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Q43644 (NDUS1_SOLTU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. 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 1, mitochondrial

EC=1.6.5.3
EC=1.6.99.3
Alternative name(s):
76 kDa mitochondrial complex I subunit
Complex I-76kD
Short name=CI-76kD
NADH-ubiquinone oxidoreductase 76 kDa subunit
OrganismSolanum tuberosum (Potato) [Reference proteome]
Taxonomic identifier4113 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum

Protein attributes

Sequence length738 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. This is the largest subunit of complex I and it is a component of the iron-sulfur (IP) fragment of the enzyme. It may form part of the active site crevice where NADH is oxidized By similarity.

Catalytic activity

NADH + ubiquinone + 5 H+(In) = NAD+ + ubiquinol + 4 H+(Out).

NADH + acceptor = NAD+ + reduced acceptor.

Cofactor

Binds 1 2Fe-2S cluster per subunit By similarity.

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 By similarity. Note: Matrix and cytoplasmic side of the mitochondrial inner membrane By similarity.

Sequence similarities

Belongs to the complex I 75 kDa subunit family.

Contains 1 2Fe-2S ferredoxin-type domain.

Contains 1 4Fe-4S Mo/W bis-MGD-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2727Mitochondrion By similarity
Chain28 – 738711NADH dehydrogenase [ubiquinone] iron-sulfur protein 1, mitochondrial
PRO_0000019973

Regions

Domain66 – 144792Fe-2S ferredoxin-type
Domain281 – 337574Fe-4S Mo/W bis-MGD-type

Sites

Metal binding1001Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1111Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1141Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1281Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1601Iron-sulfur 2 (4Fe-4S); via pros nitrogen By similarity
Metal binding1641Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1671Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1731Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding2121Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding2151Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding2181Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding2621Iron-sulfur 3 (4Fe-4S) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q43644 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 4AA955A62EEAD2E8

FASTA73879,970
        10         20         30         40         50         60 
MGLGLLASRA LRSSRIIRNS TRTIVSTPEL KNADAAAAAA AADAPSDLPK RHPVGGARVH 

        70         80         90        100        110        120 
LPNPEDVIEV FVDGYPVKIP KGMTVLQACE IAGVDIPRFC YHSRLSIAGN CRMCLVEVEK 

       130        140        150        160        170        180 
SPKPVASCAM PALPGMKIKT DTPIAKKARE GVMEFLLMNH PLDCPICDQG GECDLQDQSM 

       190        200        210        220        230        240 
AFGSDRGRFT EMKRSVVDKN LGPLVKTVMT RCIQCTRCVR FASEVAGVED LGMLGRGSGE 

       250        260        270        280        290        300 
EIGTYVEKLM TSELSGNVID ICPVGALTSK PFAFKARNWE LKGTESIDVT DAVGSNIRID 

       310        320        330        340        350        360 
SRGPEVMRVV PRLNEDINEE WISDKTRFFY DGLKRQRLND PMIRGADGRF QAVSWRDALA 

       370        380        390        400        410        420 
IVAEVMHQIK PEEIVGVAGK LSDAESMMAL KDLLNKMGSN NIFCEGNGMH PNADLRSGYI 

       430        440        450        460        470        480 
MNTSISGLEK ADAFLLVGTQ PRVEAAMVNA RIHKTVKATN AKVGYVGPAA DFNYDHEHLG 

       490        500        510        520        530        540 
TDPQTLVEIA EGRHPFSSAL KNAKNPVIIV GAGVFDRDDK DAVFAAVDTI AKNNNVVRPD 

       550        560        570        580        590        600 
WNGLNVLLLN AAQVAALDLG LVPESDKCIE SAKFVYLMGA DDVNLDKLPD DAFVVYQGHH 

       610        620        630        640        650        660 
GDRGVYRANV ILPASAFTEK EGIYENTEGC AQITLPAVPT VGDARDDWKI VRALSEVAGV 

       670        680        690        700        710        720 
GLPYDSLGAI RSRIKTVAPN LLEVDERQPA TFSTSLRPEV SQKVSATPFT PAVENFYMTD 

       730 
AITRASKIMA QCSALLKK 

« Hide

References

[1]"Molecular characterisation of the 76 kDa iron-sulphur protein subunit of potato mitochondrial complex I."
Rasmusson A.G., Heiser V., Irrgang K.D., Brennicke A., Grohmann L.
Plant Cell Physiol. 39:373-381(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Desiree.
Tissue: Leaf.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X85808 mRNA. Translation: CAA59818.1.
PIRS52737.
RefSeqNP_001275317.1. NM_001288388.1.
UniGeneStu.2837.

3D structure databases

ProteinModelPortalQ43644.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ43644. 1 interaction.

Proteomic databases

PRIDEQ43644.
ProMEXQ43644.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID102594243.
KEGGsot:102594243.

Phylogenomic databases

KOK03934.

Family and domain databases

Gene3D3.10.20.30. 1 hit.
InterProIPR001041. 2Fe-2S_ferredoxin-type.
IPR012675. Beta-grasp_dom.
IPR006656. Mopterin_OxRdtase.
IPR006963. Mopterin_OxRdtase_4Fe-4S_dom.
IPR000283. NADH_UbQ_OxRdtase_75kDa_su_CS.
IPR010228. NADH_UbQ_OxRdtase_Gsu.
IPR019574. NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
IPR015405. NuoG_C.
[Graphical view]
PfamPF09326. DUF1982. 1 hit.
PF00111. Fer2. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF10588. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view]
SMARTSM00929. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view]
SUPFAMSSF54292. SSF54292. 1 hit.
TIGRFAMsTIGR01973. NuoG. 1 hit.
PROSITEPS51085. 2FE2S_FER_2. 1 hit.
PS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00641. COMPLEX1_75K_1. 1 hit.
PS00642. COMPLEX1_75K_2. 1 hit.
PS00643. COMPLEX1_75K_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNDUS1_SOLTU
AccessionPrimary (citable) accession number: Q43644
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 107 of the entry and version 1 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