NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Tokyo 1998;
DOI=10.1038/35024074; PubMed=10993077 [NCBI, ExPASy, EBI, Israel, Japan]
Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS.";
Nature 407:81-86(2000).

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 (Potential).
SUBUNIT: Composed of 13 different subunits (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

BA000003; BAB12873.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_239987.1; -.

3D structure databases

ModBase

P57253.

Enzyme and pathway databases

BioCyc

BSP107806:BU155-MON; -.

Family and domain databases

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.

BLOCKS

P57253.

Genome annotation databases

GeneID

1109599; -.

GenomeReviews

BA000003_GR; BU155.

KEGG

buc:BU155; -.

Phylogenomic databases

HOGENOM

P57253; -.

Genome annotation databases

CMR

P57253; BU155.

Other

ProtoNet

P57253.

UniRef

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

Keywords

4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; NAD; Oxidoreductase; Quinone.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 224`	`224`	`NADH-quinone oxidoreductase subunit B.`	`PRO_0000118769`
`METAL`	`67 67`		`Iron-sulfur (4Fe-4S) (Potential).`
`METAL`	`68 68`		`Iron-sulfur (4Fe-4S) (Potential).`
`METAL`	`133 133`		`Iron-sulfur (4Fe-4S) (Potential).`
`METAL`	`162 162`		`Iron-sulfur (4Fe-4S) (Potential).`

Sequence information

Length: 224 AA [This is the length of the unprocessed precursor]

Molecular weight: 25597 Da [This is the MW of the unprocessed precursor]

CRC64: BB450B102C87CD7B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNYTLTKADS DNNNKKYPKQ TIESVSDPLE EYLKKNIFMG KITQLLHKLV NWGRKNSLWP 

        70         80         90        100        110        120 
YNFGLSCCYV EMVSAFTSVH DVARFGSEVL RASPRQADVM VIAGTPFIKM APVIQRLYDQ 

       130        140        150        160        170        180 
MLEPKWVISM GACANSGGMY DIYSVVQGVD KFLPVDIYIP GCPPRPEAYM QALILLQKLI 

       190        200        210        220 
NEERRPLSWV IGEQGVYHKK MPSERVQKRS KRINIINLST SEKI

P57253 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