NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 13543 / NRRL B-3784;
DOI=10.1021/bi00054a030; PubMed=8422400 [NCBI, ExPASy, EBI, Israel, Japan]
Xu X., Matsuno-Yagi A., Yagi T.;
"DNA sequencing of the seven remaining structural genes of the gene cluster encoding the energy-transducing NADH-quinone oxidoreductase of Paracoccus denitrificans.";
Biochemistry 32:968-981(1993).

Comments

FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
CATALYTIC ACTIVITY: NADH + quinone = NAD⁺ + quinol.
SUBUNIT: NDH-1 is composed of at least 14 different subunits, nqo1 to nqo14. The complex has a L-shaped structure, with the hydrophobic arm (subunits nqo7, nqo8, nqo10 to nqo14) embedded in the inner membrane and the hydrophilic peripheral arm (subunits nqo1 to nqo6, nqo9) protruding into the bacterial cytoplasm. The hydrophilic domain contains all the redox centers.
SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
SIMILARITY: Belongs to the complex I subunit 4 family.

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

L02354; AAA25599.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

I45456; I45456.

3D structure databases

ModBase

P29925.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0008137;	Molecular function: NADH dehydrogenase (ubiquinone) activity (inferred from electronic annotation from InterPro).
GO:0048038;	Molecular function: quinone binding (inferred from electronic annotation from UniProtKB-KW).
GO:0042773;	Biological process: ATP synthesis coupled electron transport (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR010227; NADH_quinone_OxRdtase_I_M.
IPR003918; NADHub_OxRdtase_4.
IPR001750; Oxidored_q1.
Graphical view of domain structure.

Pfam

PF00361; Oxidored_q1; 1.
Pfam graphical view of domain structure.

PRINTS

PR01437; NUOXDRDTASE4.

TIGRFAMs

TIGR01972; NDH_I_M; 1.

Other

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

Keywords

Cell inner membrane; Cell membrane; Membrane; NAD; Oxidoreductase; Quinone; Transmembrane; Ubiquinone.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 513`	`513`	`NADH-quinone oxidoreductase chain 13.`	`PRO_0000118037`
`TRANSMEM`	`3 23`	`21`	`Potential.`
`TRANSMEM`	`34 54`	`21`	`Potential.`
`TRANSMEM`	`81 101`	`21`	`Potential.`
`TRANSMEM`	`112 132`	`21`	`Potential.`
`TRANSMEM`	`133 153`	`21`	`Potential.`
`TRANSMEM`	`164 184`	`21`	`Potential.`
`TRANSMEM`	`211 231`	`21`	`Potential.`
`TRANSMEM`	`250 270`	`21`	`Potential.`
`TRANSMEM`	`277 297`	`21`	`Potential.`
`TRANSMEM`	`312 332`	`21`	`Potential.`
`TRANSMEM`	`340 360`	`21`	`Potential.`
`TRANSMEM`	`383 403`	`21`	`Potential.`
`TRANSMEM`	`418 438`	`21`	`Potential.`
`TRANSMEM`	`463 483`	`21`	`Potential.`

Sequence information

Length: 513 AA [This is the length of the unprocessed precursor]

Molecular weight: 56417 Da [This is the MW of the unprocessed precursor]

CRC64: 8164DEACA20FE739 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTNLLSIITF LPIVAAIIMA LFLRGQDEAA ARNAKWLALL TTTATFVISL FVLFRFDPAN 

        70         80         90        100        110        120 
TGFQFVEDHA WIMGVCYKMG VDGISVLFVL LTTFMMPLTI LSTWQVQDKV KEYMIAFLVL 

       130        140        150        160        170        180 
EGLMIGVFTA LDLVLFYLFF EAGLIPMFLI IGIWGGKDRI YASFKFFLYT FLGSVLMLVA 

       190        200        210        220        230        240 
MIAMYRMAGT TDIPTLLTFD FPSENFRLLG MTVVGGMQML LFLAFFASFA VKMPMWPVHT 

       250        260        270        280        290        300 
WLPDAHVQAP TAGSVLLAAV LLKMGGYGFL RFSLPMFPVA SGVAQPYVFW LSAIAIVYTS 

       310        320        330        340        350        360 
LVALAQSDMK KVIAYSSVAH MGYVTMGVFA ANQIGVDGAI FQMLSHGFIS GALFLCVGVI 

       370        380        390        400        410        420 
YDRMHTREID AYGGLVNRMP AYAAVFMFFT MANVGLPGTS GFVGEFLTLM GVFRVDTWVA 

       430        440        450        460        470        480 
LVATSGVILS AAYALWLYRR VTLGQLIKES LKSITDMTPR ERWVFIPLIA MTLILGVYPR 

       490        500        510 
LVTDVTGPAV AALVQDYNQS QPAAPVATAQ ASH

P29925 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