NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial precursor

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P80269 (NDUS8_SOLTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 97. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names	Recommended name: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial EC=1.6.5.3 EC=1.6.99.3 Alternative name(s): Complex I-28.5kD Short name=CI-28.5kD NADH-ubiquinone oxidoreductase 28.5 kDa subunit
Organism	Solanum tuberosum (Potato) [Reference proteome]
Taxonomic identifier	4113 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum

Protein attributes

Sequence length	229 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. May donate electrons to ubiquinone.
Catalytic activity	NADH + ubiquinone = NAD⁺ + ubiquinol. NADH + acceptor = NAD⁺ + reduced acceptor.
Cofactor	Binds 2 4Fe-4S clusters per subunit By similarity.
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.
Tissue specificity	Lowest expression found in storage tissues of tubers. Higher expression in older leaves than younger ones. Highest expression found in flowers.
Polymorphism	There are two alleles; TYKY1 (shown here) and TYKY2.
Sequence similarities	Belongs to the complex I 23 kDa subunit family. Contains 2 4Fe-4S ferredoxin-type domains.
Caution	Was originally (Ref.1) reported that TYKY1 and TYKY2 were two different genes.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Coding sequence diversity	Polymorphism
Domain	Repeat Transit peptide
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding NAD Ubiquinone
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell respiratory chain Inferred from electronic annotation. Source: UniProtKB-KW
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 electron carrier activity Inferred from electronic annotation. Source: InterPro metal ion 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 – 41

Mitochondrion Ref.2

Chain

42 – 229

188

NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial

PRO_0000020017

Regions

Domain

121 – 150

4Fe-4S ferredoxin-type 1

Domain

160 – 189

4Fe-4S ferredoxin-type 2

Sites

Metal binding

130

Iron-sulfur 1 (4Fe-4S) By similarity

Metal binding

133

Iron-sulfur 1 (4Fe-4S) By similarity

Metal binding

136

Iron-sulfur 1 (4Fe-4S) By similarity

Metal binding

140

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

169

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

172

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

175

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

179

Iron-sulfur 1 (4Fe-4S) By similarity

Natural variations

Natural variant

23 – 26

HTIE → QAWQ in allele TYKY2.

Natural variant

30 – 33

GYNR → TPNG in allele TYKY2.

Natural variant

E → R in strain: cv. Bintje.

Natural variant

E → K in strain: cv. Bintje.

Natural variant

K → T in strain: cv. Bintje.

Natural variant

121

R → H in allele TYKY2.

Natural variant

216

T → I in allele TYKY2.

Sequences

Sequence

Length

Mass (Da)

Tools

P80269 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: D995415DBE064A93
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FASTA

229

26,378

        10         20         30         40         50         60 
MAAILARKSL SALRSRQLVL AGHTIEGTNG YNRTLLGTRS FATKHSFSTD KDDEEREQLA 

        70         80         90        100        110        120 
KELSKDWNSV FERSINTLFL TEMVRGLMLT LKYFFEKKVT INYPFEKGPL SPRFRGEHAL 

       130        140        150        160        170        180 
RRYATGEERC IACKLCEAIC PAQAITIEAE EREDGSRRTT RYDIDMTKCI YCGFCQEACP 

       190        200        210        220 
VDAIVEGPNF EFATETHEEL LYDKEKLLEN GDRWETEIAE NLRSESLYR

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References

[1]	"The 28.5-kDa iron-sulfur protein of mitochondrial complex I is encoded in the nucleus in plants." Schmidt-Bleek K., Heiser V., Thieck O., Brennicke A., Grohmann L. Mol. Gen. Genet. 253:448-454(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELES TYKY1 AND TYKY2). Strain: cv. Desiree. Tissue: Leaf.
[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 42-65. Strain: cv. Bintje. Tissue: Tuber.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X84319 mRNA. Translation: CAA59062.1. X84320 mRNA. Translation: CAA59063.1.
PIR	S52385. S52386.
3D structure databases
ProteinModelPortal	P80269.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	PGSC0003DMT400084285; PGSC0003DMT400084285; PGSC0003DMG400033912.
Family and domain databases
Gene3D	1.10.1060.10. 1 hit.
InterPro	IPR001450. 4Fe4S-bd_dom. IPR017896. 4Fe4S_Fe-S-bd. IPR017900. 4Fe4S_Fe_S_CS. IPR012285. Fum_reductase_C. IPR010226. NADH_quinone_OxRdtase_chainI. [Graphical view]
Pfam	PF12838. Fer4_7. 1 hit. [Graphical view]
TIGRFAMs	TIGR01971. NuoI. 1 hit.
PROSITE	PS00198. 4FE4S_FER_1. 2 hits. PS51379. 4FE4S_FER_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NDUS8_SOLTU

Accession

Primary (citable) accession number: P80269
Secondary accession number(s): Q43849, Q43850

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	May 30, 2000
Last modified:	May 1, 2013
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Natural variations

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Family and domain databases

Entry information

Relevant documents