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Q0MQG2

- NDUS1_PANTR

UniProt

Q0MQG2 - NDUS1_PANTR

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Protein

NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial

Gene
NDUFS1
Organism
Pan troglodytes (Chimpanzee)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

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 activityi

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

Cofactori

Binds 1 2Fe-2S cluster per subunit By similarity.
Binds 2 4Fe-4S clusters per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi64 – 641Iron-sulfur 1 (2Fe-2S) By similarity
Metal bindingi75 – 751Iron-sulfur 1 (2Fe-2S) By similarity
Metal bindingi78 – 781Iron-sulfur 1 (2Fe-2S) By similarity
Metal bindingi92 – 921Iron-sulfur 1 (2Fe-2S) By similarity
Metal bindingi124 – 1241Iron-sulfur 2 (4Fe-4S); via pros nitrogen By similarity
Metal bindingi128 – 1281Iron-sulfur 2 (4Fe-4S) By similarity
Metal bindingi131 – 1311Iron-sulfur 2 (4Fe-4S) By similarity
Metal bindingi137 – 1371Iron-sulfur 2 (4Fe-4S) By similarity
Metal bindingi176 – 1761Iron-sulfur 3 (4Fe-4S) By similarity
Metal bindingi179 – 1791Iron-sulfur 3 (4Fe-4S) By similarity
Metal bindingi182 – 1821Iron-sulfur 3 (4Fe-4S) By similarity
Metal bindingi226 – 2261Iron-sulfur 3 (4Fe-4S) By similarity

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
  2. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  3. electron carrier activity Source: InterPro
  4. metal ion binding Source: UniProtKB-KW
  5. NADH dehydrogenase (ubiquinone) activity Source: RefGenome

GO - Biological processi

  1. apoptotic mitochondrial changes Source: UniProtKB
  2. ATP metabolic process Source: UniProtKB
  3. ATP synthesis coupled electron transport Source: InterPro
  4. cellular respiration Source: UniProtKB
  5. reactive oxygen species metabolic process Source: UniProtKB
  6. regulation of mitochondrial membrane potential Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Keywords - Ligandi

2Fe-2S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding, NAD, Ubiquinone

Names & Taxonomyi

Protein namesi
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 namesi
Name:NDUFS1
OrganismiPan troglodytes (Chimpanzee)
Taxonomic identifieri9598 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePan
ProteomesiUP000002277: Unplaced

Subcellular locationi

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

GO - Cellular componenti

  1. mitochondrial intermembrane space Source: UniProtKB
  2. mitochondrial respiratory chain complex I Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2323Mitochondrion By similarityAdd
BLAST
Chaini24 – 727704NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrialPRO_0000251855Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei84 – 841N6-acetyllysine By similarity
Modified residuei467 – 4671N6-acetyllysine By similarity
Modified residuei499 – 4991N6-acetyllysine By similarity
Modified residuei709 – 7091N6-acetyllysine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiQ0MQG2.

Interactioni

Subunit structurei

Complex I is composed of 45 different subunits By similarity.

Protein-protein interaction databases

STRINGi9598.ENSPTRP00000021965.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 108792Fe-2S ferredoxin-typeAdd
BLAST
Domaini245 – 301574Fe-4S Mo/W bis-MGD-typeAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1034.
HOGENOMiHOG000031442.
HOVERGENiHBG003482.
InParanoidiQ0MQG2.
KOiK03934.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 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]
PfamiPF09326. DUF1982. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF10588. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view]
SMARTiSM00929. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view]
SUPFAMiSSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR01973. NuoG. 1 hit.
PROSITEiPS51085. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q0MQG2-1 [UniParc]FASTAAdd to Basket

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MLRIPVRKAL VVLSKSPKGC VRTTATAASN LIEVFVDGQS VMVEPGTTVL    50
QACEKVGMQI PRFCYHERLS VAGNCRMCLV EIEKAPKVVA ACAMPVMKGW 100
NILTNSKKSK KAREGVMEFL LANHPLDCPI CDQGGECDLQ DQSMMFGNDR 150
SRFLEGKRAV EDKNIGPLVK TIMTRCIQCT RCIRFASEIA GVDDLGTTGR 200
GNDMQVGTYI EKMFMSELSG NIIDICPVGA LTSKPYAFTA RPWETRKTES 250
IDVMDAVGSN IVVSTRTGEV MRILPRMHED INEEWISDKT RFAYDGLKRQ 300
RLTEPMVRNE KGLLTYTSWE DALSRVAGML QTFQGKDVAA IAGGLVDAEA 350
LVALKDLLNR VDSDTLCTEE VFPTAGAGTD LRSNYLLNTT IAGVEEADVV 400
LLVGTNPRFE APLFNARLRK SWLHNDLKVA LIGSPVDLTY TYDHLGDSPK 450
ILQDIASGSH PFSQVLKEAK KPMVVLGSSA LQRNDGAAIL AAVSSIAQKI 500
RMTSGVTGDW KVMNILHRIA SQVAALDLGY KPGVEAIRKN PPKVLFLLGA 550
DGGCITRQDL PKDCFIIYQG HHGDVGAPIA DVILPGAAYT EKSATYVNTE 600
GRAQQTKVAV TPPGLAREDW KIIRALSEIA GMTLPYDTLD QVRNRLEEVS 650
PNLVRYDDIE GANYFQQANE LSKLVNQQLL ADPLVPPQLT IKDFYMTDSI 700
SRASQTMAKC VKAVTEGAQA VEEPSIC 727
Length:727
Mass (Da):79,523
Last modified:September 19, 2006 - v1
Checksum:iC22C6D8901A9B05F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ885672 mRNA. Translation: ABH12181.1.
RefSeqiNP_001073384.1. NM_001079915.1.
UniGeneiPtr.404.

Genome annotation databases

GeneIDi459896.
KEGGiptr:459896.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ885672 mRNA. Translation: ABH12181.1 .
RefSeqi NP_001073384.1. NM_001079915.1.
UniGenei Ptr.404.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9598.ENSPTRP00000021965.

Proteomic databases

PRIDEi Q0MQG2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 459896.
KEGGi ptr:459896.

Organism-specific databases

CTDi 4719.

Phylogenomic databases

eggNOGi COG1034.
HOGENOMi HOG000031442.
HOVERGENi HBG003482.
InParanoidi Q0MQG2.
KOi K03934.

Miscellaneous databases

NextBioi 20839934.

Family and domain databases

Gene3Di 3.10.20.30. 1 hit.
InterProi IPR001041. 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 ]
Pfami PF09326. DUF1982. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF10588. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view ]
SMARTi SM00929. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view ]
SUPFAMi SSF54292. SSF54292. 1 hit.
TIGRFAMsi TIGR01973. NuoG. 1 hit.
PROSITEi PS51085. 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 ]
ProtoNeti Search...

Publicationsi

  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].

Entry informationi

Entry nameiNDUS1_PANTR
AccessioniPrimary (citable) accession number: Q0MQG2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: September 19, 2006
Last modified: January 22, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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