NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=VF5;
DOI=10.1038/32831; PubMed=9537320 [NCBI, ExPASy, EBI, Israel, Japan]
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
Nature 392:353-358(1998).

Comments

FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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.
COFACTOR: Binds 1 4Fe-4S cluster (By similarity).
SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits nuoB, C, D, E, F, and G constitute the peripheral sector of the complex (By similarity).
SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side (By similarity).
SIMILARITY: Belongs to the complex I 20 kDa subunit 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

AE000657; AAC07297.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

C70413; C70413.

RefSeq

NP_213898.1; -.

3D structure databases

ModBase

O67334.

Enzyme and pathway databases

BioCyc

AAEO224324:AQ_1312-MON; -.

Ontologies

GO:0051539;	Molecular function: 4 iron, 4 sulfur cluster binding (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: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

HAMAP

MF_01356; -; 1.
PBIL [Tree]

InterPro

IPR006138; NADH_DHase_20kDa_su.
IPR014406; NiFe_hyd_3_ssu/Q_oxred_NuoB.
IPR006137; OxRdtase_q6.
Graphical view of domain structure.

PANTHER

PTHR11995:SF2; NADH_DH_20kDa; 1.
PTHR11995; NiFe_hyd_3_ssu/Q_oxred_NuoB; 1.

Pfam

PF01058; Oxidored_q6; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01957; nuoB_fam; 1.

PROSITE

PS01150; COMPLEX1_20K; 1.

Genome annotation databases

GeneID

1192772; -.

GenomeReviews

AE000657_GR; aq_1312.

KEGG

aae:aq_1312; -.

NMPDR

fig|224324.1.peg.913; -.

Phylogenomic databases

HOGENOM

O67334; -.

Other

LinkHub

O67334; -.

Genome annotation databases

CMR

O67334; aq_1312.

Other

ProtoNet

O67334.

UniRef

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

Keywords

4Fe-4S; Cell inner membrane; Cell membrane; Complete proteome; Iron; Iron-sulfur; Membrane; Metal-binding; NAD; Oxidoreductase; Quinone; Transport; Ubiquinone.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 179`	`179`	`NADH-quinone oxidoreductase subunit B.`	`PRO_0000118764`
`METAL`	`35 35`		`Iron-sulfur (4Fe-4S) (Potential).`
`METAL`	`36 36`		`Iron-sulfur (4Fe-4S) (Potential).`
`METAL`	`100 100`		`Iron-sulfur (4Fe-4S) (Potential).`
`METAL`	`129 129`		`Iron-sulfur (4Fe-4S) (Potential).`

Sequence information

Length: 179 AA [This is the length of the unprocessed precursor]

Molecular weight: 19880 Da [This is the MW of the unprocessed precursor]

CRC64: 239D68B6AF828B77 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVAINSNGFV TTTVEELLRW GRRNSLWPVT IGLACCAIEM MHTAASRFDL DRLGVIFRAS 

        70         80         90        100        110        120 
PRQADVLIVA GTVVNKVAPM LKLIWDQMPD PKWCISMGGC ASAGGPFPTY STLQGVDRII 

       130        140        150        160        170 
PVDVYIPGCP PTPQGLIYGI LQLQRKIKEQ GITKYDKLFA DFNREIEKEG IFVPRELKV

O67334 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