[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=RCR2011 / SU47; Schmidt R., Uhde C., Nagel A., Puehler A., Selbitschka W.; "Sinorhizobium meliloti mutant strain SP10 which is impaired in stationary phase survival shows a reduction in the energy charge due to its defect in the energy-conserving NADH dehydrogenase."; Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=41; Putnoky P., Jady B., Chellapilla K.P., Barta F., Kiss E.; "Rhizobium meliloti carries two sets of nuo genes."; Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=1021; DOI=10.1073/pnas.161294398; PubMed=11481430 [NCBI, ExPASy, EBI, Israel, Japan] Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F.; "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021."; Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).

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 (By similarity).
CATALYTIC ACTIVITY: NADH + quinone = NAD⁺ + quinol.
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
SIMILARITY: Belongs to the complex I subunit 3 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

AF055637; AAC12754.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ245398; CAB51620.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL591688; CAC45843.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_385370.1; -.

3D structure databases

ModBase

O68852.

Enzyme and pathway databases

BioCyc

SMEL266834:SMC01912-MON; -.

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:0006120;	Biological process: mitochondrial electron transport, NADH to ubiquinone (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR000440; Oxidored_q4.
Graphical view of domain structure.

PANTHER

PTHR11058; Oxidored_q4; 1.

Pfam

PF00507; Oxidored_q4; 1.
Pfam graphical view of domain structure.

Genome annotation databases

1232912; -.

AL591688_GR; R01264.

sme:SMc01912; -.

fig|266834.1.peg.2558; -.

Phylogenomic databases

HOGENOM

O68852; -.

Genome annotation databases

CMR

O68852; R01264.

Other

ProtoNet

O68852.

UniRef

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

Keywords

Cell membrane; Complete proteome; Membrane; NAD; Oxidoreductase; Quinone; Transmembrane; Ubiquinone.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 121`	`121`	`NADH-quinone oxidoreductase subunit A 1.`	`PRO_0000117872`
`TRANSMEM`	`11 31`	`21`	`Potential.`
`TRANSMEM`	`65 85`	`21`	`Potential.`
`TRANSMEM`	`90 110`	`21`	`Potential.`

Sequence information

Length: 121 AA [This is the length of the unprocessed precursor]

Molecular weight: 13804 Da [This is the MW of the unprocessed precursor]

CRC64: D3E255E405310163 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTELLGSYVP IAIFIGIALV IGLALLVAPF AVAFKAPDSE KLSAYECGFN AFDDARMKFD 

        70         80         90        100        110        120 
VRFYLVSILF IIFDLEVAFL FPWAVSFKEM GWFGFWSMMV FLLVLTVGFI YEWKKGALEW 


N

O68852 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