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Q0MQG1 (NDUS1_GORGO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 46. 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-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial

EC=1.6.5.3
EC=1.6.99.3
Alternative name(s):
Complex I-75kD
Short name=CI-75kD
Gene names
Name:NDUFS1
OrganismGorilla gorilla gorilla (Lowland gorilla) [Reference proteome]
Taxonomic identifier9595 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeGorilla

Protein attributes

Sequence length727 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 45 different subunits 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.

Ontologies

Keywords
   Biological processElectron transport
Respiratory chain
Transport
   Cellular componentMembrane
Mitochondrion
Mitochondrion inner membrane
   DomainTransit peptide
   Ligand2Fe-2S
4Fe-4S
Iron
Iron-sulfur
Metal-binding
NAD
Ubiquinone
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

ATP synthesis coupled electron transport

Inferred from electronic annotation. Source: InterPro

apoptotic mitochondrial changes

Inferred from sequence or structural similarity. Source: UniProtKB

cellular respiration

Inferred from sequence or structural similarity. Source: UniProtKB

reactive oxygen species metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of mitochondrial membrane potential

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentmitochondrial intermembrane space

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial respiratory chain complex I

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_function2 iron, 2 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

NADH dehydrogenase (ubiquinone) activity

Inferred from electronic annotation. Source: UniProtKB-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2323Mitochondrion By similarity
Chain24 – 727704NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
PRO_0000251853

Regions

Domain30 – 108792Fe-2S ferredoxin-type
Domain245 – 301574Fe-4S Mo/W bis-MGD-type

Sites

Metal binding641Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding751Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding781Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding921Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1241Iron-sulfur 2 (4Fe-4S); via pros nitrogen By similarity
Metal binding1281Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1311Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1371Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1761Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding1791Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding1821Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding2261Iron-sulfur 3 (4Fe-4S) By similarity

Amino acid modifications

Modified residue841N6-acetyllysine By similarity
Modified residue4671N6-acetyllysine By similarity
Modified residue4991N6-acetyllysine By similarity
Modified residue7091N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0MQG1 [UniParc].

Last modified September 19, 2006. Version 1.
Checksum: 860FE5560CB47D3C

FASTA72779,450
        10         20         30         40         50         60 
MLRIPVRKAL VGLSKSPKGC VRTTATAASN LIEVFVDGQS VMVEPGTTVL QACEKVGMQI 

        70         80         90        100        110        120 
PRFCYHERLS VAGNCRMCLV EIEKAPKVVA ACAMPVMKGW NILTNSEKSK KAREGVMEFL 

       130        140        150        160        170        180 
LANHPLDCPI CDQGGECDLQ DQSMMFGNDR SRFLEGKRAV EDKNIGPLVK TIMTRCIQCT 

       190        200        210        220        230        240 
RCIRFASEIA GVDDLGTTGR GNDMQVGTYI EKMFMSELSG NIIDICPVGA LTSKPYAFTA 

       250        260        270        280        290        300 
RPWETRKTES IDVMDAVGSN IVVSTRTGEV MRILPRMHED INEXWISDKT RFAYDGLKRQ 

       310        320        330        340        350        360 
RLTEPMVRNE KGLLTYTSWE DALSRVAGML QSFQGKDVAA IAGGLVDAEA LVALKDLLNR 

       370        380        390        400        410        420 
VDSDTLCTEE VFPTAGAGTD LRSNYLLNTT IAGVEEADVV LLVGTNPRFE APLFNARIRK 

       430        440        450        460        470        480 
SWLHNDLKVA LIGSPVDLTY TYDHLGDSPK ILQDIASGSH PFSQVLKEAK KPMVVLGSSA 

       490        500        510        520        530        540 
LQRNDGAAIL AAVSSIAQKI RMTSGVTGDW KVMNILHRIA SQVAALDLGY KPGVEAIRKN 

       550        560        570        580        590        600 
PPKVLFLLGA DGGCITRQDL PKDCFIIYQG HHGDVGAPIA DVILPGAAYT EKSATYVNTE 

       610        620        630        640        650        660 
GRAQQTKVAV TPPGLAREDW KIIRALSEIA GMTLPYDTLD QVRNRLEEVS PNLVRYDDIE 

       670        680        690        700        710        720 
GANYFQQANE LSKLVNQQLL ADPLVPPQLT IKDFYMTDSI SRASQTMAKC VKAVTEGAQA 


VEEPSIC 

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References

[1]"Adaptive selection of mitochondrial complex I subunits during primate radiation."
Mishmar D., Ruiz-Pesini E., Mondragon-Palomino M., Procaccio V., Gaut B., Wallace D.C.
Gene 378:11-18(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ885673 mRNA. Translation: ABH12182.1.
RefSeqNP_001266520.1. NM_001279591.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ0MQG1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID101139264.

Organism-specific databases

CTD4719.

Phylogenomic databases

HOVERGENHBG003482.

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.
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_GORGO
AccessionPrimary (citable) accession number: Q0MQG1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: September 19, 2006
Last modified: May 14, 2014
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families