O94500 (NDUV1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
NADH-ubiquinone oxidoreductase 51 kDa subunit, mitochondrial
EC=1.6.5.3
EC=1.6.99.3

Alternative name(s):
Complex I-51kD
Short name=CI-51kD

Gene names

ORF Names:

SPBC18E5.10

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	452 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (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 By similarity.
Catalytic activity	NADH + ubiquinone = NAD+ + ubiquinol. NADH + acceptor = NAD+ + reduced acceptor.
Cofactor	Binds 1 FMN Potential. Binds 1 4Fe-4S cluster Potential.
Subunit structure	Complex I is composed of about 40 different subunits. This is a component of the flavoprotein-sulfur (FP) fragment of the enzyme By similarity.
Subcellular location	Mitochondrion Ref.2.
Sequence similarities	Belongs to the complex I 51 kDa subunit family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	4Fe-4S FMN Flavoprotein Iron Iron-sulfur Metal-binding NAD
Molecular function	Oxidoreductase
PTM	Quinone
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	iron-sulfur cluster assembly Non-traceable author statement. Source: PomBase
Cellular_component	mitochondrion Inferred from direct assay Ref.2. Source: PomBase
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW NADH dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW quinone binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 25	25	Mitochondrion Potential
	Chain	26 – 452	427	NADH-ubiquinone oxidoreductase 51 kDa subunit, mitochondrial		PRO_0000317309
Regions
	Nucleotide binding	80 – 89	10	NAD By similarity
	Nucleotide binding	198 – 245	48	FMN By similarity
Sites
	Metal binding	377	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	380	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	383	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	424	1	Iron-sulfur (4Fe-4S) Potential

Sequences

	Sequence		Length	Mass (Da)
	O94500 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 6C199251A7598374	FASTA	452	50,095
	10 20 30 40 50 60 MLSRGHCCKL KHSFNGLRNV ALKRLVGSKA GYRMFPNLIE KRIRRIDDAL ADGEYENLSE 70 80 90 100 110 120 ILKYDPLNII ELVQESELRG RGRYGFPTGE KMLSLYKATS SERGRKEKPV VIVNAAENDI 130 140 150 160 170 180 GSFKDRLLLR HEPHKIIEGA IIAARAVEAS ACYLFIRKDY YEETVMMQKC IIQAYAKKLL 190 200 210 220 230 240 GKNLLGTSIG LELLIHPGAG SYITGEESAL IQSLQGEFPV PDIPINNTIT SGLFGLPTLV 250 260 270 280 290 300 LNVETVSNLP AIIKKGPKFF ISMGRPNNRG TKLFSISGEV NEPNVIEACM SIPLKDLIEN 310 320 330 340 350 360 YAGGVRGGWN KLVGIFPGGP CSGILNKNQC EQVTMDFDSL KALDSSLGTG SVIVLNDHDQ 370 380 390 400 410 420 IFESLLNFAK FYSTNTCHTC PVCRDGVEDV IETLKGLKDG HAHLSQLKDM FSKFNMPSSS 430 440 450 KVFCGFGDSM RHQIHSIQRN FPDQITFRTK VT

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.

[2]

"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329671 Genomic DNA. Translation: CAA22670.1.
PIR	T39761.
RefSeq	NP_595857.1. NM_001021761.2.
3D structure databases
HSSP	HSSP built from PDB template 2FUG based on UniProtKB Q56222.
ProteinModelPortal	O94500.
ModBase	Search...
Protein-protein interaction databases
STRING	4896.SPBC18E5.10-1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPBC18E5.10.1; SPBC18E5.10.1:pep; SPBC18E5.10.
GeneID	2540740.
KEGG	spo:SPBC18E5.10.
Organism-specific databases
PomBase	SPBC18E5.10.
Phylogenomic databases
eggNOG	COG1894.
HOGENOM	HOG000251534.
KO	K03942.
OMA	PSGMKWS.
OrthoDB	EOG4H1F42.
Family and domain databases
InterPro	IPR019575. NADH-UbQ_OxRdtase_Fsu_4Fe4S-bd. IPR011538. NADH_UbQ_OxRdtase_51kDa_su. IPR019554. Soluble_ligand-bd. [Graphical view]
Pfam	PF01512. Complex1_51K. 1 hit. PF10531. SLBB. 1 hit. [Graphical view]
SMART	SM00928. NADH_4Fe-4S. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20801862.

Entry information

Entry name

NDUV1_SCHPO

Accession

Primary (citable) accession number: O94500

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	May 1, 1999
Last modified:	April 3, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program