NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial precursor

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Reviewed, UniProtKB/Swiss-Prot Q5R911 (NDUS1_PONAB)

Last modified November 25, 2008. Version 27. History...

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

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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

Pongo abelii (Sumatran orangutan)

Taxonomic identifier

9601 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

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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 transcript level.

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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 = 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 By similarity.
Subcellular location	Mitochondrion inner membraneBy 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.

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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
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 apoptosis Inferred from sequence or structural similarity. Source: UniProtKB cellular respiration 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 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 electronic annotation. Source: InterPro 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...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 23

Mitochondrion By similarity

Chain

24 – 727

704

NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial

PRO_0000019970

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

Experimental info

Sequence conflict

119

F → L in CAH91749. Ref.2

Sequence conflict

493

V → F in CAH91749. Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

Q5R911-1 [UniParc].

Last modified October 3, 2006. Version 2.
Checksum: D9561B21A86F3BF3
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FASTA

727

79,477

        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 INEEWISDKT 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 
PPRLLFLLGA DGGCITRQDL PKDCFIIYQG HHGDVGAPIA DVILPGAAYT EKSATYVNTE 

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

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


VEEPSIC

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References

	« Hide 'large scale' referencesShow 'large scale' 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: 16828987] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Heart.

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Cross-references

Sequence databases
	DQ885674 mRNA. Translation: ABH12183.1. CR859585 mRNA. Translation: CAH91749.1.
3D structure databases
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q5R911.
Family and domain databases
InterPro	IPR006058. 2Fe2S_fd_BS. IPR001041. Ferredoxin. IPR006656. Mopterin_OxRdtase. IPR000283. NADH_DHase_75KDa_su_CS. IPR010228. NADH_quinone_OxRdtase_G. IPR015405. NuoG_C. [Graphical view]
Pfam	PF09326. DUF1982. 1 hit. PF00111. Fer2. 1 hit. PF00384. Molybdopterin. 1 hit. [Graphical view]
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...

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Entry information

Entry name

NDUS1_PONAB

Accession

Primary (citable) accession number: Q5R911
Secondary accession number(s): Q0MQG0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2005
Last sequence update:	October 3, 2006
Last modified:	November 25, 2008
This is version 27 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents