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 (By similarity).
CATALYTIC ACTIVITY: NADH + quinone = NAD⁺ + quinol.
SUBUNIT: NDH-1 is composed of 13 different subunits. Subunits nuoB, CD, E, F, and G constitute the peripheral sector of the complex (By similarity).
SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side (By similarity).
SIMILARITY: In the N-terminal section; belongs to the complex I 30 kDa subunit family.
SIMILARITY: In the C-terminal section; belongs to the complex I 49 kDa subunit family.

Copyright

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Cross-references

Sequence databases

EMBL

AE013218; AAM67717.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_660506.1; -.

3D structure databases

ModBase

Q8K9Y5.

Enzyme and pathway databases

BioCyc

BAPH198804:BUSG149-MON; -.

Ontologies

GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0051287;	Molecular function: NAD binding (inferred from electronic annotation from InterPro).
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

HAMAP

MF_01359; -; 1.
PBIL [Tree]

InterPro

IPR014029; NADH-UbQ_OxRdtase_49kDa_CS.
IPR010219; NADH_DH_1_dsu.
IPR010218; NADH_DH_csu.
IPR001268; NADH_DHase_Ub_30kDa_su.
IPR001135; NADH_UbQ_OxRdtase_49kDa.
Graphical view of domain structure.

Pfam

PF00329; Complex1_30kDa; 1.
PF00346; Complex1_49kDa; 1.
Pfam graphical view of domain structure.

ProDom

PD001581; Complex1_30K; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR01961; NuoC_fam; 1.
TIGR01962; NuoD; 1.

PROSITE

PS00542; COMPLEX1_30K; FALSE_NEG.
PS00535; COMPLEX1_49K; 1.

Genome annotation databases

GeneID

1005966; -.

GenomeReviews

AE013218_GR; BUsg_149.

KEGG

bas:BUsg149; -.

Phylogenomic databases

HOGENOM

Q8K9Y5; -.

Genome annotation databases

CMR

Q8K9Y5; BUsg_149.

Other

ProtoNet

Q8K9Y5.

UniRef

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

Keywords

Cell inner membrane; Cell membrane; Complete proteome; Membrane; Multifunctional enzyme; NAD; Oxidoreductase; Quinone; Transport; Ubiquinone.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 597`	`597`	`NADH-quinone oxidoreductase subunit C/D.`	`PRO_0000118682`
`REGION`	`1 187`	`187`	`NADH dehydrogenase I chain C (By similarity).`
`REGION`	`211 597`	`387`	`NADH dehydrogenase I chain D (By similarity).`

Sequence information

Length: 597 AA [This is the length of the unprocessed precursor]

Molecular weight: 69343 Da [This is the MW of the unprocessed precursor]

CRC64: CC39F0373D2F387A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIDENKKKNT NLNKNEYEEK SILKDLFHFF GKDFCVVQDT CIDFPVIWIN KSLLLKVGKF 

        70         80         90        100        110        120 
LSSSPKPYNM LFDLHGVDER FRLNRLNLPE ADFSIFYHLI SIERNSDILI KVPLLKDDLN 

       130        140        150        160        170        180 
VSTFISLFPN ANWYERETWE MFGIIFDQHP NLTHIIMPNE WKGFPLRKDY PARATEHESF 

       190        200        210        220        230        240 
FLDEQKEDLE MENLRFKPEL WGMKRKNDNV DFMFLNLGPN HPSAHGAFRI VLQLDGENIV 

       250        260        270        280        290        300 
DCVPDIGYHH RGAEKMAERQ SWHSYIPYTD RIEYLGGCVN EMPYVLAVEK LANISVPEKV 

       310        320        330        340        350        360 
EVIRVMLSEL FRINSHLLYI STFIQDVGCM TPVFLAFTDR QKIYDLIEAI TGARMHPAWF 

       370        380        390        400        410        420 
RIGGVAHDLP KGWNVLLKEF LEWMPKRLKY YVQLALENPI LIRRSKGIAQ YNQKEALQWG 

       430        440        450        460        470        480 
VTGSGLRSTG LDLDVRKWRP YSGYQNYTFE IPIGQGISDC YSRVIIKVEE IYQSLSILKQ 

       490        500        510        520        530        540 
CLKNMPEGPF KSDHPLTTPP PKERVLKDID TMITHFLQVS WGPVIPANES FQMIEATKGI 

       550        560        570        580        590 
NSYYLISDGG TMSYRTRIRT PSFPHLQQIP SVIRGSLISD LIVYLGSIDF VMSDVDR

Q8K9Y5 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