NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial precursor

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P15690 (NDUS1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 120. 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-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

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	727 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. 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 process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Ligand	2Fe-2S 4Fe-4S Iron Iron-sulfur Metal-binding NAD Ubiquinone
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ATP metabolic process Inferred from sequence or structural similarity. Source: UniProtKB ATP synthesis coupled electron transport Inferred from electronic annotation. Source: InterPro apoptotic process 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_component	mitochondrial intermembrane space Inferred from sequence or structural similarity. Source: UniProtKB mitochondrial respiratory chain complex I Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	2 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 Biological aspect of Ancestor. Source: RefGenome 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 – 23

Mitochondrion

Chain

24 – 727

704

NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial Ref.1

PRO_0000019967

Regions

Domain

30 – 108

2Fe-2S ferredoxin-type

Sites

Metal binding

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

124

Iron-sulfur 2 (4Fe-4S); via pros nitrogen By similarity

Metal binding

128

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

Metal binding

131

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

Metal binding

137

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

Metal binding

176

Iron-sulfur 3 (4Fe-4S) By similarity

Metal binding

179

Iron-sulfur 3 (4Fe-4S) By similarity

Metal binding

182

Iron-sulfur 3 (4Fe-4S) By similarity

Metal binding

226

Iron-sulfur 3 (4Fe-4S) By similarity

Amino acid modifications

Modified residue

N6-acetyllysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P15690 [UniParc].

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

FASTA

727

79,442

        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

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References

	« Hide 'large scale' referencesShow '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] [Europe PMC] [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
EMBL GenBank DDBJ	J02877 mRNA. Translation: AAA30662.1. BC120069 mRNA. Translation: AAI20070.1.
IPI	IPI00708027.
PIR	A33552.
RefSeq	NP_777245.1. NM_174820.4.
UniGene	Bt.4777.
3D structure databases
ProteinModelPortal	P15690.
ModBase	Search...
Protein-protein interaction databases
IntAct	P15690. 4 interactions.
STRING	9913.ENSBTAP00000029301.
Protein family/group databases
TCDB	3.D.1.6.1. H+ or Na+-translocating NADH dehydrogenase (NDH) family.
Proteomic databases
PaxDb	P15690.
PRIDE	P15690.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000029301; ENSBTAP00000029301; ENSBTAG00000021976.
GeneID	288380.
KEGG	bta:288380.
Organism-specific databases
CTD	4719.
Phylogenomic databases
eggNOG	COG1034.
GeneTree	ENSGT00390000018768.
HOGENOM	HOG000031442.
HOVERGEN	HBG003482.
InParanoid	P15690.
KO	K03934.
OMA	LNTKIAG.
OrthoDB	EOG4D26PC.
Family and domain databases
Gene3D	3.10.20.30. 1 hit.
InterPro	IPR001041. 2Fe-2S_ferredoxin-type. IPR012675. Beta-grasp_dom. 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]
Pfam	PF09326. DUF1982. 1 hit. PF00111. Fer2. 1 hit. PF00384. Molybdopterin. 1 hit. PF10588. NADH-G_4Fe-4S_3. 1 hit. [Graphical view]
SMART	SM00929. NADH-G_4Fe-4S_3. 1 hit. [Graphical view]
SUPFAM	SSF54292. Ferredoxin. 1 hit.
TIGRFAMs	TIGR01973. NuoG. 1 hit.
PROSITE	PS00197. 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]
ProtoNet	Search...
Other
NextBio	20806551.

Entry information

Entry name

NDUS1_BOVIN

Accession

Primary (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:	April 3, 2013
This is version 120 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata 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

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents