pfam

PF05187; ETF_QO; 1.
PF07992; Pyr_redox_2; 1.
Pfam graphical view of domain structure.

PRINTS

PR00469; PNDRDTASEII.

PROSITE

PS51379; 4FE4S_FER_2; 1.
PROSITE graphical view of domain structure (profiles).

Phylogenomic databases

HOVERGEN

P55931; -.

Other

ProtoNet

P55931.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; 4Fe-4S; Acetylation; Direct protein sequencing; Electron transport; FAD; Flavoprotein; Iron; Iron-sulfur; Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase; Transit peptide; Transmembrane; Transport; Ubiquinone.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`<1 23`	`>23`	`Mitochondrion (Potential).`
`CHAIN`	`24 607`	`584`	`Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial.`	`PRO_0000008663`
`TRANSMEM`	`448 468`	`21`	`Potential.`
`DOMAIN`	`567 596`	`30`	`4Fe-4S ferredoxin-type.`
`NP_BIND`	`61 75`	`15`	`FAD (Potential).`
`METAL`	`551 551`		`Iron-sulfur (4Fe-4S) (Potential).`
`METAL`	`576 576`		`Iron-sulfur (4Fe-4S) (Potential).`
`METAL`	`579 579`		`Iron-sulfur (4Fe-4S) (Potential).`
`METAL`	`582 582`		`Iron-sulfur (4Fe-4S) (Potential).`
`MOD_RES`	`86 86`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`143 143`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`213 213`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`334 334`		`N6-acetyllysine (By similarity).`
`NON_TER`	`1 1`
`TURN`	`36 38`	`3`
`HELIX`	`45 47`	`3`
`STRAND`	`56 58`	`3`
`STRAND`	`60 64`	`5`
`HELIX`	`68 83`	`16`
`STRAND`	`90 93`	`4`
`STRAND`	`95 98`	`4`
`TURN`	`99 102`	`4`
`HELIX`	`112 117`	`6`
`HELIX`	`121 124`	`4`
`STRAND`	`134 140`	`7`
`STRAND`	`145 147`	`3`
`HELIX`	`166 179`	`14`
`STRAND`	`183 185`	`3`
`STRAND`	`190 195`	`6`
`STRAND`	`199 206`	`8`
`STRAND`	`209 211`	`3`
`STRAND`	`217 222`	`6`
`STRAND`	`226 228`	`3`
`STRAND`	`230 234`	`5`
`HELIX`	`241 249`	`9`
`TURN`	`250 255`	`6`
`STRAND`	`261 270`	`10`
`HELIX`	`273 275`	`3`
`STRAND`	`280 286`	`7`
`STRAND`	`295 301`	`7`
`STRAND`	`304 306`	`3`
`STRAND`	`308 316`	`9`
`HELIX`	`326 333`	`8`
`TURN`	`337 339`	`3`
`HELIX`	`340 343`	`4`
`STRAND`	`347 357`	`11`
`HELIX`	`360 363`	`4`
`STRAND`	`372 374`	`3`
`TURN`	`376 379`	`4`
`TURN`	`384 387`	`4`
`HELIX`	`390 408`	`19`
`STRAND`	`416 419`	`4`
`HELIX`	`424 430`	`7`
`HELIX`	`433 440`	`8`
`TURN`	`441 445`	`5`
`HELIX`	`446 449`	`4`
`TURN`	`451 453`	`3`
`HELIX`	`454 464`	`11`
`TURN`	`465 470`	`6`
`HELIX`	`482 484`	`3`
`HELIX`	`489 491`	`3`
`STRAND`	`502 505`	`4`
`HELIX`	`508 513`	`6`
`TURN`	`514 516`	`3`
`STRAND`	`521 523`	`3`
`STRAND`	`526 531`	`6`
`HELIX`	`534 537`	`4`
`HELIX`	`539 543`	`5`
`HELIX`	`547 550`	`4`
`STRAND`	`556 560`	`5`
`STRAND`	`562 565`	`4`
`STRAND`	`567 571`	`5`
`HELIX`	`573 575`	`3`
`HELIX`	`581 585`	`5`
`STRAND`	`591 593`	`3`

Sequence information

Length: 607 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 67590 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 243573B0774C6FDE [This is a checksum on the sequence]

        10         20         30         40         50         60 
PAYQCFHALK IKKNYLPLCA TRWSSTCKVP RITTHYTIYP RDQDKRWEGV NMERFAEEAD 

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

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

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

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

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

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

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

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

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


GPAYNGM

P55931 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools