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Protein

NADH dehydrogenase [ubiquinone] iron-sulfur protein 1, mitochondrial

Gene
N/A
Organism
Solanum tuberosum (Potato)
Status
Reviewed-Annotation score: 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

Protein has several cofactor binding sites:
  • [2Fe-2S] clusterBy similarityNote: Binds 1 [2Fe-2S] cluster per subunit.By similarity
  • [4Fe-4S] clusterBy similarityNote: Binds 2 [4Fe-4S] clusters per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi100 – 1001Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi111 – 1111Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi114 – 1141Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi128 – 1281Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi160 – 1601Iron-sulfur 2 (4Fe-4S); via pros nitrogenBy similarity
Metal bindingi164 – 1641Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi167 – 1671Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi173 – 1731Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi212 – 2121Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi215 – 2151Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi218 – 2181Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi262 – 2621Iron-sulfur 3 (4Fe-4S)By similarity

GO - Molecular functioni

GO - Biological processi

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 dehydrogenase [ubiquinone] iron-sulfur protein 1, mitochondrial (EC:1.6.5.3, EC:1.6.99.3)
Alternative name(s):
76 kDa mitochondrial complex I subunit
Complex I-76kD
Short name:
CI-76kD
NADH-ubiquinone oxidoreductase 76 kDa subunit
OrganismiSolanum tuberosum (Potato)
Taxonomic identifieri4113 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum
ProteomesiUP000011115 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2727MitochondrionBy similarityAdd
BLAST
Chaini28 – 738711NADH dehydrogenase [ubiquinone] iron-sulfur protein 1, mitochondrialPRO_0000019973Add
BLAST

Proteomic databases

PRIDEiQ43644.
ProMEXiQ43644.

Interactioni

Subunit structurei

Complex I is composed of about 45 different subunits. This is a component of the iron-sulfur (IP) fragment of the enzyme (By similarity).By similarity

Protein-protein interaction databases

IntActiQ43644. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ43644.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini66 – 144792Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST
Domaini281 – 337574Fe-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

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.
PF00111. Fer2. 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.

Q43644-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLGLLASRA LRSSRIIRNS TRTIVSTPEL KNADAAAAAA AADAPSDLPK
60 70 80 90 100
RHPVGGARVH LPNPEDVIEV FVDGYPVKIP KGMTVLQACE IAGVDIPRFC
110 120 130 140 150
YHSRLSIAGN CRMCLVEVEK SPKPVASCAM PALPGMKIKT DTPIAKKARE
160 170 180 190 200
GVMEFLLMNH PLDCPICDQG GECDLQDQSM AFGSDRGRFT EMKRSVVDKN
210 220 230 240 250
LGPLVKTVMT RCIQCTRCVR FASEVAGVED LGMLGRGSGE EIGTYVEKLM
260 270 280 290 300
TSELSGNVID ICPVGALTSK PFAFKARNWE LKGTESIDVT DAVGSNIRID
310 320 330 340 350
SRGPEVMRVV PRLNEDINEE WISDKTRFFY DGLKRQRLND PMIRGADGRF
360 370 380 390 400
QAVSWRDALA IVAEVMHQIK PEEIVGVAGK LSDAESMMAL KDLLNKMGSN
410 420 430 440 450
NIFCEGNGMH PNADLRSGYI MNTSISGLEK ADAFLLVGTQ PRVEAAMVNA
460 470 480 490 500
RIHKTVKATN AKVGYVGPAA DFNYDHEHLG TDPQTLVEIA EGRHPFSSAL
510 520 530 540 550
KNAKNPVIIV GAGVFDRDDK DAVFAAVDTI AKNNNVVRPD WNGLNVLLLN
560 570 580 590 600
AAQVAALDLG LVPESDKCIE SAKFVYLMGA DDVNLDKLPD DAFVVYQGHH
610 620 630 640 650
GDRGVYRANV ILPASAFTEK EGIYENTEGC AQITLPAVPT VGDARDDWKI
660 670 680 690 700
VRALSEVAGV GLPYDSLGAI RSRIKTVAPN LLEVDERQPA TFSTSLRPEV
710 720 730
SQKVSATPFT PAVENFYMTD AITRASKIMA QCSALLKK
Length:738
Mass (Da):79,970
Last modified:November 1, 1996 - v1
Checksum:i4AA955A62EEAD2E8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85808 mRNA. Translation: CAA59818.1.
PIRiS52737.
RefSeqiNP_001275317.1. NM_001288388.1.
UniGeneiStu.2837.

Genome annotation databases

GeneIDi102594243.
KEGGisot:102594243.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85808 mRNA. Translation: CAA59818.1.
PIRiS52737.
RefSeqiNP_001275317.1. NM_001288388.1.
UniGeneiStu.2837.

3D structure databases

ProteinModelPortaliQ43644.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ43644. 1 interaction.

Proteomic databases

PRIDEiQ43644.
ProMEXiQ43644.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi102594243.
KEGGisot:102594243.

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.
PF00111. Fer2. 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]
ProtoNetiSearch...

Publicationsi

  1. "Molecular characterisation of the 76 kDa iron-sulphur protein subunit of potato mitochondrial complex I."
    Rasmusson A.G., Heiser V., Irrgang K.D., Brennicke A., Grohmann L.
    Plant Cell Physiol. 39:373-381(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Desiree.
    Tissue: Leaf.

Entry informationi

Entry nameiNDUS1_SOLTU
AccessioniPrimary (citable) accession number: Q43644
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: May 27, 2015
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.