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P0CB67

- NDUS1_PONAB

UniProt

P0CB67 - NDUS1_PONAB

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Protein

NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial

Gene
NDUFS1
Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
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: UniProtKB-EC

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
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595: 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_0000019970Add
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

PRIDEiP0CB67.

Interactioni

Subunit structurei

Complex I is composed of 45 different subunits By similarity.

Structurei

3D structure databases

ProteinModelPortaliP0CB67.

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

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.

P0CB67-1 [UniParc]FASTAAdd to Basket

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MLRIPVRKAL VGLSKSPKGC VRTTATAASN LIEVFVDGQS VMVEPGTTVL    50
QACEKVGMQI PRFCYHERLS VAGNCRMCLV EIEKAPKVVA ACAMPVMKGW 100
NILTNSEKSK KAREGVMELL 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 QSFQGKDVAA IAGGLVDAEA 350
LVALKDLLNR VDSDTLCTEE VFPTAGAGTD LRSNYLLNTT IAGVEEADVV 400
LLVGTNPRFE APLFNARIRK SWLHNDLKVA LIGSPVDLTY TYDHLGDSPK 450
ILQDIASGSH PFSQVLKEAK KPMVVLGSSA LQRNDGAAIL AAFSSIAQKI 500
RMTSGVTGDW KVMNILHRIA SQVAALDLGY KPGVEAIRKN PPRLLFLLGA 550
DGGCITRQDL PKDCFIIYQG HHGDVGAPIA DVILPGAAYT EKSATYVNTE 600
GRAQQTKVAV TPPGLAREDW KIIRALSEIA GVTLPYDTLD QVRNRLEEVS 650
PNLVRYDDIE GANYFQQANE LSKLVNQQLL ADPLVPPQLT IKDFYMTDSI 700
SRASQTMAKC VKAVTEGAQA VEEPSIC 727
Length:727
Mass (Da):79,492
Last modified:November 24, 2009 - v1
Checksum:iF6B9C83DD7A8CC3C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR859585 mRNA. Translation: CAH91749.1.
RefSeqiNP_001126016.1. NM_001132544.1.

Genome annotation databases

GeneIDi100172962.
KEGGipon:100172962.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR859585 mRNA. Translation: CAH91749.1 .
RefSeqi NP_001126016.1. NM_001132544.1.

3D structure databases

ProteinModelPortali P0CB67.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P0CB67.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100172962.
KEGGi pon:100172962.

Organism-specific databases

CTDi 4719.

Phylogenomic databases

KOi K03934.

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. The German cDNA consortium
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Heart.

Entry informationi

Entry nameiNDUS1_PONAB
AccessioniPrimary (citable) accession number: P0CB67
Secondary accession number(s): Q0MQG0, Q5R911
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 24, 2009
Last sequence update: November 24, 2009
Last modified: February 19, 2014
This is version 28 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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