NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=PRQ-62B;
DOI=10.1016/j.bbabio.2005.06.003; PubMed=16023073 [NCBI, ExPASy, EBI, Israel, Japan]
Melo A.M.P., Lobo S.A.L., Sousa F.L., Fernandes A.S., Pereira M.M., Hreggvidsson G.O., Kristjansson J.K., Saraiva L.M., Teixeira M.;
"A nhaD Na+/H+ antiporter and a pcd homologues are among the Rhodothermus marinus complex I genes.";
Biochim. Biophys. Acta 1709:95-103(2005).

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 menaquinone. 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 (By similarity).
CATALYTIC ACTIVITY: NADH + quinone = NAD⁺ + quinol.
SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits NQO7-14 constitute the membrane sector of the complex (By similarity).
SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein (Potential).
SIMILARITY: Belongs to the complex I subunit 1 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

AY972098; AAY42992.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q4QSC6.

Ontologies

GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01350; -; 1.
PBIL [Tree]

InterPro

IPR001694; Resp_NADH_DHase_1.
Graphical view of domain structure.

PANTHER

PTHR11432; Resp_NADH_DH_1; 1.

Pfam

PF00146; NADHdh; 1.
Pfam graphical view of domain structure.

PROSITE

PS00667; COMPLEX1_ND1_1; FALSE_NEG.
PS00668; COMPLEX1_ND1_2; 1.

Other

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 341`	`341`	`NADH-quinone oxidoreductase subunit 8.`	`PRO_0000240051`
`TRANSMEM`	`9 29`	`21`	`Potential.`
`TRANSMEM`	`75 95`	`21`	`Potential.`
`TRANSMEM`	`108 128`	`21`	`Potential.`
`TRANSMEM`	`154 174`	`21`	`Potential.`
`TRANSMEM`	`180 200`	`21`	`Potential.`
`TRANSMEM`	`244 264`	`21`	`Potential.`
`TRANSMEM`	`278 298`	`21`	`Potential.`
`TRANSMEM`	`321 341`	`21`	`Potential.`

Sequence information

Length: 341 AA [This is the length of the unprocessed precursor]

Molecular weight: 37374 Da [This is the MW of the unprocessed precursor]

CRC64: 546A00803E4605A9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDLPLYWTAL IAFLIINAML LTASVLVYAE RKISGFIQHR LGPNRVGPAG FLQPFADVVK 

        70         80         90        100        110        120 
LLFKEDIIPA QANRFIHALA PTIMVTIAMT VPALIPFARG VVIADIDVGV LAILALTSIS 

       130        140        150        160        170        180 
VYGITLAGWS SNSKYSLLGG LRSSAQMISY ELAMGTAVLS VILQAGSLNV SAIVEAQRDG 

       190        200        210        220        230        240 
WAILGWHVFT NPIGALIFIV TAFAETNRLP FDLPEAEQEL VGGYHTEYSG MKFGMFFLAE 

       250        260        270        280        290        300 
YVNLFVASFV IATLFFGGYL VPFEPLLLKA FPALEGSVLL GLLQFLSLLA KTCFFAFLYI 

       310        320        330        340 
WVRWTFPRFK YNQLMTLGWK YLLPIGLANV ILIALGVALF S

Q4QSC6 in FASTA format

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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