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P80261 (NDUS3_SOLTU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 dehydrogenase [ubiquinone] iron-sulfur protein 3

EC=1.6.5.3
EC=1.6.99.3
Alternative name(s):
Complex I-27kD
Short name=CI-27kD
NADH dehydrogenase subunit 9
NADH-ubiquinone oxidoreductase 27 kDa subunit
Gene names
Name:NAD9
Encoded onMitochondrion
OrganismSolanum tuberosum (Potato) [Reference proteome]
Taxonomic identifier4113 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum

Protein attributes

Sequence length190 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. HAMAP-Rule MF_01357

Catalytic activity

NADH + ubiquinone + 5 H+(In) = NAD+ + ubiquinol + 4 H+(Out). HAMAP-Rule MF_01357

NADH + acceptor = NAD+ + reduced acceptor. HAMAP-Rule MF_01357

Subunit structure

Complex I is composed of about 45 different subunits. This is a component of the iron-sulfur (IP) fragment of the enzyme By similarity.

Subcellular location

Mitochondrion inner membrane; Peripheral membrane protein; Matrix side HAMAP-Rule MF_01357.

Sequence similarities

Belongs to the complex I 30 kDa subunit family.

RNA editing

Edited at positions 31, 56, 100, 110, 122, 133 and 147. Ref.1

Ontologies

Keywords
   Biological processElectron transport
Respiratory chain
Transport
   Cellular componentMembrane
Mitochondrion
Mitochondrion inner membrane
   Coding sequence diversityRNA editing
   LigandNAD
Ubiquinone
   Molecular functionOxidoreductase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Cellular_componentmitochondrial inner membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

respiratory chain

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionNADH dehydrogenase (ubiquinone) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 190190NADH dehydrogenase [ubiquinone] iron-sulfur protein 3 HAMAP-Rule MF_01357
PRO_0000118643

Sequences

Sequence LengthMass (Da)Tools
P80261 [UniParc].

Last modified November 28, 2003. Version 3.
Checksum: A150CF461B493A53

FASTA19022,883
        10         20         30         40         50         60 
MDNQFIFKYS WETLPKKWVK KMERSEHGNR FDTNTDYLFQ LLCFMKLHTY TRVQVLIDIC 

        70         80         90        100        110        120 
GVDYPSRKQR FEVVYNLLSI RYNSRIRVQT SADEVTRISS VVSLFPSAGW WEREVWDMFG 

       130        140        150        160        170        180 
VFSINHPDLR RILTDYGFEG HPLRKDFPLS GYVEVRYDDP EKRVVSEPIE MTQEFRYFDF 

       190 
ASPWEQRSDG 

« Hide

References

[1]"Translation of nad9 mRNAs in mitochondria from Solanum tuberosum is restricted to completely edited transcripts."
Grohmann L., Thieck O., Herz U., Schroeder W., Brennicke A.
Nucleic Acids Res. 22:3304-3311(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, RNA EDITING.
Tissue: Tuber.
[2]"Purification of the NADH:ubiquinone oxidoreductase (complex I) of the respiratory chain from the inner mitochondrial membrane of Solanum tuberosum."
Herz U., Schroeder W., Liddell A., Leaver C.J., Brennicke A., Grohmann L.
J. Biol. Chem. 269:2263-2269(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-17.
Strain: cv. Bintje.
Tissue: Tuber.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X79774 Genomic DNA. Translation: CAA56168.1. Sequence problems.
PIRS48062.

3D structure databases

ProteinModelPortalP80261.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

HAMAPMF_01357. NDH1_NuoC.
InterProIPR010218. NADH_DH_suC.
IPR001268. NADH_UbQ_OxRdtase_30kDa_su.
IPR020396. NADH_UbQ_OxRdtase_CS.
[Graphical view]
PfamPF00329. Complex1_30kDa. 1 hit.
[Graphical view]
ProDomPD001581. NADH_UbQ_OxRdtase_30kDa_su. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01961. NuoC_fam. 1 hit.
PROSITEPS00542. COMPLEX1_30K. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNDUS3_SOLTU
AccessionPrimary (citable) accession number: P80261
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: November 28, 2003
Last modified: February 19, 2014
This is version 80 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families