[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=1917890 [NCBI, ExPASy, EBI, Israel, Japan] Xu X., Koyama N., Cui M., Yamagishi A., Nosoh Y., Oshima T.; "Nucleotide sequence of the gene encoding NADH dehydrogenase from an alkalophile, Bacillus sp. strain YN-1."; J. Biochem. 109:678-683(1991).
[2]	PARTIAL PROTEIN SEQUENCE. PubMed=2760020 [NCBI, ExPASy, EBI, Israel, Japan] Xu X., Kanaya S., Koyama N., Sekiguchi T., Nosoh Y., Ohashi S., Tsuda K.; "Tryptic digestion of NADH dehydrogenase from alkalophilic Bacillus."; J. Biochem. 105:626-632(1989).

Comments

FUNCTION: Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
CATALYTIC ACTIVITY: NADH + acceptor = NAD⁺ + reduced acceptor.
COFACTOR: Binds 1 FAD per subunit (By similarity).
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase 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

D10701; BAA01545.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P35340; 1FL2. [HSSP ENTRY / PDB]

ModBase

P26829.

Ontologies

GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660;	Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0051287;	Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0003954;	Molecular function: NADH dehydrogenase activity (inferred from electronic annotation from EC).
GO:0015035;	Molecular function: protein disulfide oxidoreductase activity (inferred from electronic annotation from InterPro).
GO:0045454;	Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0022900;	Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0006810;	Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000759; Adrndx_reductase.
IPR012081; Alkyl_hydroperoxide_Rdtase_suF.
IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
IPR001327; Pyr_OxRdtase_NAD_bd.
IPR000103; Pyridine_nuc-diS_OxRdtase_2.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.30.10; Thioredoxin_fold; 2.

Pfam

PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000238; AhpF; 1.

PRINTS

PR00419; ADXRDTASE.
PR00368; FADPNR.
PR00469; PNDRDTASEII.

ProDom

PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR03140; AhpF; 1.

PROSITE

PS51354; GLUTAREDOXIN_2; 1.
PS00573; PYRIDINE_REDOX_2; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P26829.

Other

UniRef

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

Keywords

Cell membrane; Direct protein sequencing; Electron transport; FAD; Flavoprotein; Membrane; NAD; Oxidoreductase; Redox-active center; Transport; Ubiquinone.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 519`	`519`	`NADH dehydrogenase.`	`PRO_0000166788`
`NP_BIND`	`210 241`	`32`	`FAD (By similarity).`
`NP_BIND`	`349 379`	`31`	`NAD (By similarity).`
`NP_BIND`	`469 479`	`11`	`FAD (By similarity).`
`REGION`	`1 ?183`		`Membrane-binding.`
`REGION`	`?184 519`		`Catalytic.`
`DISULFID`	`337 340`		`Redox-active (By similarity).`

Sequence information

Length: 519 AA [This is the length of the unprocessed precursor]

Molecular weight: 55830 Da [This is the MW of the unprocessed precursor]

CRC64: 054FA461B5A156C2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVLEPQIKSQ LNQYLQLMEG DVLLKVSAGN DKVSEDMLSL VDELASMSSR ITVEKTNLER 

        70         80         90        100        110        120 
TPSFSVNRPG EDTGIVFAGI PLGHEFTSLV LALLQVSGRA PKAEQNVIDQ IKNIEGEYHF 

       130        140        150        160        170        180 
ESYISLSCQN CPDVVQALNL MSVLNPGISH TMIDGAAFKD EVESKDIMAV PTVYLNGESF 

       190        200        210        220        230        240 
TSGRMTVEEI LAQLGSGPDA SELADKDPFD VLVVGGGPAG ASSAIYAARK GIRTGIVADR 

       250        260        270        280        290        300 
FGGQIMDTLS IENFISQKYT EGPKLAASLE EHVKEYDIDV MKLQRAKRLE KKDLIEIELE 

       310        320        330        340        350        360 
NGAVLKSKSV ILSTGARWRN VGVPGEQEFK NKGVAYCPHC DGPLFEGKDV AVIGGGNSGV 

       370        380        390        400        410        420 
EAAIDLAGIV NHVTVLEFMP ELKADEVLQE RLNSLPNVTV IKNAQTKEIT GDDKVNGISY 

       430        440        450        460        470        480 
MDRDTEEVHH IELAGVFVQI GLVPNTDWLD GTLERNRFGE IVVDSHGATN VPGVFAAGDC 

       490        500        510 
TNSAYKQIII SMGSGATAAL GAFDYLIRNT TPAESAAAK

P26829 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