[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-16. STRAIN=ATCC 13543 / NRRL B-3784; DOI=10.1016/0003-9861(92)90542-5; PubMed=1605643 [NCBI, ExPASy, EBI, Israel, Japan] Xu X., Matsuno-Yagi A., Yagi T.; "Structural features of the 66-kDa subunit of the energy-transducing NADH-ubiquinone oxidoreductase (NDH-1) of Paracoccus denitrificans."; Arch. Biochem. Biophys. 296:40-48(1992).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 658-673. DOI=10.1021/bi00054a030; PubMed=8422400 [NCBI, ExPASy, EBI, Israel, Japan] Xu X., Matsuno-Yagi A., Yagi T.; "DNA sequencing of the seven remaining structural genes of the gene cluster encoding the energy-transducing NADH-quinone oxidoreductase of Paracoccus denitrificans."; Biochemistry 32:968-981(1993).
[3]	IDENTIFICATION OF A [2FE--2S] AND A [4FE--4S] CLUSTER. DOI=10.1074/jbc.270.31.18264; PubMed=7629145 [NCBI, ExPASy, EBI, Israel, Japan] Yano T., Yagi T., Sled' V.D., Ohnishi T.; "Expression and characterization of the 66-kilodalton (NQO3) iron-sulfur subunit of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans."; J. Biol. Chem. 270:18264-18270(1995).
[4]	IDENTIFICATION OF A SECOND [4FE--4S] CLUSTER, AND MUTAGENESIS OF HIS-106. DOI=10.1074/jbc.M212275200; PubMed=12600982 [NCBI, ExPASy, EBI, Israel, Japan] Yano T., Sklar J., Nakamaru-Ogiso E., Takahashi Y., Yagi T., Ohnishi T.; "Characterization of cluster N5 as a fast-relaxing [4Fe-4S] cluster in the Nqo3 subunit of the proton-translocating NADH-ubiquinone oxidoreductase from Paracoccus denitrificans."; J. Biol. Chem. 278:15514-15522(2003).

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 per subunit. The 2Fe-2S cluster is known as N1b.
COFACTOR: Binds 2 4Fe-4S clusters per subunit. The 4Fe-4S cluster 1 is known as N5 and 4Fe-4S cluster 2 as N4.
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 75 kDa subunit family.
SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain.

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

M84572; AAA25587.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S23948; A45456.

3D structure databases

ModBase

P29915.

Family and domain databases

InterPro

IPR006058; 2Fe2S_fd_BS.
IPR001041; Ferredoxin.
IPR006656; Mopterin_OxRdtase.
IPR000283; NADH_DHase_75KDa_su_CS.
IPR010228; NADH_quinone_OxRdtase_G.
IPR015405; NuoG_C.
Graphical view of domain structure.

Pfam

PF09326; DUF1982; 1.
PF00111; Fer2; 1.
PF00384; Molybdopterin; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01973; NuoG; 1.

PROSITE

PS00197; 2FE2S_FER_1; FALSE_NEG.
PS51085; 2FE2S_FER_2; 1.
PS00641; COMPLEX1_75K_1; 1.
PS00642; COMPLEX1_75K_2; 1.
PS00643; COMPLEX1_75K_3; 1.
PROSITE graphical view of domain structure (profiles).

Other

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

Keywords

2Fe-2S; 4Fe-4S; Cell inner membrane; Cell membrane; Direct protein sequencing; Iron; Iron-sulfur; Membrane; Metal-binding; NAD; Oxidoreductase; Quinone; Ubiquinone.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 673`	`672`	`NADH-quinone oxidoreductase chain 3.`	`PRO_0000118540`
`DOMAIN`	`5 90`	`86`	`2Fe-2S ferredoxin-type.`
`METAL`	`37 37`		`Iron-sulfur 1 (2Fe-2S) (Potential).`
`METAL`	`48 48`		`Iron-sulfur 1 (2Fe-2S) (Potential).`
`METAL`	`51 51`		`Iron-sulfur 1 (2Fe-2S) (Potential).`
`METAL`	`66 66`		`Iron-sulfur 1 (2Fe-2S) (Potential).`
`METAL`	`106 106`		`Iron-sulfur 2 (4Fe-4S); via pros nitrogen (Probable).`
`METAL`	`110 110`		`Iron-sulfur 2 (4Fe-4S) (Potential).`
`METAL`	`113 113`		`Iron-sulfur 2 (4Fe-4S) (Potential).`
`METAL`	`119 119`		`Iron-sulfur 2 (4Fe-4S) (Potential).`
`METAL`	`158 158`		`Iron-sulfur 3 (4Fe-4S) (Potential).`
`METAL`	`161 161`		`Iron-sulfur 3 (4Fe-4S) (Potential).`
`METAL`	`164 164`		`Iron-sulfur 3 (4Fe-4S) (Potential).`
`METAL`	`208 208`		`Iron-sulfur 3 (4Fe-4S) (Potential).`
`MUTAGEN`	`106 106`		`H->A: Very little incorporation of iron-sulfur centers into protein in E.coli.`
`MUTAGEN`	`106 106`		`H->C: Alters the EPR signal of the N5 cluster; all 3 iron-sulfur clusters are less stable in E.coli.`

Sequence information

Length: 673 AA [This is the length of the unprocessed precursor]

Molecular weight: 73159 Da [This is the MW of the unprocessed precursor]

CRC64: 5778B4A77940CF1D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MADLRKIKID DTIIEVDPNM TLIQACEMAG IEVPRFCYHE RLSIAGNCRM CLVEVVGGPP 

        70         80         90        100        110        120 
KPAASCAMQV KDLRPGPEGA PSEIRTNSPM VKKAREGVME FLLINHPLDC PICDQGGECD 

       130        140        150        160        170        180 
LQDQAMAYGV DFSRYREPKR ATEDLNLGPL VETHMTRCIS CTRCVRFTTE VAGITQMGQT 

       190        200        210        220        230        240 
GRGEDSEITS YLNQTLESNM QGNIIDLCPV GALVSKPYAF TARPWELTKT ESIDVMDALG 

       250        260        270        280        290        300 
SSIRIDTKGR EVMRILPRNH DGVNEEWISD KTRFVWDGLR RQRLDRPYIR ENGRLRPASW 

       310        320        330        340        350        360 
PEALEAAARA MKGKKIAGLI GDLVPAEAAF SLKQLVEGLG GKVECRVDGA RLPAGNRSAY 

       370        380        390        400        410        420 
VGTARIEDID DAEMIQLIGT NPRDEAPVLN ARIRKAWSKG AKVGLVGEPV DLTYDYAHVG 

       430        440        450        460        470        480 
TDRAALESLS SREISDETKA RPSIVIVGQG AIARRDGEAV LAHAMKLAEN SNSGLLILHT 

       490        500        510        520        530        540 
AAGRVGAMDV GAVTEGGLLA AIDGAEVVYN LGADEVDIDQ GPFVIYQGSH GDRGAHRDII 

       550        560        570        580        590        600 
LPGACYTEES GLFVNTEGRP QLAMRANFAP GEGKENWAIL RALSAELGAT QPWDSLAGLR 

       610        620        630        640        650        660 
RKLVEAVPHL AQIDQVPQNE WQPLGRFDLG QASFRYAIRD FYLTNPIARS SPLMGELSAM 

       670 
AAARKAPAPL AAE

P29915 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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