NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 13543 / NRRL B-3784;
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).

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 2 4Fe-4S clusters per subunit (By similarity).
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 23 kDa subunit family.
SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains.

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

L02354; AAA25593.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

D45456; D45456.

3D structure databases

HSSP

P00198; 2FDN. [HSSP ENTRY / PDB]

ModBase

P29921.

Ontologies

GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from HAMAP).
GO:0050136;	Molecular function: NADH dehydrogenase (quinone) activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from HAMAP).
GO:0019684;	Biological process: photosynthesis, light reaction (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01351; -; 1.
PBIL [Tree]

InterPro

IPR001450; 4Fe4S_Fe_S_bd.
IPR010226; NADH_quinone_OxRdtase_I.
Graphical view of domain structure.

Pfam

PF00037; Fer4; 2.
Pfam graphical view of domain structure.

PRINTS

PR00353; 4FE4SFRDOXIN.

TIGRFAMs

TIGR01971; NuoI; 1.

PROSITE

PS00198; 4FE4S_FER_1; 2.
PS51379; 4FE4S_FER_2; 2.
PROSITE graphical view of domain structure (profiles).

Other

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 163`	`163`	`NADH-quinone oxidoreductase subunit 9.`	`PRO_0000118720`
`DOMAIN`	`54 84`	`31`	`4Fe-4S ferredoxin-type 1.`
`DOMAIN`	`94 123`	`30`	`4Fe-4S ferredoxin-type 2.`
`METAL`	`64 64`		`Iron-sulfur 1 (4Fe-4S) (By similarity).`
`METAL`	`67 67`		`Iron-sulfur 1 (4Fe-4S) (By similarity).`
`METAL`	`70 70`		`Iron-sulfur 1 (4Fe-4S) (By similarity).`
`METAL`	`74 74`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`103 103`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`106 106`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`109 109`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`113 113`		`Iron-sulfur 1 (4Fe-4S) (By similarity).`

Sequence information

Length: 163 AA [This is the length of the unprocessed precursor]

Molecular weight: 18960 Da [This is the MW of the unprocessed precursor]

CRC64: 71163CEA824B2475 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAFDFARATK YFLMWDFIKG FGLGMRYFVS PKPTLNYPHE KGPLSPRFRG EHALRRYPNG 

        70         80         90        100        110        120 
EERCIACKLC EAVCPAQAIT IDAERREDGS RRTTRYDIDM TKCIYCGFCQ EACPVDAIVE 

       130        140        150        160 
GPNFEYATET REELFYDKQK LLANGERWEA EIARNLQLDA PYR

P29921 in FASTA format

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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