NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=PRQ 62B;
DOI=10.1016/j.bbabio.2005.06.003; PubMed=16023073 [NCBI, ExPASy, EBI, Israel, Japan]
Melo A.M.P., Lobo S.A.L., Sousa F.L., Fernandes A.S., Pereira M.M., Hreggvidsson G.O., Kristjansson J.K., Saraiva L.M., Teixeira M.;
"A nhaD Na+/H+ antiporter and a pcd homologues are among the Rhodothermus marinus complex I genes.";
Biochim. Biophys. Acta 1709:95-103(2005).

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 menaquinone. 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 2 4Fe-4S clusters per subunit (By similarity).
SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits NQO7-14 constitute the membrane sector of the complex (By similarity).
SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein (Potential).
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

AY972099; AAY42993.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q4QSC5.

Ontologies

GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from HAMAP).
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.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 230`	`230`	`NADH-quinone oxidoreductase subunit 9.`	`PRO_0000245739`
`DOMAIN`	`60 93`	`34`	`4Fe-4S ferredoxin-type 1.`
`DOMAIN`	`104 133`	`30`	`4Fe-4S ferredoxin-type 2.`
`METAL`	`73 73`		`Iron-sulfur 1 (4Fe-4S) (By similarity).`
`METAL`	`76 76`		`Iron-sulfur 1 (4Fe-4S) (By similarity).`
`METAL`	`79 79`		`Iron-sulfur 1 (4Fe-4S) (By similarity).`
`METAL`	`83 83`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`113 113`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`116 116`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`119 119`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`123 123`		`Iron-sulfur 1 (4Fe-4S) (By similarity).`

Sequence information

Length: 230 AA [This is the length of the unprocessed precursor]

Molecular weight: 27120 Da [This is the MW of the unprocessed precursor]

CRC64: E951770E49179E57 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPGKPVNLAS PNERKLNFWE RLYLPAVVQG LAYTWRKMRS PRYTFQYPDE LWYPPDSYRG 

        70         80         90        100        110        120 
RPVLVEENGR PRCVACGLCA RACPPLAISM QAKEVDDVKE REPAWFEINM LRCIYCGYCE 

       130        140        150        160        170        180 
EVCPEEAIVM SKEYDLTFQS RDEAIFGLEK LLVPAERLKD RLEWLDRYKD PQYGQHWEFR 

       190        200        210        220        230 
KENNLHSLKD RPFLKWLLEE EGMEELKSTH LRPEEPVAAE RSWGGVRAEG

Q4QSC5 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