NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 50394;
DOI=10.1038/387493a0; PubMed=9168110 [NCBI, ExPASy, EBI, Israel, Japan]
Lang B.F., Burger G., O'Kelly C.J., Cedergren R., Golding G.B., Lemieux C., Sankoff D., Turmel M., Gray M.W.;
"An ancestral mitochondrial DNA resembling a eubacterial genome in miniature.";
Nature 387:493-497(1997).

Comments

FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). This is the largest subunit of complex I and it is a component of the iron-sulfur (IP) fragment of the enzyme. It may form part of the active site crevice where NADH is oxidized (By similarity).
CATALYTIC ACTIVITY: NADH + ubiquinone = NAD⁺ + ubiquinol.
CATALYTIC ACTIVITY: NADH + acceptor = NAD⁺ + reduced acceptor.
COFACTOR: Binds 1 2Fe-2S cluster per subunit (By similarity).
COFACTOR: Binds 2 4Fe-4S clusters per subunit (By similarity).
SUBUNIT: Complex I is composed of about 30 different subunits (By similarity).
SUBCELLULAR LOCATION: Mitochondrion inner membrane (By similarity). Note=Matrix and cytoplasmic side of the mitochondrial inner membrane (By similarity).
SIMILARITY: Belongs to the complex I 75 kDa subunit family.
SIMILARITY: Contains 1 2Fe-2S 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

Sequence databases

EMBL

AF007261; AAD11868.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S78135; S78135.

RefSeq

NP_044753.1; -.

3D structure databases

ModBase

O21241.

Ontologies

GO:0005746;	Cellular component: mitochondrial respiratory chain (inferred from electronic annotation from UniProtKB-KW).
GO:0051537;	Molecular function: 2 iron, 2 sulfur cluster binding (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:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008137;	Molecular function: NADH dehydrogenase (ubiquinone) activity (inferred from electronic annotation from InterPro).
GO:0042773;	Biological process: ATP synthesis coupled electron transport (inferred from electronic annotation from InterPro).
GO:0006810;	Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR006058; 2Fe2S_fd_BS.
IPR001041; Ferredoxin.
IPR006656; Mopterin_OxRdtase.
IPR000283; NADH_DHase_75KDa_su_CS.
IPR010228; NADH_quinone_OxRdtase_G.
IPR015405; NuoG_C.
Graphical view of domain structure.

Pfam

PF09326; DUF1982; 1.
PF00111; Fer2; 1.
PF00384; Molybdopterin; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01973; NuoG; 1.

PROSITE

PS00197; 2FE2S_FER_1; FALSE_NEG.
PS51085; 2FE2S_FER_2; 1.
PS00641; COMPLEX1_75K_1; 1.
PS00642; COMPLEX1_75K_2; 1.
PS00643; COMPLEX1_75K_3; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

801135; -.

Other

ProtoNet

O21241.

UniRef

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

Keywords

2Fe-2S; 4Fe-4S; Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane; NAD; Oxidoreductase; Respiratory chain; Transit peptide; Transport; Ubiquinone.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 691`	`691`	`NADH-ubiquinone oxidoreductase 75 kDa subunit.`	`PRO_0000118537`
`DOMAIN`	`1 78`	`78`	`2Fe-2S ferredoxin-type.`
`METAL`	`34 34`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`45 45`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`48 48`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`62 62`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`94 94`		`Iron-sulfur 2 (4Fe-4S); via pros nitrogen (By similarity).`
`METAL`	`98 98`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`101 101`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`107 107`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`146 146`		`Iron-sulfur 3 (4Fe-4S) (By similarity).`
`METAL`	`149 149`		`Iron-sulfur 3 (4Fe-4S) (By similarity).`
`METAL`	`152 152`		`Iron-sulfur 3 (4Fe-4S) (By similarity).`
`METAL`	`196 196`		`Iron-sulfur 3 (4Fe-4S) (By similarity).`

Sequence information

Length: 691 AA [This is the length of the unprocessed precursor]

Molecular weight: 77718 Da [This is the MW of the unprocessed precursor]

CRC64: 1FB45AF558F469E2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVNVFVDGLS VEVKKGATIL QACAQVGIEI PRFCYHERLS IAGNCRMCLV EVEKSPKPVA 

        70         80         90        100        110        120 
SCAMPVMDNM KIFTNTPLVK KAREGVLEFL LVNHPLDCPI CDQGGECDLQ DLTMVYGSDR 

       130        140        150        160        170        180 
GRFHEYKRGV EDKNIGPLVK TVMTRCIHCT RCVRFATEVA GVPDLGTVGR GRDTEISTYI 

       190        200        210        220        230        240 
QKVFNSELSG NVIDLCPVGA LTSKPYAFTA RSWELQSTES IDVSDAIGSN IRIDVRGSEI 

       250        260        270        280        290        300 
MRILPRLNED VNEEWISDKA RFCYDGLKRQ RLNNPIIKEN GQYKTVTWEK AFNFILKNLQ 

       310        320        330        340        350        360 
EIQNSNRIVG VVGNLMDVES ILLFKELLNK LGSSKIYLES STPILQLNDD EKEDQILNNA 

       370        380        390        400        410        420 
DFRNNYISNT PLAKIEESDL CLLIGTNIRL EAPLLNTRIR KRYLQGNYSV YSVGPTNNLT 

       430        440        450        460        470        480 
YNTENLGNDI STLLEISEGR HPFCKKLMKS KKPLIIIGTH VLQRTDGTSI IELVKTLFKY 

       490        500        510        520        530        540 
TQIKTSNWNG FNILHTSASS VGALDLGIGS TKRYSEKISN SKIEKHFIYL LGADEIRIEN 

       550        560        570        580        590        600 
SKEHFIVYQG HHGDYGANIA DVILPGSAYT EKTATYVNVE GRVQNTKSAF YAPGNAREDW 

       610        620        630        640        650        660 
KIIRALSEVL NKKLPYDSFE DIHTRFMSIA PHLLKVNAIE KNKIVIENSL PFKGLIKNIG 

       670        680        690 
FKPLFNNFYL TNAICRSSQT MAKCSSIYKL N

O21241 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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