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O94500 (NDUV1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length452 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred 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 + 5 H+(In) = NAD+ + ubiquinol + 4 H+(Out).

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2525Mitochondrion Potential
Chain26 – 452427NADH-ubiquinone oxidoreductase 51 kDa subunit, mitochondrial
PRO_0000317309

Regions

Nucleotide binding80 – 8910NAD By similarity
Nucleotide binding198 – 24548FMN By similarity

Sites

Metal binding3771Iron-sulfur (4Fe-4S) Potential
Metal binding3801Iron-sulfur (4Fe-4S) Potential
Metal binding3831Iron-sulfur (4Fe-4S) Potential
Metal binding4241Iron-sulfur (4Fe-4S) Potential

Sequences

Sequence LengthMass (Da)Tools
O94500 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 6C199251A7598374

FASTA45250,095
        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 

« Hide

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. expand/collapse author list , 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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329671 Genomic DNA. Translation: CAA22670.1.
PIRT39761.
RefSeqNP_595857.1. NM_001021761.2.

3D structure databases

ProteinModelPortalO94500.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4684703.
STRING4896.SPBC18E5.10-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC18E5.10.1; SPBC18E5.10.1:pep; SPBC18E5.10.
GeneID2540740.
KEGGspo:SPBC18E5.10.

Organism-specific databases

PomBaseSPBC18E5.10.

Phylogenomic databases

eggNOGCOG1894.
HOGENOMHOG000251534.
KOK03942.
OMACKDAPLM.
OrthoDBEOG7M3J8B.
PhylomeDBO94500.

Family and domain databases

InterProIPR019575. NADH-UbQ_OxRdtase_Fsu_4Fe4S-bd.
IPR011538. NADH_UbQ_OxRdtase_51kDa_su.
IPR019554. Soluble_ligand-bd.
[Graphical view]
PfamPF01512. Complex1_51K. 1 hit.
PF10531. SLBB. 1 hit.
[Graphical view]
SMARTSM00928. NADH_4Fe-4S. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20801862.
PROO94500.

Entry information

Entry nameNDUV1_SCHPO
AccessionPrimary (citable) accession number: O94500
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names