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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.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 nitrogenBy 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 – 2323MitochondrionBy similarityAdd
BLAST
Chaini24 – 727704NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrialPRO_0000251855Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei84 – 841N6-acetyllysineBy similarity
Modified residuei467 – 4671N6-acetyllysineBy similarity
Modified residuei499 – 4991N6-acetyllysineBy similarity
Modified residuei709 – 7091N6-acetyllysineBy 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-typePROSITE-ProRule annotationAdd
BLAST
Domaini245 – 301574Fe-4S Mo/W bis-MGD-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the complex I 75 kDa subunit family.Curated
Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
Contains 1 4Fe-4S Mo/W bis-MGD-type domain.PROSITE-ProRule annotation

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

« Hide

        10         20         30         40         50
MLRIPVRKAL VVLSKSPKGC VRTTATAASN LIEVFVDGQS VMVEPGTTVL
60 70 80 90 100
QACEKVGMQI PRFCYHERLS VAGNCRMCLV EIEKAPKVVA ACAMPVMKGW
110 120 130 140 150
NILTNSKKSK KAREGVMEFL LANHPLDCPI CDQGGECDLQ DQSMMFGNDR
160 170 180 190 200
SRFLEGKRAV EDKNIGPLVK TIMTRCIQCT RCIRFASEIA GVDDLGTTGR
210 220 230 240 250
GNDMQVGTYI EKMFMSELSG NIIDICPVGA LTSKPYAFTA RPWETRKTES
260 270 280 290 300
IDVMDAVGSN IVVSTRTGEV MRILPRMHED INEEWISDKT RFAYDGLKRQ
310 320 330 340 350
RLTEPMVRNE KGLLTYTSWE DALSRVAGML QTFQGKDVAA IAGGLVDAEA
360 370 380 390 400
LVALKDLLNR VDSDTLCTEE VFPTAGAGTD LRSNYLLNTT IAGVEEADVV
410 420 430 440 450
LLVGTNPRFE APLFNARLRK SWLHNDLKVA LIGSPVDLTY TYDHLGDSPK
460 470 480 490 500
ILQDIASGSH PFSQVLKEAK KPMVVLGSSA LQRNDGAAIL AAVSSIAQKI
510 520 530 540 550
RMTSGVTGDW KVMNILHRIA SQVAALDLGY KPGVEAIRKN PPKVLFLLGA
560 570 580 590 600
DGGCITRQDL PKDCFIIYQG HHGDVGAPIA DVILPGAAYT EKSATYVNTE
610 620 630 640 650
GRAQQTKVAV TPPGLAREDW KIIRALSEIA GMTLPYDTLD QVRNRLEEVS
660 670 680 690 700
PNLVRYDDIE GANYFQQANE LSKLVNQQLL ADPLVPPQLT IKDFYMTDSI
710 720
SRASQTMAKC VKAVTEGAQA VEEPSIC
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: October 1, 2014
This is version 60 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