NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10.
STRAIN=ATCC 13543 / NRRL B-3784;
DOI=10.1021/bi00099a027; PubMed=1909571 [NCBI, ExPASy, EBI, Israel, Japan]
Xu X., Matsuno-Yagi A., Yagi T.;
"Characterization of the 25-kilodalton subunit of the energy-transducing NADH-ubiquinone oxidoreductase of Paracoccus denitrificans: sequence similarity to the 24-kilodalton subunit of the flavoprotein fraction of mammalian complex I.";
Biochemistry 30:8678-8684(1991).

[2]

MUTAGENESIS OF CYS-61; HIS-92; CYS-96; CYS-101; CYS-104; CYS-113; CYS-137 AND CYS-141.
DOI=10.1016/0014-5793(94)01107-9; PubMed=7957917 [NCBI, ExPASy, EBI, Israel, Japan]
Yano T., Sled V.D., Ohnishi T., Yagi T.;
"Identification of amino acid residues associated with the [2Fe-2S] cluster of the 25 kDa (NQO2) subunit of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans.";
FEBS Lett. 354:160-164(1994).

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.
CATALYTIC ACTIVITY: NADH + quinone = NAD⁺ + quinol.
COFACTOR: Binds 1 2Fe-2S cluster (Potential).
SUBUNIT: NDH-1 is composed of at least 14 different subunits, nqo1 to nqo14. The complex has a L-shaped structure, with the hydrophobic arm (subunits nqo7, nqo8, nqo10 to nqo14) embedded in the inner membrane and the hydrophilic peripheral arm (subunits nqo1 to nqo6, nqo9) protruding into the bacterial cytoplasm. The hydrophilic domain contains all the redox centers.
SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein.
SIMILARITY: Belongs to the complex I 24 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

M74171; AAA25588.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A40296; A40296.

3D structure databases

ModBase

P29914.

Ontologies

GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0051537;	Molecular function: 2 iron, 2 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051287;	Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0050136;	Molecular function: NADH dehydrogenase (quinone) activity (inferred from electronic annotation from EC).
GO:0048038;	Molecular function: quinone binding (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR002023; NADH_DHase_Ub_24kDa_su.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.30.10; Thioredoxin_fold; 1.

PANTHER

PTHR10371; Cmplx1_24kDa; 1.

Pfam

PF01257; Complex1_24kDa; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000216; NADH_DH_24kDa; 1.

ProDom

PD003859; Cmplx1_24kDa; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR01958; nuoE_fam; 1.

PROSITE

PS01099; COMPLEX1_24K; 1.

ProtoNet

P29914.

Other

UniRef

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

Keywords

2Fe-2S; Cell inner membrane; Cell membrane; Direct protein sequencing; Iron; Iron-sulfur; Membrane; Metal-binding; NAD; Oxidoreductase; Quinone; Ubiquinone.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 239`	`239`	`NADH-quinone oxidoreductase chain 2.`	`PRO_0000118685`
`METAL`	`96 96`		`Iron-sulfur (2Fe-2S).`
`METAL`	`101 101`		`Iron-sulfur (2Fe-2S).`
`METAL`	`137 137`		`Iron-sulfur (2Fe-2S).`
`METAL`	`141 141`		`Iron-sulfur (2Fe-2S).`
`MUTAGEN`	`61 61`		`C->S: No change in UV-visible and EPR spectra.`
`MUTAGEN`	`92 92`		`H->A: No change in UV-visible and EPR spectra.`
`MUTAGEN`	`96 96`		`C->A,S: Alters UV-visible and EPR spectra.`
`MUTAGEN`	`101 101`		`C->A,S: Alters UV-visible and EPR spectra.`
`MUTAGEN`	`104 104`		`C->S: No change in UV-visible and EPR spectra.`
`MUTAGEN`	`113 113`		`C->S: No change in UV-visible and EPR spectra.`
`MUTAGEN`	`137 137`		`C->A,S: Alters UV-visible and EPR spectra.`
`MUTAGEN`	`141 141`		`C->A,S: Alters UV-visible and EPR spectra.`

Sequence information

Length: 239 AA [This is the length of the unprocessed precursor]

Molecular weight: 26122 Da [This is the MW of the unprocessed precursor]

CRC64: 6BF734257D670F41 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLRRLSPIQP DSFEFTPANL EWARAQMTKY PEGRQQSAII PVLWRAQEQE GWLSRPAIEY 

        70         80         90        100        110        120 
CADLLGMPYI RALEVATFYF MFQLQPVGSV AHIQICGTTT CMICGAEDLI RVCKEKIAPE 

       130        140        150        160        170        180 
PHALSADGRF SWEEVECLGA CTNAPMAQIG KDFYEDLTVE KLAALIDRFA AGEVPVPGPQ 

       190        200        210        220        230 
NGRFSAEALG GPTALADLKG GEAHNASVAR ALRLGDSIKR IDGTEVPITT PWLATQNGV

P29914 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