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Reviewed, UniProtKB/Swiss-Prot P15690 (NDUS1_BOVIN)

Last modified June 16, 2009. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length727 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. 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.

Catalytic activity

NADH + ubiquinone = NAD+ + ubiquinol.

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.

Subcellular location

Mitochondrion inner membrane.

Sequence similarities

Belongs to the complex I 75 kDa subunit family.

Contains 1 2Fe-2S ferredoxin-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 termDirect protein sequencing
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

apoptosis

Inferred from sequence or structural similarity. Source: UniProtKB

oxygen and 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

transport

Inferred from electronic annotation. Source: UniProtKB-KW

   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: EC

electron carrier activity

Inferred from electronic annotation. Source: InterPro

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2323Mitochondrion
Chain24 – 727704NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial Ref.1
PRO_0000019967

Regions

Domain30 – 108792Fe-2S ferredoxin-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

Sequences

Sequence LengthMass (Da)Tools
P15690-1 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: BEAD8AB5D76FC22D

FASTA72779,442
        10         20         30         40         50         60 
MLRIPVRKAL VGLSKSSKGC VRTTATAASN LIEVFVDGQS VMVEPGTTVL QACEKVGMQI 

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

       130        140        150        160        170        180 
LANHPLDCPI CDQGGECDLQ DQSMMFGSDR 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 INEEWISDKT RFAYDGLKRQ 

       310        320        330        340        350        360 
RLTEPMVRNE KGLLTHTTWE DALSRVAGML QSFQGNDVAA IAGGLVDAEA LIALKDLLNR 

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

       430        440        450        460        470        480 
SWLHNDLKVA LIGSPVDLTY RYDHLGDSPK ILQDIASGSH PFSQVLQEAK KPMVILGSSA 

       490        500        510        520        530        540 
LQRNDGAAIL AAVSNIAQKI RTSSGVTGDW KVMNILHRIA SQVAALDLGY KPGVEAIQKN 

       550        560        570        580        590        600 
PPKMLFLLGA DGGCITRQDL PKDCFIVYQG HHGDVGAPIA DVILPGAAYT EKSATYVNTE 

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

       670        680        690        700        710        720 
GANYFQQASE LSKLVNQQLL ADPLVPPQLT IKDFYMTDSI SRASQTMAKC VKAVTEGAHA 


VEEPSIC 

« Hide

References

« Hide 'large scale' references
[1]"Mitochondrial NADH:ubiquinone reductase: complementary DNA sequence of the import precursor of the bovine 75-kDa subunit."
Runswick M.J., Gennis R.B., Fearnley I.M., Walker J.E.
Biochemistry 28:9452-9459(1989) [PubMed: 2514801] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal pons.

Cross-references

Sequence databases

J02877 mRNA. Translation: AAA30662.1.
BC120069 mRNA. Translation: AAI20070.1.
IPIIPI00708027.
PIRA33552.
RefSeqNP_777245.1.
UniGeneBt.4777

3D structure databases

ModBaseSearch...

Protein family/group databases

TCDB3.D.1.6.1. proton-translocating NADH dehydrogenase (NDH) family.

Genome annotation databases

EnsemblENSBTAG00000021976. Bos taurus. [Contig view]
GeneID288380.
KEGGbta:288380.

Phylogenomic databases

HOVERGENP15690.
OMAP15690. RMSSGVT.

Enzyme and pathway databases

BRENDA1.6.5.3. 251.
1.6.99.3. 251.

Family and domain databases

InterProIPR006058. 2Fe2S_fd_BS.
IPR001041. Ferredoxin.
IPR006656. Mopterin_OxRdtase.
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]
TIGRFAMsTIGR01973. NuoG. 1 hit.
PROSITEPS00197. 2FE2S_FER_1. False negative.
PS51085. 2FE2S_FER_2. 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_BOVIN
AccessionPrimary (citable) accession number: P15690
Secondary accession number(s): Q0VCP7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: June 16, 2009
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents