[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/S0005-2728(99)00014-6; PubMed=10216160 [NCBI, ExPASy, EBI, Israel, Japan] Sousa R., Barquera B., Duarte M., Finel M., Videira A.; "Characterisation of the last Fe-S cluster-binding subunit of Neurospora crassa complex I."; Biochim. Biophys. Acta 1411:142-146(1999).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987; DOI=10.1093/nar/gkg293; PubMed=12655011 [NCBI, ExPASy, EBI, Israel, Japan] Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.; "What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence."; Nucleic Acids Res. 31:1944-1954(2003).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987; DOI=10.1038/nature01554; PubMed=12712197 [NCBI, ExPASy, EBI, Israel, Japan] Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.; "The genome sequence of the filamentous fungus Neurospora crassa."; Nature 422:859-868(2003).

Comments

FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
CATALYTIC ACTIVITY: NADH + ubiquinone = NAD⁺ + ubiquinol.
CATALYTIC ACTIVITY: NADH + acceptor = NAD⁺ + reduced acceptor.
COFACTOR: Binds 1 4Fe-4S cluster (Potential).
SUBUNIT: Complex I is composed of about 40 different subunits. This is a component of the iron-sulfur (IP) fragment of the enzyme.
SUBCELLULAR LOCATION: Mitochondrion.
SIMILARITY: Belongs to the complex I 20 kDa subunit 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

AJ001520; CAA04802.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BX908812; CAF06152.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AABX02000012; EAA28356.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

XP_957592.1; -.

3D structure databases

ModBase

O47950.

Enzyme and pathway databases

BioCyc

NCRA-XX3-01:NCRA-XX3-01-007701-MON; -.

Family and domain databases

InterPro

IPR006138; NADH_DHase_20kDa_su.
IPR014406; NiFe_hyd_3_ssu/Q_oxred_NuoB.
IPR006137; OxRdtase_q6.
Graphical view of domain structure.

PANTHER

PTHR11995:SF2; NADH_DH_20kDa; 1.
PTHR11995; NiFe_hyd_3_ssu/Q_oxred_NuoB; 1.

Pfam

PF01058; Oxidored_q6; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01957; nuoB_fam; 1.

PROSITE

PS01150; COMPLEX1_20K; 1.

BLOCKS

O47950.

Genome annotation databases

GeneID

3873682; -.

KEGG

ncr:NCU03953; -.

NMPDR

fig|5141.1.peg.1205; -.

Other

ProtoNet

O47950.

UniRef

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

Keywords

4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; Metal-binding; Mitochondrion; NAD; Oxidoreductase; Respiratory chain; Transit peptide; Transport; Ubiquinone.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 ?`		`Mitochondrion (Potential).`
`CHAIN`	`? 226`		`NADH-ubiquinone oxidoreductase 19.3 kDa subunit, mitochondrial.`	`PRO_0000020032`
`METAL`	`101 101`		`Iron-sulfur (4Fe-4S) (Potential).`
`METAL`	`102 102`		`Iron-sulfur (4Fe-4S) (Potential).`
`METAL`	`166 166`		`Iron-sulfur (4Fe-4S) (Potential).`
`METAL`	`196 196`		`Iron-sulfur (4Fe-4S) (Potential).`

Sequence information

Length: 226 AA [This is the length of the unprocessed precursor]

Molecular weight: 24972 Da [This is the MW of the unprocessed precursor]

CRC64: E48CB09C64AAAFC6 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MMSSVRTGAS MALRARPTAQ IVPFRAAAVA SISSSSRKDA TGAVAPAGAQ HGIARRERRE 

        70         80         90        100        110        120 
VPLPSQEGTK GAVQYALTTL DSIVNWARQS SLWPMTFGLA CCAVEMMHLS TPRYDQDRLG 

       130        140        150        160        170        180 
IIFRASPRQS DVMIVAGTLT NKMAPALRQV YDQMPDPRWV ISMGSCANGG GYYHYSYSVV 

       190        200        210        220 
RGCDRIVPVD IYVPGCPPTS EALMYGIFQL QRKMRNTKIT RMWYRK

O47950 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