NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=SCRI 193;
PubMed=9643539 [NCBI, ExPASy, EBI, Israel, Japan]
Harris S.J., Shih Y.L., Bentley S.D., Salmond G.P.C.;
"The hexA gene of Erwinia carotovora encodes a LysR homologue and regulates motility and the expression of multiple virulence determinants.";
Mol. Microbiol. 28:705-717(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 (Potential).
SUBUNIT: Composed of 13 different subunits.
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

AF057063; AAC38641.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

O85274.

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

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.

ProtoNet

O85274.

Other

UniRef

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

Keywords

4Fe-4S; 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_0000118772`
`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: 25606 Da [This is the MW of the unprocessed precursor]

CRC64: D02202559740BC81 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDYTLTRIEP DGENDRYPLQ RQEIVSDPLE QHVHRSVYMG KLEHALHDTV NWGRQNSLWP 

        70         80         90        100        110        120 
YNFGLSCCYV EMVTSFTAVH DVARFGAEVL RASPRQADFM VVAGTCFTKM APVIQRLYEQ 

       130        140        150        160        170        180 
MLEPKWVISM GACANSGGMY DIYSVVQGVD KFLPVDVYIP GCPPRPEAYM QALLLLKESI 

       190        200        210        220 
GKERRPLSWV VGEQGVYRAN MQSERERKRG ERIAVTNLRS PDEI

O85274 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